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   25-MAY-2022, entry version 80.
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) (Atherina mordax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Stomiati; Osmeriformes; Osmeridae;
OC   Osmerus.
OX   NCBI_TaxID=8014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-65; 69-78; 145-154
RP   AND 161-173.
RC   TISSUE=Liver;
RX   PubMed=1599470; DOI=10.1016/s0006-291x(05)90005-3;
RA   Ewart K.V., Rubinsky B., Fletcher G.L.;
RT   "Structural and functional similarity between fish antifreeze proteins and
RT   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.
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DR   EMBL; M96154; AAA49442.1; -; mRNA.
DR   PIR; JH0626; JH0626.
DR   AlphaFoldDB; Q01758; -.
DR   SMR; Q01758; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR002353; AntifreezeII.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   PRINTS; PR00356; ANTIFREEZEII.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 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
FT                   /evidence="ECO:0000255"
FT   PROPEP          17..33
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000017546"
FT   CHAIN           34..175
FT                   /note="Type-2 ice-structuring protein"
FT                   /id="PRO_0000017547"
FT   DOMAIN          36..163
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        38..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        66..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        103..134
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        123..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        135..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
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