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   25-MAY-2022, entry version 55.
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 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 [MRNA], PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=6548752; DOI=10.1016/s0021-9258(17)42697-4;
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: 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6548752}.
CC   -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC       {ECO:0000269|PubMed:6548752}.
CC   -!- SIMILARITY: Belongs to the type-I AFP family. {ECO:0000305}.
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DR   EMBL; M10148; AAA49465.1; -; mRNA.
DR   PIR; A22592; A22592.
DR   AlphaFoldDB; P07835; -.
DR   SMR; P07835; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0050825; F:ice binding; IEA:InterPro.
DR   InterPro; IPR000104; Antifreeze_1.
DR   PRINTS; PR00308; ANTIFREEZEI.
PE   1: Evidence at protein level;
KW   Antifreeze protein; Direct protein sequencing; Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..39
FT                   /note="Removed by a dipeptidylpeptidase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000001687"
FT   CHAIN           40..91
FT                   /note="Ice-structuring protein 2A7"
FT                   /id="PRO_0000001688"
SQ   SEQUENCE   91 AA;  8326 MW;  D1FC542FD865012C CRC64;
     MALSLFTVGQ LIFLFWTMRI TEANPDPAAK AVPAAAAPDT ASDAAAAAAA TAATAAAAAA
     ATAATAAKAA ALTAANAAAA AAATAAAAAR G