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   25-MAY-2022, entry version 83.
DE   RecName: Full=Type-3 ice-structuring protein 1.9;
DE   AltName: Full=Antifreeze protein type III;
DE   AltName: Full=ISP 3;
DE   Flags: Precursor;
OS   Anarhichas lupus (Atlantic wolffish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Zoarcales; Anarhichadidae; Anarhichas.
OX   NCBI_TaxID=8204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2851724; DOI=10.1128/mcb.8.9.3670-3675.1988;
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: 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:0000250}.
CC   -!- SIMILARITY: Belongs to the type-III AFP family. {ECO:0000305}.
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DR   EMBL; M22125; AAA74890.1; -; Genomic_DNA.
DR   PIR; A30238; A30238.
DR   AlphaFoldDB; P12416; -.
DR   SMR; P12416; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006190; AFP_Neu5c_C.
DR   InterPro; IPR036732; AFP_Neu5c_C_sf.
DR   InterPro; IPR006013; Antifreeze_III.
DR   InterPro; IPR013974; SAF.
DR   Pfam; PF08666; SAF; 1.
DR   PRINTS; PR00357; ANTIFREEZIII.
DR   SMART; SM00858; SAF; 1.
DR   SUPFAM; SSF51269; SSF51269; 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
FT                   /note="Type-3 ice-structuring protein 1.9"
FT                   /id="PRO_0000001696"
FT   DOMAIN          25..84
FT                   /note="AFP-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT   SITE            30
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            35
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            39
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
FT   SITE            65
FT                   /note="Important for ice-binding"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   88 AA;  9438 MW;  738EB9E62B3F347C CRC64;
     MKSAILTGLL FVLLCVDHLS SASQSVVATQ LIPINTALTP IMMKGQVVNP AGIPFAEMSQ
     IVGKQVNRPV AKDETLMPNM VKTYRAAK