ANPA_PSEAM
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 25-MAY-2022, entry version 97.
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 americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Pleuronectidae;
OC Pseudopleuronectes.
OX NCBI_TaxID=8265;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASP-70, FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND PARTIAL PROTEIN SEQUENCE.
RX 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 PubMed=6086629; DOI=10.1016/s0021-9258(17)47291-7;
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 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 PubMed=1555765; DOI=10.1016/0378-1119(92)90372-v;
RA Davies P.L.;
RT "Conservation of antifreeze protein-encoding genes in tandem repeats.";
RL Gene 112:163-170(1992).
RN [5]
RP PROTEIN SEQUENCE OF 24-28, FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP 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 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 ARG-81.
RX PubMed=7760940; DOI=10.1038/375427a0;
RA Sicheri F., Yang D.S.C.;
RT "Ice-binding structure and mechanism of an antifreeze protein from winter
RT flounder.";
RL Nature 375:427-431(1995).
RN [8]
RP STRUCTURE BY NMR OF 45-81, AMIDATION AT ARG-81, AND MUTAGENESIS OF THR-46;
RP ALA-51; ALA-55; THR-57; THR-68; ALA-73; ALA-77 AND THR-79.
RX PubMed=11856360; DOI=10.1046/j.1432-1033.2002.02766.x;
RA Liepinsh E., Otting G., Harding M.M., Ward L.G., Mackay J.P., 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: Contributes to protect fish blood from freezing at subzero
CC sea water temperatures. Lowers the blood freezing point. Binds to
CC nascent ice crystals and prevents further growth.
CC {ECO:0000269|PubMed:3769927, ECO:0000269|PubMed:6952188}.
CC -!- INTERACTION:
CC P04002; P04002: -; NbExp=3; IntAct=EBI-11769728, EBI-11769728;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6952188}.
CC -!- TISSUE SPECIFICITY: Detected in liver and in blood serum (at protein
CC level). {ECO:0000269|PubMed:3769927, ECO:0000269|PubMed:6952188}.
CC -!- INDUCTION: By winter conditions, at least in part by water temperatures
CC of below 8 degrees Celsius. {ECO:0000269|PubMed:3769927}.
CC -!- SIMILARITY: Belongs to the type-I AFP family. {ECO:0000305}.
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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; 1J5B; NMR; -; A=58-81.
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; 1J5B; -.
DR PDBsum; 1WFA; -.
DR PDBsum; 1WFB; -.
DR AlphaFoldDB; P04002; -.
DR SMR; P04002; -.
DR MINT; P04002; -.
DR EvolutionaryTrace; P04002; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0050825; F:ice binding; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR InterPro; IPR000104; Antifreeze_1.
DR PRINTS; PR00308; ANTIFREEZEI.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Antifreeze protein; Direct protein sequencing;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:3769927"
FT PROPEP 24..44
FT /note="Removed by a dipeptidylpeptidase"
FT /evidence="ECO:0000305"
FT /id="PRO_0000001685"
FT CHAIN 45..81
FT /note="Ice-structuring protein A"
FT /id="PRO_0000001686"
FT MOD_RES 81
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:11856360,
FT ECO:0000269|PubMed:7760940"
FT VARIANT 36
FT /note="A -> V"
FT /evidence="ECO:0000269|PubMed:1555765"
FT VARIANT 70
FT /note="A -> D"
FT /evidence="ECO:0000269|PubMed:6952188"
FT MUTAGEN 46
FT /note="T->V: No significant effect on 3D structure; when
FT associated with K-51; E-55; V-57; V-68; K-73; E-77 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 51
FT /note="A->K: No significant effect on 3D structure; when
FT associated with V-46; E-55; V-57; V-68; K-73; E-77 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 55
FT /note="A->E: No significant effect on 3D structure; when
FT associated with V-46; K-51; V-57; V-68; K-73; E-77 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 57
FT /note="T->V: No significant effect on 3D structure; when
FT associated with V-46; K-51; E-55; V-68; K-73; E-77 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 68
FT /note="T->V: No significant effect on 3D structure; when
FT associated with V-46; K-51; E-55; V-57; K-73; E-77 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 73
FT /note="A->K: No significant effect on 3D structure; when
FT associated with V-46; K-51; E-55; V-57; V-68; E-77 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 77
FT /note="A->E: No significant effect on 3D structure; when
FT associated with V-46; K-51; E-55; V-57; V-68; K-73 and V-
FT 79."
FT /evidence="ECO:0000269|PubMed:11856360"
FT MUTAGEN 79
FT /note="T->V: No significant effect on 3D structure; when
FT associated with V-46; K-51; E-55; V-57; V-68; K-73 and E-
FT 77."
FT /evidence="ECO:0000269|PubMed:11856360"
FT CONFLICT 24
FT /note="S -> R (in Ref. 3; CAA30389 and 4; AAA49469)"
FT /evidence="ECO:0000305"
FT HELIX 46..79
FT /evidence="ECO:0007829|PDB:1WFB"
SQ SEQUENCE 82 AA; 7711 MW; C2AE7B74C0D46CC1 CRC64;
MALSLFTVGQ LIFLFWTMRI TEASPDPAAK AAPAAAAAPA AAAPDTASDA AAAAALTAAN
AKAAAELTAA NAAAAAAATA RG
