ID   AFP4_GADMO              Reviewed;         125 AA.
AC   Q56TU0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   22-SEP-2009, entry version 20.
DE   RecName: Full=Type-4 ice-structuring protein;
DE   AltName: Full=Antifreeze protein type IV;
DE   Flags: Precursor;
OS   Gadus morhua (Atlantic cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Gadus.
OX   NCBI_TaxID=8049;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Goetz F.W., Norberg B., Duman J.;
RT   "A cod antifreeze protein.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
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DR   EMBL; AY584595; AAT95404.1; -; mRNA.
DR   HOVERGEN; Q56TU0; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    125       Type-4 ice-structuring protein.
FT                                /FTId=PRO_0000042948.
SQ   SEQUENCE   125 AA;  13991 MW;  4ED7D330E8D66FF8 CRC64;
     MKYTLIAAIV VLALAQGTLA VEQSPELEKM AQFFEGMKTE LMATVQKVSE SLQSQTIIED
     GRTQLEPIMT QIQEHLAPLA TSVQEKVTPL AEDMQQKLKP YVDEFQSELE SVLRKLLDQA
     KAITQ
//
ID   AFP4_MYOOC              Reviewed;         128 AA.
AC   P80961; O73699;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   22-SEP-2009, entry version 44.
DE   RecName: Full=Type-4 ice-structuring protein LS-12;
DE            Short=ISP LS-12;
DE   AltName: Full=Antifreeze protein LS-12;
DE   Flags: Precursor;
OS   Myoxocephalus octodecimspinosis (Longhorn sculpin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes;
OC   Cottoidei; Cottidae; Myoxocephalus.
OX   NCBI_TaxID=68557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=98201665; PubMed=9540788; DOI=10.1016/S0167-4838(97)00197-0;
RA   Zhao Z., Deng G., Lui Q., Laursen R.A.;
RT   "Cloning and sequencing of cDNA encoding the LS-12 antifreeze protein
RT   in the longhorn sculpin, Myoxocephalus octodecimspinosis.";
RL   Biochim. Biophys. Acta 1382:177-180(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-128.
RC   TISSUE=Blood;
RX   MEDLINE=97165956; PubMed=9013849; DOI=10.1016/S0014-5793(96)01466-4;
RA   Deng G., Andrews D.W., Laursen R.A.;
RT   "Amino acid sequence of a new type of antifreeze protein, from the
RT   longhorn sculpin Myoxocephalus octodecimspinosis.";
RL   FEBS Lett. 402:17-20(1997).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
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DR   EMBL; AF026525; AAC27986.1; -; mRNA.
DR   PIR; A59010; A59010.
DR   HOVERGEN; P80961; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:InterPro.
DR   GO; GO:0042157; P:lipoprotein metabolic process; IEA:InterPro.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR000074; ApoA1_A4_E.
DR   Pfam; PF01442; Apolipoprotein; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing;
KW   Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL        1     20
FT   CHAIN        21    128       Type-4 ice-structuring protein LS-12.
FT                                /FTId=PRO_0000001698.
FT   MOD_RES      21     21       Pyrrolidone carboxylic acid.
SQ   SEQUENCE   128 AA;  14378 MW;  FC9688BD6E32F55D CRC64;
     MKFSLVATIV LLALAQGSFA QGAADLESLG QYFEEMKTKL IQDMTEIIRS QDLANQAQAF
     VEDKKTQLQP LVAQIQEQMK TVATNVEEQI RPLTANVQAH LQPQIDNFQK QMEAIIKKLT
     DQTMAIEN
//
ID   AFP4_PAROL              Reviewed;         124 AA.
AC   Q8JI37;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   22-SEP-2009, entry version 22.
DE   RecName: Full=Type-4 ice-structuring protein;
DE   AltName: Full=Antifreeze protein type IV;
DE   Flags: Precursor;
OS   Paralichthys olivaceus (Japanese flounder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Paralichthyidae; Paralichthys.
OX   NCBI_TaxID=8255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lee J., Song Y.;
RT   "Antifreeze protein gene of Japanese flounder similar to antifreeze
RT   protein type IV of Longhorn sculpin.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
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DR   EMBL; AF384676; AAM46175.1; -; Genomic_DNA.
DR   HOVERGEN; Q8JI37; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Antifreeze protein; Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    124       Type-4 ice-structuring protein.
FT                                /FTId=PRO_0000042949.
FT   MOD_RES      21     21       Pyrrolidone carboxylic acid (By
FT                                similarity).
SQ   SEQUENCE   124 AA;  13946 MW;  EA84868080E761F5 CRC64;
     MKFSLIAAVA LLALAQGSFA QDAADLEKIT QYFENLKNKM TEDVTAFLTN QDVANQAQTF
     MQERKTQLEP LATQIQEQLR AAATKFEEHI TPLAANVQPV VENFQQQMEA LVQKLMEKTR
     SISN
//
ID   ANP11_MACAM             Reviewed;          62 AA.
AC   P19613;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 52.
DE   RecName: Full=Ice-structuring protein SP2(HPLC 11);
DE            Short=ISP SP2(HPLC 11);
DE   AltName: Full=Antifreeze protein SP2(HPLC 11);
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; I31075; I31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19613; 1-62.
DR   HOVERGEN; P19613; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     62       Ice-structuring protein SP2(HPLC 11).
FT                                /FTId=PRO_0000155156.
FT   DOMAIN        1     60       AFP-like.
FT   SITE          6      6       Important for ice-binding (By
FT                                similarity).
FT   SITE         11     11       Important for ice-binding (By
FT                                similarity).
FT   SITE         15     15       Important for ice-binding (By
FT                                similarity).
FT   SITE         41     41       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   62 AA;  6585 MW;  3F8B94CDE6977E89 CRC64;
     SVVATQLIPI NTALTPAMME GKVTNPIGIP FAEMSQIVGK QVNRIVAKGQ TLMPNMVKTY
     AA
//
ID   ANP12_MACAM             Reviewed;          66 AA.
AC   P19614;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 64.
DE   RecName: Full=Type-3 ice-structuring protein HPLC 12;
DE   AltName: Full=ISP type III HPLC 12;
DE   AltName: Full=Antifreeze protein QAE(HPLC 12);
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=12050776;
RA   Clarke C.J., Buckley S.L., Lindner N.;
RT   "Ice structuring proteins - a new name for antifreeze proteins.";
RL   Cryo Lett. 23:89-92(2002).
RN   [3]
RP   STRUCTURE BY NMR.
RX   MEDLINE=97094988; PubMed=8939756; DOI=10.1016/S0969-2126(96)00140-2;
RA   Soennichsen F.D., Deluca C.I., Davies P.L., Sykes B.D.;
RT   "Refined solution structure of type III antifreeze protein:
RT   hydrophobic groups may be involved in the energetics of the protein-
RT   ice interaction.";
RL   Structure 4:1325-1337(1996).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS).
RX   MEDLINE=97078758; PubMed=8918883; DOI=10.1038/384285a0;
RA   Jia Z., Deluca C.I., Chao H., Davies P.L.;
RT   "Structural basis for the binding of a globular antifreeze protein to
RT   ice.";
RL   Nature 384:285-288(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF MUTANTS.
RX   MEDLINE=98139965; PubMed=9466928; DOI=10.1006/jmbi.1997.1482;
RA   Deluca C.I., Davies P.L., Ye Q., Jia Z.;
RT   "The effects of steric mutations on the structure of type III
RT   antifreeze protein and its interaction with ice.";
RL   J. Mol. Biol. 275:515-525(1998).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RA   Antson A.A., Lewis S., Roper D.I., Smith D.J., Hubbard R.E.;
RL   Submitted (OCT-1996) to the PDB data bank.
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
RX   MEDLINE=99223507; PubMed=10207002; DOI=10.1074/jbc.274.17.11842;
RA   Graether S.P., Deluca C.I., Baardsnes J., Hill G.A., Davies P.L.,
RA   Jia Z.;
RT   "Quantitative and qualitative analysis of type III antifreeze protein
RT   structure and function.";
RL   J. Biol. Chem. 274:11842-11847(1999).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; A30839; A30839.
DR   PDB; 1AME; X-ray; 1.65 A; A=1-63.
DR   PDB; 1B7I; X-ray; 1.65 A; A=1-63.
DR   PDB; 1B7J; X-ray; 1.65 A; A=1-63.
DR   PDB; 1B7K; X-ray; 2.50 A; A=1-63.
DR   PDB; 1EKL; X-ray; 1.65 A; A=1-63.
DR   PDB; 1GZI; X-ray; 1.80 A; A=1-63.
DR   PDB; 1HG7; X-ray; 1.15 A; A=1-63.
DR   PDB; 1JAB; X-ray; 1.65 A; A=1-63.
DR   PDB; 1KDE; NMR; -; A=1-63.
DR   PDB; 1KDF; NMR; -; A=1-63.
DR   PDB; 1MSI; X-ray; 1.25 A; A=2-63.
DR   PDB; 1MSJ; X-ray; 2.30 A; A=1-63.
DR   PDB; 2AME; X-ray; 2.00 A; A=1-63.
DR   PDB; 2JIA; X-ray; 1.60 A; A=1-63.
DR   PDB; 2MSI; X-ray; 1.90 A; A=2-63.
DR   PDB; 2MSJ; X-ray; 1.90 A; A=1-63.
DR   PDB; 2SPG; X-ray; 1.75 A; A=1-63.
DR   PDB; 3AME; X-ray; 2.30 A; A=1-63.
DR   PDB; 3MSI; X-ray; 1.43 A; A=2-63.
DR   PDB; 4AME; X-ray; 2.05 A; A=1-63.
DR   PDB; 4MSI; X-ray; 1.60 A; A=2-63.
DR   PDB; 5MSI; X-ray; 1.60 A; A=2-63.
DR   PDB; 6AME; X-ray; 2.10 A; A=1-63.
DR   PDB; 6MSI; X-ray; 1.65 A; A=2-63.
DR   PDB; 7AME; X-ray; 1.70 A; A=1-63.
DR   PDB; 7MSI; X-ray; 1.70 A; A=2-63.
DR   PDB; 8AME; X-ray; 1.90 A; A=1-63.
DR   PDB; 8MSI; X-ray; 2.60 A; A=1-63.
DR   PDB; 9AME; X-ray; 1.80 A; A=1-63.
DR   PDB; 9MSI; X-ray; 2.60 A; A=1-63.
DR   PDBsum; 1AME; -.
DR   PDBsum; 1B7I; -.
DR   PDBsum; 1B7J; -.
DR   PDBsum; 1B7K; -.
DR   PDBsum; 1EKL; -.
DR   PDBsum; 1GZI; -.
DR   PDBsum; 1HG7; -.
DR   PDBsum; 1JAB; -.
DR   PDBsum; 1KDE; -.
DR   PDBsum; 1KDF; -.
DR   PDBsum; 1MSI; -.
DR   PDBsum; 1MSJ; -.
DR   PDBsum; 2AME; -.
DR   PDBsum; 2JIA; -.
DR   PDBsum; 2MSI; -.
DR   PDBsum; 2MSJ; -.
DR   PDBsum; 2SPG; -.
DR   PDBsum; 3AME; -.
DR   PDBsum; 3MSI; -.
DR   PDBsum; 4AME; -.
DR   PDBsum; 4MSI; -.
DR   PDBsum; 5MSI; -.
DR   PDBsum; 6AME; -.
DR   PDBsum; 6MSI; -.
DR   PDBsum; 7AME; -.
DR   PDBsum; 7MSI; -.
DR   PDBsum; 8AME; -.
DR   PDBsum; 8MSI; -.
DR   PDBsum; 9AME; -.
DR   PDBsum; 9MSI; -.
DR   HOVERGEN; P19614; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     66       Type-3 ice-structuring protein HPLC 12.
FT                                /FTId=PRO_0000155160.
FT   DOMAIN        4     63       AFP-like.
FT   SITE          9      9       Important for ice-binding.
FT   SITE         14     14       Important for ice-binding.
FT   SITE         18     18       Important for ice-binding.
FT   SITE         44     44       Important for ice-binding.
FT   STRAND        4      9
FT   HELIX        19     21
FT   STRAND       22     25
FT   HELIX        34     36
FT   HELIX        37     40
FT   STRAND       44     47
FT   HELIX        57     59
SQ   SEQUENCE   66 AA;  7027 MW;  B6121A9902ED89F9 CRC64;
     NQASVVANQL IPINTALTLV MMRSEVVTPV GIPAEDIPRL VSMQVNRAVP LGTTLMPDMV
     KGYPPA
//
ID   ANP1_ANALU              Reviewed;          88 AA.
AC   P12416;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 55.
DE   RecName: Full=Type-3 ice-structuring protein 1.9;
DE   AltName: Full=ISP 3;
DE   AltName: Full=Antifreeze protein type III;
DE   Flags: Precursor;
OS   Anarhichas lupus (Atlantic wolffish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Anarhichadidae; Anarhichas.
OX   NCBI_TaxID=8204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89127205; PubMed=2851724;
RA   Scott G.K., Hayes P.H., Fletcher G.L., Davies P.L.;
RT   "Wolffish antifreeze protein genes are primarily organized as tandem
RT   repeats that each contain two genes in inverted orientation.";
RL   Mol. Cell. Biol. 8:3670-3675(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   EMBL; M22125; AAA74890.1; -; Genomic_DNA.
DR   PIR; A30238; A30238.
DR   HSSP; P19608; 1OPS.
DR   SMR; P12416; 23-86.
DR   HOVERGEN; P12416; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24     88       Type-3 ice-structuring protein 1.9.
FT                                /FTId=PRO_0000001696.
FT   DOMAIN       25     84       AFP-like.
FT   SITE         30     30       Important for ice-binding (By
FT                                similarity).
FT   SITE         35     35       Important for ice-binding (By
FT                                similarity).
FT   SITE         39     39       Important for ice-binding (By
FT                                similarity).
FT   SITE         65     65       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   88 AA;  9438 MW;  738EB9E62B3F347C CRC64;
     MKSAILTGLL FVLLCVDHLS SASQSVVATQ LIPINTALTP IMMKGQVVNP AGIPFAEMSQ
     IVGKQVNRPV AKDETLMPNM VKTYRAAK
//
ID   ANP1_LYCPO              Reviewed;          66 AA.
AC   P24028;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   22-SEP-2009, entry version 49.
DE   RecName: Full=Ice-structuring protein LP;
DE            Short=ISP LP;
DE   AltName: Full=Antifreeze protein LP;
OS   Lycodes polaris (Canadian eelpout).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Lycodinae; Lycodes.
OX   NCBI_TaxID=8197;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88000728; PubMed=3477289; DOI=10.1016/0167-4838(87)90021-5;
RA   Schrag J.D., Cheng C.-H.C., Panico M., Morris H.R., Devries A.L.;
RT   "Primary and secondary structure of antifreeze peptides from arctic
RT   and antarctic zoarcid fishes.";
RL   Biochim. Biophys. Acta 915:357-370(1987).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   PIR; S07150; FDFILC.
DR   HSSP; P19614; 9AME.
DR   SMR; P24028; 1-64.
DR   HOVERGEN; P24028; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     66       Ice-structuring protein LP.
FT                                /FTId=PRO_0000155154.
FT   DOMAIN        4     63       AFP-like.
FT   SITE          9      9       Important for ice-binding (By
FT                                similarity).
FT   SITE         14     14       Important for ice-binding (By
FT                                similarity).
FT   SITE         18     18       Important for ice-binding (By
FT                                similarity).
FT   SITE         44     44       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   66 AA;  6982 MW;  6F06E38A329767EC CRC64;
     NKASVVANQL IPINTALTLV MMRAEVVTPA GIPAEDIPRL VGLQVNRAVL IGTTLMPDMV
     KGYAPQ
//
ID   ANP1_MACAM              Reviewed;          64 AA.
AC   P19608;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 58.
DE   RecName: Full=Ice-structuring protein SP2(HPLC 1);
DE            Short=ISP SP2(HPLC 1);
DE   AltName: Full=Antifreeze protein SP2(HPLC 1);
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   PIR; D31075; D31075.
DR   PDB; 1OPS; X-ray; 2.00 A; A=1-64.
DR   PDBsum; 1OPS; -.
DR   HOVERGEN; P19608; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     64       Ice-structuring protein SP2(HPLC 1).
FT                                /FTId=PRO_0000155155.
FT   DOMAIN        3     62       AFP-like.
FT   SITE          8      8       Important for ice-binding (By
FT                                similarity).
FT   SITE         13     13       Important for ice-binding (By
FT                                similarity).
FT   SITE         17     17       Important for ice-binding (By
FT                                similarity).
FT   SITE         43     43       Important for ice-binding (By
FT                                similarity).
FT   STRAND        3      8
FT   HELIX        18     20
FT   STRAND       21     24
FT   HELIX        33     38
FT   TURN         39     41
FT   STRAND       43     46
FT   HELIX        56     58
FT   TURN         60     63
SQ   SEQUENCE   64 AA;  6775 MW;  DC6F90A2119FE0B0 CRC64;
     SQSVVATQLI PMNTALTPVM MEGKVTNPIG IPFAEMSQIV GKQVNTPVAK GQTIMPNMVK
     TYAA
//
ID   ANP1_PACBR              Reviewed;          63 AA.
AC   P12100;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 55.
DE   RecName: Full=Ice-structuring protein AB1;
DE            Short=ISP AB1;
DE   AltName: Full=Antifreeze peptide AB1;
OS   Pachycara brachycephalum (Antarctic eelpout) (Austrolycichthys
OS   brachycephalus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Lycodinae; Pachycara.
OX   NCBI_TaxID=36221;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=89323219; PubMed=2752054; DOI=10.1016/0167-4838(89)90135-0;
RA   Cheng C.-H.C., Devries A.L.;
RT   "Structures of antifreeze peptides from the antarctic eel pout,
RT   Austrolycicthys brachycephalus.";
RL   Biochim. Biophys. Acta 997:55-64(1989).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   PIR; S04973; S04973.
DR   HSSP; P35753; 1C8A.
DR   SMR; P12100; 2-63.
DR   HOVERGEN; P12100; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     63       Ice-structuring protein AB1.
FT                                /FTId=PRO_0000155149.
FT   DOMAIN        3     62       AFP-like.
FT   SITE          8      8       Important for ice-binding (By
FT                                similarity).
FT   SITE         13     13       Important for ice-binding (By
FT                                similarity).
FT   SITE         17     17       Important for ice-binding (By
FT                                similarity).
FT   SITE         43     43       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   63 AA;  6846 MW;  AC84FD14247193B4 CRC64;
     TKSVVASQLI PINTALTPAM MKAKEVSPKG IPAEEMSKIV GMQVNRAVNL DETLMPDMVK
     TYQ
//
ID   ANP1_RHIDE              Reviewed;          64 AA.
AC   P35751;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   22-SEP-2009, entry version 56.
DE   RecName: Full=Ice-structuring protein RD1;
DE            Short=ISP RD1;
DE   AltName: Full=Antifreeze peptide RD1;
OS   Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Lycodinae; Lycodichthys.
OX   NCBI_TaxID=8201;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=95210308; PubMed=7696304; DOI=10.1016/0167-4838(94)00205-U;
RA   Wang X., Devries A.L., Cheng C.-H.C.;
RT   "Antifreeze peptide heterogeneity in an antarctic eel pout includes an
RT   unusually large major variant comprised of two 7 kDa type III AFPs
RT   linked in tandem.";
RL   Biochim. Biophys. Acta 1247:163-172(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (0.62 ANGSTROMS).
RX   PubMed=12547803;
RA   Ko T.-P., Robinson H., Gao Y.-G., Cheng C.H.-C., DeVries A.L.,
RA   Wang A.H.-J.;
RT   "The refined crystal structure of an eel pout type III antifreeze
RT   protein RD1 at 0.62-A resolution reveals structuRAl microheterogeneity
RT   of protein and solvation.";
RL   Biophys. J. 84:1228-1237(2003).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   PIR; S53512; S53512.
DR   PDB; 1UCS; X-ray; 0.62 A; A=1-64.
DR   PDBsum; 1UCS; -.
DR   HOVERGEN; P35751; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     64       Ice-structuring protein RD1.
FT                                /FTId=PRO_0000155151.
FT   DOMAIN        4     63       AFP-like.
FT   SITE          9      9       Important for ice-binding (By
FT                                similarity).
FT   SITE         14     14       Important for ice-binding (By
FT                                similarity).
FT   SITE         18     18       Important for ice-binding (By
FT                                similarity).
FT   SITE         44     44       Important for ice-binding (By
FT                                similarity).
FT   STRAND        4      9
FT   HELIX        19     21
FT   STRAND       22     25
FT   HELIX        34     36
FT   HELIX        37     40
FT   STRAND       44     47
FT   HELIX        57     59
SQ   SEQUENCE   64 AA;  6906 MW;  154C6BE62D913192 CRC64;
     NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPKL VGMQVNRAVP LGTTLMPDMV
     KNYE
//
ID   ANP1C_MACAM             Reviewed;          87 AA.
AC   P07457; P19610;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   22-SEP-2009, entry version 64.
DE   RecName: Full=Ice-structuring protein SP1-C;
DE            Short=ISP SP1-C;
DE   AltName: Full=Antifreeze protein SP1-C;
DE   Flags: Precursor;
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86033715; PubMed=3840475;
RA   Li X.-M., Trinh K.-Y., Hew C.-L., Buettner B., Baenziger J.,
RA   Davies P.L.;
RT   "Structure of an antifreeze polypeptide and its precursor from the
RT   ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 260:12904-12909(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 23-86.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; M11790; AAA49347.1; -; mRNA.
DR   PIR; A24081; FDFICP.
DR   HSSP; P19608; 1OPS.
DR   SMR; P07457; 22-85.
DR   HOVERGEN; P07457; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing;
KW   Pyrrolidone carboxylic acid; Secreted; Signal.
FT   SIGNAL        1     22
FT   CHAIN        23     87       Ice-structuring protein SP1-C.
FT                                /FTId=PRO_0000001691.
FT   DOMAIN       24     83       AFP-like.
FT   SITE         29     29       Important for ice-binding (By
FT                                similarity).
FT   SITE         34     34       Important for ice-binding (By
FT                                similarity).
FT   SITE         38     38       Important for ice-binding (By
FT                                similarity).
FT   SITE         64     64       Important for ice-binding (By
FT                                similarity).
FT   MOD_RES      23     23       Pyrrolidone carboxylic acid.
SQ   SEQUENCE   87 AA;  9229 MW;  58D79961968D87B8 CRC64;
     MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPA MMEGKVTNPI GIPFAEMSQI
     VGKQVNTPVA KGQTLMPNMV KTYVAGK
//
ID   ANP2_ANALU              Reviewed;          88 AA.
AC   P12417;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 54.
DE   RecName: Full=Type-3 ice-structuring protein 1.5;
DE   AltName: Full=ISP 3;
DE   AltName: Full=Antifreeze protein type III;
DE   Flags: Precursor;
OS   Anarhichas lupus (Atlantic wolffish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Anarhichadidae; Anarhichas.
OX   NCBI_TaxID=8204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89127205; PubMed=2851724;
RA   Scott G.K., Hayes P.H., Fletcher G.L., Davies P.L.;
RT   "Wolffish antifreeze protein genes are primarily organized as tandem
RT   repeats that each contain two genes in inverted orientation.";
RL   Mol. Cell. Biol. 8:3670-3675(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; M22125; AAA74891.1; -; Genomic_DNA.
DR   HSSP; P19608; 1OPS.
DR   SMR; P12417; 23-86.
DR   HOVERGEN; P12417; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     23
FT   CHAIN        24     88       Type-3 ice-structuring protein 1.5.
FT                                /FTId=PRO_0000001697.
FT   DOMAIN       25     84       AFP-like.
FT   SITE         30     30       Important for ice-binding (By
FT                                similarity).
FT   SITE         35     35       Important for ice-binding (By
FT                                similarity).
FT   SITE         39     39       Important for ice-binding (By
FT                                similarity).
FT   SITE         65     65       Important for ice-binding (By
FT                                similarity).
FT   CONFLICT     24     24       Q -> QQ (in Ref. 1; AAA74891).
SQ   SEQUENCE   88 AA;  9430 MW;  72CAFCFA474E85CC CRC64;
     MKSAILTGLL FVLLCVDHMS SASQSVVATQ LIPINTALTP IMMKGQVVNP AGIPFAEMSQ
     IVGKQVNRAV AKDETLMPNM VKTYRAAK
//
ID   ANP2_PACBR              Reviewed;          63 AA.
AC   P12101;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 55.
DE   RecName: Full=Ice-structuring protein AB2;
DE            Short=ISP AB2;
DE   AltName: Full=Antifreeze peptide AB2;
OS   Pachycara brachycephalum (Antarctic eelpout) (Austrolycichthys
OS   brachycephalus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Lycodinae; Pachycara.
OX   NCBI_TaxID=36221;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=89323219; PubMed=2752054; DOI=10.1016/0167-4838(89)90135-0;
RA   Cheng C.-H.C., Devries A.L.;
RT   "Structures of antifreeze peptides from the antarctic eel pout,
RT   Austrolycicthys brachycephalus.";
RL   Biochim. Biophys. Acta 997:55-64(1989).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   PIR; S04974; S04974.
DR   HSSP; P35753; 1C8A.
DR   SMR; P12101; 2-63.
DR   HOVERGEN; P12101; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     63       Ice-structuring protein AB2.
FT                                /FTId=PRO_0000155150.
FT   DOMAIN        3     62       AFP-like.
FT   SITE          8      8       Important for ice-binding (By
FT                                similarity).
FT   SITE         13     13       Important for ice-binding (By
FT                                similarity).
FT   SITE         17     17       Important for ice-binding (By
FT                                similarity).
FT   SITE         43     43       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   63 AA;  7001 MW;  A1E7F954598DD061 CRC64;
     TKSVVANQLI PINTALTLVM MKAEEVSPKG IPAEEIPRLV GMQVNRAVYL DETLMPDMVK
     NYE
//
ID   ANP2_RHIDE              Reviewed;          64 AA.
AC   P12102; P35752;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 56.
DE   RecName: Full=Ice-structuring protein RD2;
DE            Short=ISP RD2;
DE   AltName: Full=Antifreeze peptide RD2;
OS   Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Lycodinae; Lycodichthys.
OX   NCBI_TaxID=8201;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=95210308; PubMed=7696304; DOI=10.1016/0167-4838(94)00205-U;
RA   Wang X., Devries A.L., Cheng C.-H.C.;
RT   "Antifreeze peptide heterogeneity in an antarctic eel pout includes an
RT   unusually large major variant comprised of two 7 kDa type III AFPs
RT   linked in tandem.";
RL   Biochim. Biophys. Acta 1247:163-172(1995).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88000728; PubMed=3477289; DOI=10.1016/0167-4838(87)90021-5;
RA   Schrag J.D., Cheng C.-H.C., Panico M., Morris H.R., Devries A.L.;
RT   "Primary and secondary structure of antifreeze peptides from arctic
RT   and antarctic zoarcid fishes.";
RL   Biochim. Biophys. Acta 915:357-370(1987).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; S08561; FDFIRE.
DR   HSSP; P35751; 1UCS.
DR   SMR; P12102; 1-64.
DR   HOVERGEN; P12102; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     64       Ice-structuring protein RD2.
FT                                /FTId=PRO_0000155152.
FT   DOMAIN        4     63       AFP-like.
FT   SITE          9      9       Important for ice-binding (By
FT                                similarity).
FT   SITE         14     14       Important for ice-binding (By
FT                                similarity).
FT   SITE         18     18       Important for ice-binding (By
FT                                similarity).
FT   SITE         44     44       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   64 AA;  6934 MW;  41EBAF6F2C812084 CRC64;
     NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEDIPRI IGMQVNRAVP LGTTLMPDMV
     KNYE
//
ID   ANP3_MACAM              Reviewed;          91 AA.
AC   P19606;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 58.
DE   RecName: Full=Ice-structuring protein lambda OP-3;
DE            Short=ISP lambda OP-3;
DE   AltName: Full=Antifreeze protein lambda OP-3;
DE   Flags: Precursor;
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   EMBL; J03923; AAA49348.1; -; Genomic_DNA.
DR   PIR; B30839; B30839.
DR   HSSP; P19614; 1HG7.
DR   SMR; P19606; 21-84.
DR   HOVERGEN; P19606; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23     91       Ice-structuring protein lambda OP-3.
FT                                /FTId=PRO_0000001694.
FT   DOMAIN       25     84       AFP-like.
FT   SITE         30     30       Important for ice-binding (By
FT                                similarity).
FT   SITE         35     35       Important for ice-binding (By
FT                                similarity).
FT   SITE         39     39       Important for ice-binding (By
FT                                similarity).
FT   SITE         65     65       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   91 AA;  9912 MW;  B85C9037F969F7CE CRC64;
     MKSVILTGLL FVLLCVDHMS SANQSVVATQ LIPINTALTL VMMTTRVIYP TGIPAEDIPR
     LVSMQVNQAV PMGTTLMPDM VKFYCLCAPK N
//
ID   ANP3_MYOSC              Reviewed;          33 AA.
AC   P04367;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   22-SEP-2009, entry version 52.
DE   RecName: Full=Ice-structuring protein SS-3;
DE            Short=ISP SS-3;
DE   AltName: Full=Antifreeze peptide SS-3;
OS   Myoxocephalus scorpius (Shorthorn sculpin) (Daddy sculpin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes;
OC   Cottoidei; Cottidae; Myoxocephalus.
OX   NCBI_TaxID=8097;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=85285003; PubMed=4029130;
RX   DOI=10.1111/j.1432-1033.1985.tb09081.x;
RA   Hew C.-L., Joshi S., Wang N.-C., Kao M.H., Ananthanarayanan V.S.;
RT   "Structures of shorthorn sculpin antifreeze polypeptides.";
RL   Eur. J. Biochem. 151:167-172(1985).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=96223980; PubMed=8626748; DOI=10.1074/jbc.271.8.4106;
RA   Gong Z., Ewart K.V., Hu Z., Fletcher G.L., Hew C.-L.;
RT   "Skin antifreeze protein genes of the winter flounder, Pleuronectes
RT   americanus, encode distinct and active polypeptides without the
RT   secretory signal and prosequences.";
RL   J. Biol. Chem. 271:4106-4112(1996).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=15697223; DOI=10.1021/bi047782j;
RA   Kwan A.H., Fairley K., Anderberg P.I., Liew C.W., Harding M.M.,
RA   Mackay J.P.;
RT   "Solution structure of a recombinant type I sculpin antifreeze
RT   protein.";
RL   Biochemistry 44:1980-1988(2005).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   PIR; A05162; A05162.
DR   PDB; 1Y03; NMR; -; A=1-33.
DR   PDB; 1Y04; NMR; -; A=1-33.
DR   PDBsum; 1Y03; -.
DR   PDBsum; 1Y04; -.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Direct protein sequencing; Repeat.
FT   CHAIN         1     33       Ice-structuring protein SS-3.
FT                                /FTId=PRO_0000155144.
FT   HELIX         3      8
FT   HELIX        10     31
SQ   SEQUENCE   33 AA;  2939 MW;  8B74CC4C06A1208A CRC64;
     MNAPARAAAK TAADALAAAK KTAADAAAAA AAA
//
ID   ANP3_PAGBO              Reviewed;          31 AA.
AC   P02732;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   22-SEP-2009, entry version 41.
DE   RecName: Full=Ice-structuring glycoprotein 3;
DE            Short=ISGP 3;
DE   AltName: Full=Antifreeze glycoprotein 3;
DE   Flags: Fragments;
OS   Pagothenia borchgrevinki (Bald rockcod) (Trematomus borchgrevinki).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes;
OC   Notothenioidei; Nototheniidae; Pagothenia.
OX   NCBI_TaxID=8213;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=71104882; PubMed=5542001;
RA   Devries A.L., Vandenheede J., Feeney R.E.;
RT   "Primary structure of freezing point-depressing glycoproteins.";
RL   J. Biol. Chem. 246:305-308(1971).
RN   [2]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=72056127; PubMed=5006918; DOI=10.1016/0006-291X(72)90633-X;
RA   Lin Y., Duman J.G., Devries A.L.;
RT   "Studies on the structure and activity of low molecular weight
RT   glycoproteins from an antarctic fish.";
RL   Biochem. Biophys. Res. Commun. 46:87-92(1972).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point. This
CC       fish lives in antarctic waters where it experiences water
CC       temperatures near -1.9 degrees Celsius. Its blood has a freezing
CC       point of about -2.0 degrees Celsius, and 30% of the freezing-point
CC       depression is due mainly to the 3 major high molecular weight
CC       glycoproteins in the plasma.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-linked glycans consist of Gal-GalNAc disaccharides. The
CC       three proteins may differ only in the number of repeating units of
CC       -Ala-Ala-Thr-.
CC   -!- MISCELLANEOUS: The two small glycopeptides are present in a much
CC       higher concentration (5 times by weight) than the HMW
CC       glycoproteins but produce only a small depression effect. The
CC       exact physiological role of the small glycopeptides is not known.
CC   -!- MISCELLANEOUS: The three major glycoproteins (3, 4, and 5) have
CC       the same N-terminal sequence, A-A-T-A-A-T, and C-terminal Ala.
CC       Each protein is composed only of Ala and Thr residues in a ratio
CC       of 2:1 and arranged in the repeating sequence -A-A-T-.
CC   -!- MISCELLANEOUS: The small glycopeptides 7 and 8 appear to contain
CC       20 and 14 residues, respectively, and to have the same N-terminal
CC       sequence and C-terminal residue as the 3 major proteins. However,
CC       each has 2 Pro residues (instead of 1 of the Ala in each of 2
CC       repeating units).
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DR   PIR; A03191; A03191.
DR   HOVERGEN; P02732; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Glycoprotein; Repeat;
KW   Secreted.
FT   CHAIN         1     31       Ice-structuring glycoprotein 3.
FT                                /FTId=PRO_0000155143.
FT   CARBOHYD      3      3       O-linked (GalNAc...).
FT   CARBOHYD      6      6       O-linked (GalNAc...).
FT   CARBOHYD      9      9       O-linked (GalNAc...).
FT   CARBOHYD     12     12       O-linked (GalNAc...).
FT   CARBOHYD     15     15       O-linked (GalNAc...).
FT   CARBOHYD     18     18       O-linked (GalNAc...).
FT   CARBOHYD     21     21       O-linked (GalNAc...).
FT   CARBOHYD     24     24       O-linked (GalNAc...).
FT   CARBOHYD     27     27       O-linked (GalNAc...).
FT   CARBOHYD     30     30       O-linked (GalNAc...).
FT   NON_CONS     30     31
SQ   SEQUENCE   31 AA;  2522 MW;  613109D78109D7D0 CRC64;
     AATAATAATA ATAATAATAA TAATAATAAT A
//
ID   ANP3_PSEAM              Reviewed;          37 AA.
AC   P02733;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   22-SEP-2009, entry version 41.
DE   RecName: Full=Ice-structuring protein 3;
DE            Short=ISP 3;
DE   AltName: Full=Antifreeze peptide 3;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes
OS   americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=78060969; PubMed=588591; DOI=10.1016/0005-2795(77)90395-6;
RA   Devries A.L., Lin Y.;
RT   "Structure of a peptide antifreeze and mechanism of adsorption to
RT   ice.";
RL   Biochim. Biophys. Acta 495:388-392(1977).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   PIR; A03192; FDFL3W.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
DR   GO; GO:0042309; P:homoiothermy; IEA:InterPro.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Repeat.
FT   CHAIN         1     37       Ice-structuring protein 3.
FT                                /FTId=PRO_0000155148.
SQ   SEQUENCE   37 AA;  3144 MW;  46AA951A962DECA9 CRC64;
     DTASDAAAAA ALTAABAAAA AKLTABBAAA AAAATAA
//
ID   ANP3_RHIDE              Reviewed;         134 AA.
AC   P35753;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   22-SEP-2009, entry version 59.
DE   RecName: Full=Ice-structuring protein RD3;
DE            Short=ISP RD3;
DE   AltName: Full=Antifreeze peptide RD3;
OS   Rhigophila dearborni (Antarctic eelpout) (Lycodichthys dearborni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Lycodinae; Lycodichthys.
OX   NCBI_TaxID=8201;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=95210308; PubMed=7696304; DOI=10.1016/0167-4838(94)00205-U;
RA   Wang X., Devries A.L., Cheng C.-H.C.;
RT   "Antifreeze peptide heterogeneity in an antarctic eel pout includes an
RT   unusually large major variant comprised of two 7 kDa type III AFPs
RT   linked in tandem.";
RL   Biochim. Biophys. Acta 1247:163-172(1995).
RN   [2]
RP   STRUCTURE BY NMR OF 1-73.
RX   MEDLINE=99353969; PubMed=10423534;
RA   Miura K., Ohgiya S., Hoshino T., Nemoto N., Odaira M., Nitta K.,
RA   Tsuda S.;
RT   "Determination of the solution structure of the N-domain plus linker
RT   of antarctic eel pout antifreeze protein RD3.";
RL   J. Biochem. 126:387-394(1999).
RN   [3]
RP   STRUCTURE BY NMR.
RX   PubMed=11010977; DOI=10.1074/jbc.M007902200;
RA   Miura K., Ohgiya S., Hoshino T., Nemoto N., Suetake T., Miura A.,
RA   Spyracopoulos L., Kondo H., Tsuda S.;
RT   "NMR analysis of type III antifreeze protein intramolecular dimer.
RT   Structural basis for enhanced activity.";
RL   J. Biol. Chem. 276:1304-1310(2001).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 2 AFP-like domains.
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DR   PIR; S53514; S53514.
DR   PDB; 1C89; NMR; -; A=1-134.
DR   PDB; 1C8A; NMR; -; A=1-134.
DR   PDB; 3NLA; NMR; -; A=1-73.
DR   PDB; 3RDN; NMR; -; A=1-73.
DR   PDBsum; 1C89; -.
DR   PDBsum; 1C8A; -.
DR   PDBsum; 3NLA; -.
DR   PDBsum; 3RDN; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 2.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 2.
DR   PROSITE; PS50844; AFP_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Direct protein sequencing; Repeat;
KW   Secreted.
FT   CHAIN         1    134       Ice-structuring protein RD3.
FT                                /FTId=PRO_0000155153.
FT   DOMAIN        4     63       AFP-like 1.
FT   DOMAIN       74    133       AFP-like 2.
FT   REGION       65     70       Linker.
FT   SITE          9      9       Important for ice-binding (By
FT                                similarity).
FT   SITE         14     14       Important for ice-binding (By
FT                                similarity).
FT   SITE         18     18       Important for ice-binding (By
FT                                similarity).
FT   SITE         44     44       Important for ice-binding (By
FT                                similarity).
FT   SITE         79     79       Important for ice-binding (By
FT                                similarity).
FT   SITE         84     84       Important for ice-binding (By
FT                                similarity).
FT   SITE         88     88       Important for ice-binding (By
FT                                similarity).
FT   SITE        114    114       Important for ice-binding (By
FT                                similarity).
FT   STRAND        4      9
FT   TURN         19     21
FT   STRAND       22     25
FT   STRAND       32     34
FT   HELIX        37     40
FT   TURN         57     59
FT   STRAND       71     79
FT   TURN         89     91
FT   STRAND       93     96
FT   STRAND      103    106
FT   HELIX       107    110
FT   STRAND      121    124
FT   TURN        127    129
SQ   SEQUENCE   134 AA;  14480 MW;  F7F208BF3E2CAA54 CRC64;
     NKASVVANQL IPINTALTLI MMKAEVVTPM GIPAEEIPNL VGMQVNRAVP LGTTLMPDMV
     KNYEDGTTSP GLKSVVANQL IPINTALTLV MMKAEEVSPK GIPSEEISKL VGMQVNRAVY
     LDQTLMPDMV KNYE
//
ID   ANP4_MACAM              Reviewed;          63 AA.
AC   P19609;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 52.
DE   RecName: Full=Ice-structuring protein SP1(HPLC 4);
DE            Short=ISP SP1(HPLC 4);
DE   AltName: Full=Antifreeze protein SP1(HPLC 4);
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; E31075; E31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19609; 1-63.
DR   HOVERGEN; P19609; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     63       Ice-structuring protein SP1(HPLC 4).
FT                                /FTId=PRO_0000155157.
FT   DOMAIN        2     61       AFP-like.
FT   SITE          7      7       Important for ice-binding (By
FT                                similarity).
FT   SITE         12     12       Important for ice-binding (By
FT                                similarity).
FT   SITE         16     16       Important for ice-binding (By
FT                                similarity).
FT   SITE         42     42       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   63 AA;  6642 MW;  3FEFE507C6972FD8 CRC64;
     QSVVATQLIP INTALTPAMM EGKVTNPIGI PFAEMSQIVG KQVNTPVAKG QTIMPNMVKT
     YAA
//
ID   ANP4_PSEAM              Reviewed;          85 AA.
AC   P02734;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   22-SEP-2009, entry version 47.
DE   RecName: Full=Ice-structuring protein 4;
DE            Short=ISP 4;
DE   AltName: Full=Antifreeze peptide 4;
DE   Flags: Precursor;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes
OS   americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=81247379; PubMed=6265915; DOI=10.1073/pnas.78.5.2825;
RA   Lin Y., Gross J.K.;
RT   "Molecular cloning and characterization of winter flounder antifreeze
RT   cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 78:2825-2829(1981).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   EMBL; J00930; AAA49467.1; -; mRNA.
DR   PIR; A03193; FDFL4W.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
DR   GO; GO:0042309; P:homoiothermy; IEA:InterPro.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   3: Inferred from homology;
KW   Antifreeze protein; Repeat; Secreted; Signal.
FT   SIGNAL        1     21
FT   CHAIN        22     85       Ice-structuring protein 4.
FT                                /FTId=PRO_0000001684.
SQ   SEQUENCE   85 AA;  7215 MW;  8E62E1D2B44117BC CRC64;
     MRITEANPDP DAKAVPAAAA PSTASDAAAA AAATAATAAA AAAATAATAA AAAAATAATA
     AKAAALTAAN AAAAAAATAA AAARG
//
ID   ANP5_MACAM              Reviewed;          87 AA.
AC   P19607;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 56.
DE   RecName: Full=Ice-structuring protein lambda OP-5;
DE            Short=ISP lambda OP-5;
DE   AltName: Full=Antifreeze protein lambda OP-5;
DE   Flags: Precursor;
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   EMBL; J03924; AAA49346.1; -; Genomic_DNA.
DR   PIR; C31075; C31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19607; 22-85.
DR   HOVERGEN; P19607; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     21       By similarity.
FT   CHAIN        22     87       Ice-structuring protein lambda OP-5.
FT                                /FTId=PRO_0000001695.
FT   DOMAIN       24     83       AFP-like.
FT   SITE         29     29       Important for ice-binding (By
FT                                similarity).
FT   SITE         34     34       Important for ice-binding (By
FT                                similarity).
FT   SITE         38     38       Important for ice-binding (By
FT                                similarity).
FT   SITE         64     64       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   87 AA;  9229 MW;  B5615B2E868D87AB CRC64;
     MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPV MMEGKVTNPI GIPFAEMSQI
     VGKQVNTPVA KGQTLMPNMV KTYAAGK
//
ID   ANP5_MYOAE              Reviewed;          33 AA.
AC   P20421;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 35.
DE   RecName: Full=Ice-structuring protein GS-5;
DE            Short=ISP GS-5;
DE   AltName: Full=Antifreeze peptide GS-5;
OS   Myoxocephalus aenaeus (Grubby sculpin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes;
OC   Cottoidei; Cottidae; Myoxocephalus.
OX   NCBI_TaxID=8096;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Chakrabartty A., Hew C.-L., Shears M., Fletcher G.;
RT   "Primary structures of the alanine-rich antifreeze polypeptides from
RT   grubby sculpin, Myoxocephalus aenaeus.";
RL   Can. J. Zool. 66:403-408(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   PIR; S06417; FDFI5G.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Repeat.
FT   CHAIN         1     33       Ice-structuring protein GS-5.
FT                                /FTId=PRO_0000155146.
FT   MOD_RES       1      1       Blocked amino end (Met).
SQ   SEQUENCE   33 AA;  2980 MW;  7F2ACC56B70A2080 CRC64;
     MDAPAIAAAK TAADALAAAK KTAADAAAAA AKP
//
ID   ANP7_ELEGR              Reviewed;          19 AA.
AC   P11920;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 33.
DE   RecName: Full=Ice-structuring glycoprotein 7R;
DE            Short=ISGP 7R;
DE   AltName: Full=Antifreeze glycoprotein 7R;
OS   Eleginus gracilis (Saffron cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Eleginus.
OX   NCBI_TaxID=8047;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=86196057; PubMed=3700395;
RA   Burcham T.S., Osuga D.T., Rao B.N.N., Bush C.A., Feeney R.E.;
RT   "Purification and primary sequences of the major arginine-containing
RT   antifreeze glycopeptides from the fish Eleginus gracilis.";
RL   J. Biol. Chem. 261:6384-6389(1986).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-glycosylated; contains disaccharide galactose-N-
CC       acetylgalactosamine attached to threonines (By similarity).
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DR   PIR; B25213; B25213.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted.
FT   PEPTIDE       1     19       Ice-structuring glycoprotein 7R.
FT                                /FTId=PRO_0000155141.
SQ   SEQUENCE   19 AA;  1656 MW;  E290F8FEF1FD9324 CRC64;
     AATAATPATA ATPATAARA
//
ID   ANP7_MACAM              Reviewed;          64 AA.
AC   P19611;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 52.
DE   RecName: Full=Ice-structuring protein SP4(HPLC 7);
DE            Short=ISP SP4(HPLC 7);
DE   AltName: Full=Antifreeze protein SP4(HPLC 7);
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; G31075; G31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19611; 1-64.
DR   HOVERGEN; P19611; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     64       Ice-structuring protein SP4(HPLC 7).
FT                                /FTId=PRO_0000155158.
FT   DOMAIN        3     62       AFP-like.
FT   SITE          8      8       Important for ice-binding (By
FT                                similarity).
FT   SITE         13     13       Important for ice-binding (By
FT                                similarity).
FT   SITE         17     17       Important for ice-binding (By
FT                                similarity).
FT   SITE         43     43       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   64 AA;  6846 MW;  FD2E27DB328C423A CRC64;
     SQSVVATRLI PMNTALTPAM MEGKVTNPIG IPFAEMSQIV GKQVNRIVAK GQTLMPNMVK
     TYAA
//
ID   ANP8_ELEGR              Reviewed;          16 AA.
AC   P11921;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   22-SEP-2009, entry version 33.
DE   RecName: Full=Ice-structuring glycoprotein 8R;
DE            Short=ISGP 8R;
DE   AltName: Full=Antifreeze glycoprotein 8R;
OS   Eleginus gracilis (Saffron cod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Paracanthopterygii; Gadiformes; Gadidae; Eleginus.
OX   NCBI_TaxID=8047;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=86196057; PubMed=3700395;
RA   Burcham T.S., Osuga D.T., Rao B.N.N., Bush C.A., Feeney R.E.;
RT   "Purification and primary sequences of the major arginine-containing
RT   antifreeze glycopeptides from the fish Eleginus gracilis.";
RL   J. Biol. Chem. 261:6384-6389(1986).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O-glycosylated; contains disaccharide galactose-N-
CC       acetylgalactosamine attached to threonines (By similarity).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   PIR; A25213; A25213.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted.
FT   PEPTIDE       1     16       Ice-structuring glycoprotein 8R.
FT                                /FTId=PRO_0000155142.
SQ   SEQUENCE   16 AA;  1413 MW;  8EF45D9324E88994 CRC64;
     AATAATPATA ATPARA
//
ID   ANP8_MYOAE              Reviewed;          40 AA.
AC   P20617;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 35.
DE   RecName: Full=Ice-structuring protein GS-8;
DE            Short=ISP GS-8;
DE   AltName: Full=Antifreeze peptide GS-8;
OS   Myoxocephalus aenaeus (Grubby sculpin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes;
OC   Cottoidei; Cottidae; Myoxocephalus.
OX   NCBI_TaxID=8096;
RN   [1]
RP   PROTEIN SEQUENCE.
RA   Chakrabartty A., Hew C.-L., Shears M., Fletcher G.;
RT   "Primary structures of the alanine-rich antifreeze polypeptides from
RT   grubby sculpin, Myoxocephalus aenaeus.";
RL   Can. J. Zool. 66:403-408(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   PIR; S07046; FDFI8G.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Repeat.
FT   CHAIN         1     40       Ice-structuring protein GS-8.
FT                                /FTId=PRO_0000155147.
FT   MOD_RES       1      1       Blocked amino end (Met).
SQ   SEQUENCE   40 AA;  3579 MW;  32F50EE243C2AD11 CRC64;
     MDGETPAQKA ARLAAAAAAL AAKTAADAAA KAAAIAAAAA
//
ID   ANP8_MYOSC              Reviewed;          45 AA.
AC   P04368;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   22-SEP-2009, entry version 42.
DE   RecName: Full=Ice-structuring protein SS-8;
DE            Short=ISP SS-8;
DE   AltName: Full=Antifreeze peptide SS-8;
OS   Myoxocephalus scorpius (Shorthorn sculpin) (Daddy sculpin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes;
OC   Cottoidei; Cottidae; Myoxocephalus.
OX   NCBI_TaxID=8097;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=85285003; PubMed=4029130;
RX   DOI=10.1111/j.1432-1033.1985.tb09081.x;
RA   Hew C.-L., Joshi S., Wang N.-C., Kao M.H., Ananthanarayanan V.S.;
RT   "Structures of shorthorn sculpin antifreeze polypeptides.";
RL   Eur. J. Biochem. 151:167-172(1985).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   PIR; A05163; A05163.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Repeat.
FT   CHAIN         1     45       Ice-structuring protein SS-8.
FT                                /FTId=PRO_0000155145.
FT   REPEAT        9     21
FT   REPEAT       22     33
FT   REPEAT       34     45
FT   MOD_RES       1      1       Blocked amino end (Met).
SQ   SEQUENCE   45 AA;  4007 MW;  260C0BCC663B6878 CRC64;
     MNGETPAQKA ARLAAAAALA AKTAADAAAK AAAKAAAIAA AAASA
//
ID   ANP9_MACAM              Reviewed;          64 AA.
AC   P19612;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 52.
DE   RecName: Full=Ice-structuring protein SP3(HPLC 9);
DE            Short=ISP SP3(HPLC 9);
DE   AltName: Full=Antifreeze protein SP3(HPLC 9);
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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CC   -----------------------------------------------------------------------
DR   PIR; H31075; H31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19612; 1-64.
DR   HOVERGEN; P19612; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Secreted.
FT   CHAIN         1     64       Ice-structuring protein SP3(HPLC 9).
FT                                /FTId=PRO_0000155159.
FT   DOMAIN        3     62       AFP-like.
FT   SITE          8      8       Important for ice-binding (By
FT                                similarity).
FT   SITE         13     13       Important for ice-binding (By
FT                                similarity).
FT   SITE         17     17       Important for ice-binding (By
FT                                similarity).
FT   SITE         43     43       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   64 AA;  6818 MW;  FE2D27D8318C423A CRC64;
     SQSVVATQLI PMNTALTPAM MEGKVTNPIG IPFAEMSQIV GKQVNRIVAK GQTLMPNMVK
     TYAA
//
ID   ANP_LIMFE               Reviewed;          97 AA.
AC   P09031;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   22-SEP-2009, entry version 44.
DE   RecName: Full=Ice-structuring protein;
DE            Short=ISP;
DE   AltName: Full=Antifreeze protein;
DE            Short=AFP;
DE   Flags: Precursor;
OS   Limanda ferruginea (Yellowtail flounder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Limanda.
OX   NCBI_TaxID=8258;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88029483; PubMed=3665937;
RX   DOI=10.1111/j.1432-1033.1987.tb13462.x;
RA   Scott G.K., Davies P.L., Shears M.A., Fletcher G.L.;
RT   "Structural variations in the alanine-rich antifreeze proteins of the
RT   pleuronectinae.";
RL   Eur. J. Biochem. 168:629-633(1987).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   EMBL; X06356; CAA29655.1; -; mRNA.
DR   PIR; S02376; S02376.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
DR   GO; GO:0042309; P:homoiothermy; IEA:InterPro.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   3: Inferred from homology;
KW   Antifreeze protein; Repeat; Secreted; Signal.
FT   SIGNAL        1     23
FT   PROPEP       24     48       Removed by a dipeptidylpeptidase
FT                                (Probable).
FT                                /FTId=PRO_0000001682.
FT   CHAIN        49     97       Ice-structuring protein.
FT                                /FTId=PRO_0000001683.
SQ   SEQUENCE   97 AA;  8865 MW;  62AD582DF8E459B6 CRC64;
     MALSLFTVGQ LIFLFWTLRI TEANPDPAAK AAPAAVADPA AAAAAAVADT ASDAAAAAAA
     TAAAAAKAAA DTAAAAAKAA ADTAAAAAEA AAATARG
//
ID   ANP_NOTCO               Reviewed;         790 AA.
AC   P24856;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   22-SEP-2009, entry version 58.
DE   RecName: Full=Ice-structuring glycoprotein;
DE            Short=ISGP;
DE   AltName: Full=Antifreeze glycopeptide polyprotein;
DE            Short=AFGP polyprotein;
DE   Contains:
DE     RecName: Full=AFGP7;
DE     AltName: Full=AFGP 7;
DE   Contains:
DE     RecName: Full=AFGP8;
DE     AltName: Full=AFGP 8;
DE   Contains:
DE     RecName: Full=AFGP8-like;
DE   Flags: Precursor; Fragment;
GN   Name=afgp8;
OS   Notothenia coriiceps neglecta (Black rockcod) (Yellowbelly rockcod).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes;
OC   Notothenioidei; Nototheniidae; Notothenia.
OX   NCBI_TaxID=8209;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Testis;
RX   MEDLINE=91067687; PubMed=2251271; DOI=10.1073/pnas.87.23.9265;
RA   Hsiao K.-C., Cheng C.-H.C., Fernandes I.E., Detrich H.W. III,
RA   Devries A.L.;
RT   "An antifreeze glycopeptide gene from the antarctic cod Notothenia
RT   coriiceps neglecta encodes a polyprotein of high peptide copy
RT   number.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9265-9269(1990).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS AND 457.
RA   Cheng C.-H.C.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Synthesized by the liver and secreted into the
CC       blood from which they become distributed to almost the entire
CC       extracellular space.
CC   -!- DOMAIN: Contains 44 copies of AFGP8 and two copies of AFGP7.
CC   -!- PTM: O-glycosylated; contains disaccharide galactose-N-
CC       acetylgalactosamine attached to threonines in AFGP8 and AFGP7.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Cool news - Issue 5 of
CC       December 2000;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt005.shtml";
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DR   EMBL; M55000; AAA49392.2; -; Genomic_DNA.
DR   PIR; A38420; A38420.
DR   HOVERGEN; P24856; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Glycoprotein; Repeat;
KW   Secreted.
FT   PROPEP       <1      5
FT                                /FTId=PRO_0000001634.
FT   CHAIN         6    790       Ice-structuring glycoprotein.
FT                                /FTId=PRO_0000001635.
FT   PEPTIDE       6     19       AFGP8.
FT                                /FTId=PRO_0000001636.
FT   PEPTIDE      23     36       AFGP8.
FT                                /FTId=PRO_0000001637.
FT   PEPTIDE      40     53       AFGP8.
FT                                /FTId=PRO_0000001638.
FT   PEPTIDE      57     70       AFGP8.
FT                                /FTId=PRO_0000001639.
FT   PEPTIDE      74     87       AFGP8.
FT                                /FTId=PRO_0000001640.
FT   PEPTIDE      91    104       AFGP8.
FT                                /FTId=PRO_0000001641.
FT   PEPTIDE     108    121       AFGP8.
FT                                /FTId=PRO_0000001642.
FT   PEPTIDE     125    138       AFGP8.
FT                                /FTId=PRO_0000001643.
FT   PEPTIDE     142    155       AFGP8.
FT                                /FTId=PRO_0000001644.
FT   PEPTIDE     159    172       AFGP8.
FT                                /FTId=PRO_0000001645.
FT   PEPTIDE     176    189       AFGP8.
FT                                /FTId=PRO_0000001646.
FT   PEPTIDE     193    206       AFGP8.
FT                                /FTId=PRO_0000001647.
FT   PEPTIDE     210    223       AFGP8.
FT                                /FTId=PRO_0000001648.
FT   PEPTIDE     227    240       AFGP8.
FT                                /FTId=PRO_0000001649.
FT   PEPTIDE     244    257       AFGP8.
FT                                /FTId=PRO_0000001650.
FT   PEPTIDE     261    274       AFGP8.
FT                                /FTId=PRO_0000001651.
FT   PEPTIDE     278    291       AFGP8.
FT                                /FTId=PRO_0000001652.
FT   PEPTIDE     295    308       AFGP8.
FT                                /FTId=PRO_0000001653.
FT   PEPTIDE     312    325       AFGP8.
FT                                /FTId=PRO_0000001654.
FT   PEPTIDE     329    342       AFGP8.
FT                                /FTId=PRO_0000001655.
FT   PEPTIDE     346    359       AFGP8.
FT                                /FTId=PRO_0000001656.
FT   PEPTIDE     363    376       AFGP8.
FT                                /FTId=PRO_0000001657.
FT   PEPTIDE     380    393       AFGP8.
FT                                /FTId=PRO_0000001658.
FT   PEPTIDE     397    410       AFGP8.
FT                                /FTId=PRO_0000001659.
FT   PEPTIDE     414    427       AFGP8.
FT                                /FTId=PRO_0000001660.
FT   PEPTIDE     431    444       AFGP8.
FT                                /FTId=PRO_0000001661.
FT   PEPTIDE     448    461       AFGP8.
FT                                /FTId=PRO_0000001662.
FT   PEPTIDE     465    478       AFGP8.
FT                                /FTId=PRO_0000001663.
FT   PEPTIDE     482    495       AFGP8.
FT                                /FTId=PRO_0000001664.
FT   PEPTIDE     499    512       AFGP8.
FT                                /FTId=PRO_0000001665.
FT   PEPTIDE     516    529       AFGP8.
FT                                /FTId=PRO_0000001666.
FT   PEPTIDE     533    546       AFGP8.
FT                                /FTId=PRO_0000001667.
FT   PEPTIDE     550    563       AFGP8.
FT                                /FTId=PRO_0000001668.
FT   PEPTIDE     567    580       AFGP8.
FT                                /FTId=PRO_0000001669.
FT   PEPTIDE     584    597       AFGP8.
FT                                /FTId=PRO_0000001670.
FT   PEPTIDE     601    614       AFGP8.
FT                                /FTId=PRO_0000001671.
FT   PEPTIDE     618    631       AFGP8.
FT                                /FTId=PRO_0000001672.
FT   PEPTIDE     635    648       AFGP8.
FT                                /FTId=PRO_0000001673.
FT   PEPTIDE     652    665       AFGP8.
FT                                /FTId=PRO_0000001674.
FT   PEPTIDE     669    682       AFGP8.
FT                                /FTId=PRO_0000001675.
FT   PEPTIDE     686    699       AFGP8.
FT                                /FTId=PRO_0000001676.
FT   PEPTIDE     703    716       AFGP8.
FT                                /FTId=PRO_0000001677.
FT   PEPTIDE     720    736       AFGP7.
FT                                /FTId=PRO_0000001678.
FT   PEPTIDE     740    756       AFGP7.
FT                                /FTId=PRO_0000001679.
FT   PEPTIDE     760    773       AFGP8.
FT                                /FTId=PRO_0000001680.
FT   PEPTIDE     777    790       AFGP8-like.
FT                                /FTId=PRO_0000001681.
FT   NON_TER       1      1
SQ   SEQUENCE   790 AA;  71267 MW;  4C7CCCADC48FE902 CRC64;
     VTAAPAATAA TAATPATAAL NFAATAATPA TPATPALIFA ATAATAATPA TAALNFAATA
     ATPATAATPA LIFAAAAATA ATPATAALNF AATAATPATA ATPALIFAAT AATAATPATP
     AFHFAATAAT PATAATPALI FAATAATAAT PATPAFHFAA TAATPATAAT PALIFAATAA
     TAATPATAAL NFAATAATPA TAATPALIFA ATAATAATPA TAALNFAATA ATAATPATAA
     CNFAATAATP ATAATPALIF AATAATAATP ATAACNFAAT AATPATAATP ALIFAATAAT
     AATPATAALN FAATAATPAT AATPALIFAA TAATAATPAT AALNFAATAA TPATAATPAL
     IFAATAATAA TPATAALNFA ATAATAATPA TPAFNFAATA ATPATAATPA LIFAATAATA
     ATPATAALNF AATAATPATA ATPALIFAAT AATAATPATA ALHFAATAAT AATPATAALN
     FAATAATPAT AATPALIFAA TAATAATPAT AAFNFAATAA TAATPATAAL NFAATAATPA
     TAATPALIFA ATAATAATPA TAALNFAATA ATPATAATPA LIFAATAATA ATPATPAFHF
     AATAATPATA ATPALIFAAT AATAATPATA ALNFAATAAT AATPATAALN FAATAATPAT
     AATPALIFAA TAATAATPAT AALNFAATAA TPATAATPAL IFAATAATAA TPATAAFNFA
     ATAATAATPA TAATPALIFA ATAATAATPA TPATPALIFA ATAATAATPA TPALNFAATA
     ATAATTAARG
//
ID   ANPA_PSEAM              Reviewed;          82 AA.
AC   P04002; Q7SIC4;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-1986, sequence version 1.
DT   28-JUL-2009, entry version 67.
DE   RecName: Full=Ice-structuring protein A;
DE            Short=ISP A;
DE   AltName: Full=Antifreeze protein A;
DE   AltName: Full=HPLC6;
DE   Flags: Precursor;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes
OS   americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-70.
RX   MEDLINE=82197490; PubMed=6952188; DOI=10.1073/pnas.79.2.335;
RA   Davies P.L., Roach A.H., Hew C.-L.;
RT   "DNA sequence coding for an antifreeze protein precursor from winter
RT   flounder.";
RL   Proc. Natl. Acad. Sci. U.S.A. 79:335-339(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84264559; PubMed=6086629;
RA   Davies P.L., Hough C., Scott G.K., Ng N.F.L., White B.N., Hew C.-L.;
RT   "Antifreeze protein genes of the winter flounder.";
RL   J. Biol. Chem. 259:9241-9247(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88259236; PubMed=3133486; DOI=10.1007/BF02099727;
RA   Scott G.K., Davies P.L., Kao M.H., Fletcher G.L.;
RT   "Differential amplification of antifreeze protein genes in the
RT   pleuronectinae.";
RL   J. Mol. Evol. 27:29-35(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT VAL-36.
RC   TISSUE=Testis;
RX   MEDLINE=92209995; PubMed=1555765; DOI=10.1016/0378-1119(92)90372-V;
RA   Davies P.L.;
RT   "Conservation of antifreeze protein-encoding genes in tandem
RT   repeats.";
RL   Gene 112:163-170(1992).
RN   [5]
RP   PROTEIN SEQUENCE OF 24-28, AND AMIDATION.
RC   TISSUE=Liver;
RX   PubMed=3769927; DOI=10.1111/j.1432-1033.1986.tb09966.x;
RA   Hew C.-L., Wang N.-C., Yan S., Cai H., Sclater A., Fletcher G.L.;
RT   "Biosynthesis of antifreeze polypeptides in the winter flounder.
RT   Characterization and seasonal occurrence of precursor polypeptides.";
RL   Eur. J. Biochem. 160:267-272(1986).
RN   [6]
RP   3D-STRUCTURE MODELING OF 45-81.
RX   MEDLINE=92148833; PubMed=1738160; DOI=10.1016/0022-2836(92)90666-8;
RA   Chou K.-C.;
RT   "Energy-optimized structure of antifreeze protein and its binding
RT   mechanism.";
RL   J. Mol. Biol. 223:509-517(1992).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 45-81, AND AMIDATION AT
RP   ARG-81.
RX   MEDLINE=95281060; PubMed=7760940; DOI=10.1038/375427a0;
RA   Sicheri F., Yang D.S.C.;
RT   "Ice-binding structure and mechanism of an antifreeze protein from
RT   winter flounder.";
RL   Nature 375:427-431(1995).
RN   [8]
RP   STRUCTURE BY NMR OF 45-81, AMIDATION AT ARG-81, AND MUTAGENESIS OF
RP   THR-46; ALA-51; ALA-55; THR-57; THR-68; ALA-73; ALA-77 AND THR-79.
RX   MEDLINE=21845977; PubMed=11856360;
RX   DOI=10.1046/j.1432-1033.2002.02766.x;
RA   Liepinsh E., Otting G., Harding M.M., Ward L.G., Mackay J.P.,
RA   Haymet A.D.;
RT   "Solution structure of a hydrophobic analogue of the winter flounder
RT   antifreeze protein.";
RL   Eur. J. Biochem. 269:1259-1266(2002).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- INDUCTION: By winter conditions, at least in part by water
CC       temperatures of below 8 degrees Celsius.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   EMBL; L00138; AAB59964.1; -; Genomic_DNA.
DR   EMBL; L29178; AAB59964.1; JOINED; Genomic_DNA.
DR   EMBL; X07506; CAA30389.1; -; Genomic_DNA.
DR   EMBL; M62414; AAA49469.1; -; Genomic_DNA.
DR   EMBL; M62416; AAA49471.1; -; Genomic_DNA.
DR   EMBL; M62417; AAA49472.1; -; Genomic_DNA.
DR   PIR; A05161; A05161.
DR   PIR; JS0704; FDFLAW.
DR   PIR; JS0706; JS0706.
DR   PIR; S02326; S02326.
DR   PDB; 1ATF; Model; -; A=45-81.
DR   PDB; 1J5B; NMR; -; A=47-81.
DR   PDB; 1WFA; X-ray; 1.70 A; A/B=45-81.
DR   PDB; 1WFB; X-ray; 1.50 A; A/B=45-81.
DR   PDBsum; 1ATF; -.
DR   PDBsum; 1J5B; -.
DR   PDBsum; 1WFA; -.
DR   PDBsum; 1WFB; -.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0050825; F:ice binding; TAS:UniProtKB.
DR   GO; GO:0042309; P:homoiothermy; IEP:UniProtKB.
DR   GO; GO:0050826; P:response to freezing; IEP:UniProtKB.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   1: Evidence at protein level;
KW   3D-structure; Amidation; Antifreeze protein;
KW   Direct protein sequencing; Polymorphism; Repeat; Secreted; Signal.
FT   SIGNAL        1     23
FT   PROPEP       24     44       Removed by a dipeptidylpeptidase
FT                                (Probable).
FT                                /FTId=PRO_0000001685.
FT   CHAIN        45     81       Ice-structuring protein A.
FT                                /FTId=PRO_0000001686.
FT   COMPBIAS     28     80       Ala-rich.
FT   MOD_RES      81     81       Arginine amide.
FT   VARIANT      36     36       A -> V.
FT   VARIANT      70     70       A -> D.
FT   MUTAGEN      46     46       T->V: No significant effect on 3D
FT                                structure; when associated with K-51; E-
FT                                55; V-57; V-68; K-73; E-77 and V-79.
FT   MUTAGEN      51     51       A->K: No significant effect on 3D
FT                                structure; when associated with V-46; E-
FT                                55; V-57; V-68; K-73; E-77 and V-79.
FT   MUTAGEN      55     55       A->E: No significant effect on 3D
FT                                structure; when associated with V-46; K-
FT                                51; V-57; V-68; K-73; E-77 and V-79.
FT   MUTAGEN      57     57       T->V: No significant effect on 3D
FT                                structure; when associated with V-46; K-
FT                                51; E-55; V-68; K-73; E-77 and V-79.
FT   MUTAGEN      68     68       T->V: No significant effect on 3D
FT                                structure; when associated with V-46; K-
FT                                51; E-55; V-57; K-73; E-77 and V-79.
FT   MUTAGEN      73     73       A->K: No significant effect on 3D
FT                                structure; when associated with V-46; K-
FT                                51; E-55; V-57; V-68; E-77 and V-79.
FT   MUTAGEN      77     77       A->E: No significant effect on 3D
FT                                structure; when associated with V-46; K-
FT                                51; E-55; V-57; V-68; K-73 and V-79.
FT   MUTAGEN      79     79       T->V: No significant effect on 3D
FT                                structure; when associated with V-46; K-
FT                                51; E-55; V-57; V-68; K-73 and E-77.
FT   CONFLICT     24     24       S -> R (in Ref. 3; CAA30389 and 4;
FT                                AAA49469).
FT   HELIX        46     79
SQ   SEQUENCE   82 AA;  7711 MW;  C2AE7B74C0D46CC1 CRC64;
     MALSLFTVGQ LIFLFWTMRI TEASPDPAAK AAPAAAAAPA AAAPDTASDA AAAAALTAAN
     AKAAAELTAA NAAAAAAATA RG
//
ID   ANPB_PSEAM              Reviewed;          82 AA.
AC   Q99013;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   28-JUL-2009, entry version 36.
DE   RecName: Full=Ice-structuring protein B;
DE            Short=ISP B;
DE   AltName: Full=Antifreeze protein B;
DE   AltName: Full=HPLC8;
DE   Flags: Precursor;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes
OS   americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Testis;
RX   MEDLINE=92209995; PubMed=1555765; DOI=10.1016/0378-1119(92)90372-V;
RA   Davies P.L.;
RT   "Conservation of antifreeze protein-encoding genes in tandem
RT   repeats.";
RL   Gene 112:163-170(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-28, AND AMIDATION.
RC   TISSUE=Liver;
RX   PubMed=3769927; DOI=10.1111/j.1432-1033.1986.tb09966.x;
RA   Hew C.-L., Wang N.-C., Yan S., Cai H., Sclater A., Fletcher G.L.;
RT   "Biosynthesis of antifreeze polypeptides in the winter flounder.
RT   Characterization and seasonal occurrence of precursor polypeptides.";
RL   Eur. J. Biochem. 160:267-272(1986).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- INDUCTION: By winter conditions, at least in part by water
CC       temperatures of below 8 degrees Celsius.
CC   -!- PTM: Amidated.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   EMBL; M62413; AAA49468.1; -; Genomic_DNA.
DR   PIR; JS0705; JS0705.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0050825; F:ice binding; TAS:UniProtKB.
DR   GO; GO:0042309; P:homoiothermy; IEP:UniProtKB.
DR   GO; GO:0050826; P:response to freezing; IEP:UniProtKB.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   1: Evidence at protein level;
KW   Amidation; Antifreeze protein; Direct protein sequencing; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     23
FT   PROPEP       24     44       Removed by a dipeptidylpeptidase
FT                                (Probable).
FT                                /FTId=PRO_0000225596.
FT   CHAIN        45     81       Ice-structuring protein B.
FT                                /FTId=PRO_0000225597.
FT   COMPBIAS     28     80       Ala-rich.
FT   MOD_RES      81     81       Arginine amide (By similarity).
SQ   SEQUENCE   82 AA;  7794 MW;  C8AEDA75DA4B87FA CRC64;
     MALSLFTVGQ LIFLFWTMRI TEARPDPAAK AAPAAAAVPA AAAPDTASDA AAAAALTAAN
     AAAAAKLTAD NAAAAAAATA RG
//
ID   ANPD_MACAM              Reviewed;          87 AA.
AC   P19604;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 54.
DE   RecName: Full=Ice-structuring protein C7;
DE            Short=ISP C7;
DE   AltName: Full=Antifreeze protein C7;
DE   Flags: Precursor;
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; B31075; B31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19604; 22-85.
DR   HOVERGEN; P19604; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     21       By similarity.
FT   CHAIN        22     87       Ice-structuring protein C7.
FT                                /FTId=PRO_0000001692.
FT   DOMAIN       24     83       AFP-like.
FT   SITE         29     29       Important for ice-binding (By
FT                                similarity).
FT   SITE         34     34       Important for ice-binding (By
FT                                similarity).
FT   SITE         38     38       Important for ice-binding (By
FT                                similarity).
FT   SITE         64     64       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   87 AA;  9229 MW;  B5615B2E82DC87AB CRC64;
     MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPINTALTPV MMEGKVTNPI GIPFAEMSQI
     VGKQVNTPVA KGQTIMPNMV KTYAAGK
//
ID   ANPE_MACAM              Reviewed;          87 AA.
AC   P19605;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   22-SEP-2009, entry version 54.
DE   RecName: Full=Ice-structuring protein C10;
DE            Short=ISP C10;
DE   AltName: Full=Antifreeze protein C10;
DE   Flags: Precursor;
OS   Macrozoarces americanus (Ocean pout) (Zoarces americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Perciformes; Zoarcoidei;
OC   Zoarcidae; Zoarcinae; Macrozoarces.
OX   NCBI_TaxID=8199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=88298890; PubMed=3403560;
RA   Hew C.-L., Wang N.-C., Joshi S., Fletcher G.L., Scott G.K.,
RA   Hayes P.H., Buettner B., Davies P.L.;
RT   "Multiple genes provide the basis for antifreeze protein diversity and
RT   dosage in the ocean pout, Macrozoarces americanus.";
RL   J. Biol. Chem. 263:12049-12055(1988).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point by
CC       absorbing ice and inhibiting its growth.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the type-III AFP family.
CC   -!- SIMILARITY: Contains 1 AFP-like domain.
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DR   PIR; A31075; A31075.
DR   HSSP; P19608; 1OPS.
DR   SMR; P19605; 22-85.
DR   HOVERGEN; P19605; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   ProDom; PD003258; AntifreezeIII; 1.
DR   PROSITE; PS50844; AFP_LIKE; 1.
PE   3: Inferred from homology;
KW   Antifreeze protein; Secreted; Signal.
FT   SIGNAL        1     21       By similarity.
FT   CHAIN        22     87       Ice-structuring protein C10.
FT                                /FTId=PRO_0000001693.
FT   DOMAIN       24     83       AFP-like.
FT   SITE         29     29       Important for ice-binding (By
FT                                similarity).
FT   SITE         34     34       Important for ice-binding (By
FT                                similarity).
FT   SITE         38     38       Important for ice-binding (By
FT                                similarity).
FT   SITE         64     64       Important for ice-binding (By
FT                                similarity).
SQ   SEQUENCE   87 AA;  9306 MW;  92655F2AC313A0B5 CRC64;
     MKSVILTGLL FVLLCVDHMT ASQSVVATQL IPMNSALTPV MMEGKVTNPI GIPFAEMSQM
     VGKQVNRPVA KGQTIMPNMV KTYAAGK
//
ID   ANPX_PSEAM              Reviewed;          91 AA.
AC   P07835;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   22-SEP-2009, entry version 46.
DE   RecName: Full=Ice-structuring protein 2A7;
DE            Short=ISP 2A7;
DE   AltName: Full=Antifreeze protein IIA7;
DE            Short=AFP;
DE   Flags: Precursor;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes
OS   americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85054993; PubMed=6548752;
RA   Gourlie B., Lin Y., Price J., Devries A.L., Powers D., Huang R.C.C.;
RT   "Winter flounder antifreeze proteins: a multigene family.";
RL   J. Biol. Chem. 259:14960-14965(1984).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   EMBL; M10148; AAA49465.1; -; mRNA.
DR   PIR; A22592; A22592.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
DR   GO; GO:0042309; P:homoiothermy; IEA:InterPro.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   3: Inferred from homology;
KW   Antifreeze protein; Repeat; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22     39       Removed by a dipeptidylpeptidase
FT                                (Probable).
FT                                /FTId=PRO_0000001687.
FT   CHAIN        40     91       Ice-structuring protein 2A7.
FT                                /FTId=PRO_0000001688.
SQ   SEQUENCE   91 AA;  8326 MW;  D1FC542FD865012C CRC64;
     MALSLFTVGQ LIFLFWTMRI TEANPDPAAK AVPAAAAPDT ASDAAAAAAA TAATAAAAAA
     ATAATAAKAA ALTAANAAAA AAATAAAAAR G
//
ID   ANPY_PSEAM              Reviewed;          91 AA.
AC   P23699;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   22-SEP-2009, entry version 46.
DE   RecName: Full=Ice-structuring protein;
DE            Short=ISP;
DE   AltName: Full=Antifreeze protein;
DE            Short=AFP;
DE   Flags: Precursor;
OS   Pseudopleuronectes americanus (Winter flounder) (Pleuronectes
OS   americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Pleuronectiformes;
OC   Pleuronectoidei; Pleuronectidae; Pleuronectinae; Pseudopleuronectes.
OX   NCBI_TaxID=8265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90384854; PubMed=2402466; DOI=10.1093/nar/18.17.5303;
RA   Gauthier S., Wu Y., Davies P.L.;
RT   "Nucleotide sequence of a variant antifreeze protein gene.";
RL   Nucleic Acids Res. 18:5303-5303(1990).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the type-I AFP family.
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DR   EMBL; X53718; CAA37754.1; -; Genomic_DNA.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
DR   GO; GO:0042309; P:homoiothermy; IEA:InterPro.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   3: Inferred from homology;
KW   Antifreeze protein; Repeat; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22     39       Removed by a dipeptidylpeptidase
FT                                (Probable).
FT                                /FTId=PRO_0000001689.
FT   CHAIN        40     91       Ice-structuring protein.
FT                                /FTId=PRO_0000001690.
SQ   SEQUENCE   91 AA;  8355 MW;  D1FC5439A902012C CRC64;
     MALSLFTVGQ LIFLFWTMRI TEANPDPAAK AVPAAAAPDT ASDAAAAAAA TAATAAAAAA
     ATAVTAAKAA ALTAANAAAA AAATAAAAAR G
//
ID   ANTF_ANTPS              Reviewed;          20 AA.
AC   P86268;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   22-SEP-2009, entry version 3.
DE   RecName: Full=Antifreeze protein;
DE   Flags: Fragment;
OS   Antarctomyces psychrotrophicus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Thelebolales; Thelebolaceae; Antarctomyces.
OX   NCBI_TaxID=89416;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RP   GLYCOSYLATION, AND MASS SPECTROMETRY.
RC   STRAIN=KG-1;
RA   Xiao N., Takamichi M., Suzuki K., Nishimiya Y., Kondo H., Tsuda S.,
RA   Hoshino T.;
RT   "A new antifreeze protein from Antarctic ascomycota.";
RL   Submitted (MAR-2009) to UniProtKB.
CC   -!- FUNCTION: Modification of ice crystals, thermal hysteresis and
CC       recrystallization inhibiton.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- INDUCTION: By low temperature.
CC   -!- PTM: N-glycosylated and O-glycosylated.
CC   -!- MASS SPECTROMETRY: Mass=21742; Method=MALDI; Range=1-?;
CC       Source=Ref.1;
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DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Glycoprotein; Secreted;
KW   Stress response.
FT   CHAIN         1    >20       Antifreeze protein.
FT                                /FTId=PRO_0000373064.
FT   NON_TER      20     20
SQ   SEQUENCE   20 AA;  1848 MW;  F48180EEC1E885E8 CRC64;
     AGLDLGAASX FGALAFEGVA
//
ID   ISP2_HEMAM              Reviewed;         163 AA.
AC   P05140;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   22-SEP-2009, entry version 67.
DE   RecName: Full=Type-2 ice-structuring protein;
DE   AltName: Full=Type II antifreeze protein;
DE            Short=AFP;
DE   Flags: Precursor;
OS   Hemitripterus americanus (Sea raven).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Scorpaeniformes;
OC   Cottoidei; Hemitripteridae; Hemitripterus.
OX   NCBI_TaxID=8094;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87057207; PubMed=3782083;
RA   Ng N.F.L., Trinh K.-Y., Hew C.-L.;
RT   "Structure of an antifreeze polypeptide precursor from the sea raven,
RT   Hemitripterus americanus.";
RL   J. Biol. Chem. 261:15690-15695(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   MEDLINE=90036986; PubMed=2572595;
RA   Hayes P., Scott G.K., Ng N.F.L., Hew C.-L., Davies P.L.;
RT   "Cystine-rich type II antifreeze protein precursor is initiated from
RT   the third AUG codon of its mRNA.";
RL   J. Biol. Chem. 264:18761-18767(1989).
RN   [3]
RP   PRELIMINARY DISULFIDE BONDS, AND SIMILARITY TO C-TYPE LECTINS.
RX   MEDLINE=92355557; PubMed=1644794;
RA   Ng N.F.L., Hew C.-L.;
RT   "Structure of an antifreeze polypeptide from the sea raven. Disulfide
RT   bonds and similarity to lectin-binding proteins.";
RL   J. Biol. Chem. 267:16069-16075(1992).
RN   [4]
RP   STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX   MEDLINE=98206886; PubMed=9537986; DOI=10.1021/bi972788c;
RA   Gronwald W., Loewen M.C., Lix B., Daugulis A.J., Soennichsen F.D.,
RA   Davies P.L., Sykes B.D.;
RT   "The solution structure of type II antifreeze protein reveals a new
RT   member of the lectin family.";
RL   Biochemistry 37:4712-4721(1998).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
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DR   EMBL; J02593; AAA49617.1; ALT_INIT; mRNA.
DR   EMBL; J05100; AAA49618.1; -; Genomic_DNA.
DR   PIR; A34313; A34313.
DR   PDB; 2AFP; NMR; -; A=35-163.
DR   PDBsum; 2AFP; -.
DR   HOVERGEN; P05140; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR002353; AntifreezeII.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   PRINTS; PR00356; ANTIFREEZEII.
DR   SMART; SM00034; CLECT; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antifreeze protein; Direct protein sequencing;
KW   Disulfide bond; Lectin; Secreted; Signal.
FT   SIGNAL        1     17       Potential.
FT   PROPEP       18     34
FT                                /FTId=PRO_0000017544.
FT   CHAIN        35    163       Type-2 ice-structuring protein.
FT                                /FTId=PRO_0000017545.
FT   DOMAIN       39    163       C-type lectin.
FT   DISULFID     41     52
FT   DISULFID     69    159
FT   DISULFID    103    134
FT   DISULFID    123    145
FT   DISULFID    135    151
FT   CONFLICT     38     38       P -> G (in Ref. 2; AAA49618).
FT   STRAND       43     45
FT   STRAND       49     53
FT   HELIX        62     72
FT   STRAND       80     82
FT   HELIX        83     91
FT   STRAND      103    107
FT   STRAND      110    114
FT   STRAND      122    124
FT   STRAND      141    144
FT   STRAND      159    161
SQ   SEQUENCE   163 AA;  17509 MW;  52C2D284F65E8A47 CRC64;
     MLTVSLLVCA MMALTQANDD KILKGTATEA GPVSQRAPPN CPAGWQPLGD RCIYYETTAM
     TWALAETNCM KLGGHLASIH SQEEHSFIQT LNAGVVWIGG SACLQAGAWT WSDGTPMNFR
     SWCSTKPDDV LAACCMQMTA AADQCWDDLP CPASHKSVCA MTF
//
ID   ISP2_OSMMO              Reviewed;         175 AA.
AC   Q01758;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   22-SEP-2009, entry version 51.
DE   RecName: Full=Type-2 ice-structuring protein;
DE   AltName: Full=Type II antifreeze protein;
DE            Short=AFP;
DE   Flags: Precursor;
OS   Osmerus mordax (Rainbow smelt).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Euteleostei;
OC   Protacanthopterygii; Salmoniformes; Osmeridae; Osmerus.
OX   NCBI_TaxID=8014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-65; 69-78;
RP   145-154 AND 161-173.
RC   TISSUE=Liver;
RX   MEDLINE=92287116; PubMed=1599470;
RA   Ewart K.V., Rubinsky B., Fletcher G.L.;
RT   "Structural and functional similarity between fish antifreeze proteins
RT   and calcium-dependent lectins.";
RL   Biochem. Biophys. Res. Commun. 185:335-340(1992).
CC   -!- FUNCTION: Antifreeze proteins lower the blood freezing point.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
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DR   EMBL; M96154; AAA49442.1; -; mRNA.
DR   PIR; JH0626; JH0626.
DR   HSSP; P05140; 2AFP.
DR   HOVERGEN; Q01758; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0050826; P:response to freezing; IEA:UniProtKB-KW.
DR   InterPro; IPR002353; AntifreezeII.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   PRINTS; PR00356; ANTIFREEZEII.
DR   SMART; SM00034; CLECT; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Disulfide bond; Lectin;
KW   Secreted; Signal.
FT   SIGNAL        1     16       Potential.
FT   PROPEP       17     33       Potential.
FT                                /FTId=PRO_0000017546.
FT   CHAIN        34    175       Type-2 ice-structuring protein.
FT                                /FTId=PRO_0000017547.
FT   DOMAIN       36    163       C-type lectin.
FT   DISULFID     38     49       By similarity.
FT   DISULFID     66    159       By similarity.
FT   DISULFID    103    134       By similarity.
FT   DISULFID    123    145       By similarity.
FT   DISULFID    135    151       By similarity.
SQ   SEQUENCE   175 AA;  19054 MW;  E2A72D8C030AFAA3 CRC64;
     MLAALLVCAM VALTRAANGD TGKEAVMTGS SGKNLTECPT DWKMFNGRCF LFNPLQLHWA
     HAQISCMKDG ANLASIHSLE EYAFVKELTT AGLIPAWIGG SDCHVSTYWF WMDSTSMDFT
     DWCAAQPDFT LTECCIQINV GVGKCWNDTP CTHLHASVCA KPATVIPEVT PPSIM
//
