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-FEB-2023, entry version 82.
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; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Zoarcales; Zoarcidae; Lycodinae;
OC Pachycara.
OX NCBI_TaxID=36221;
RN [1]
RP PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX 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: 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:2752054}.
CC -!- TISSUE SPECIFICITY: Detected in blood serum (at protein level).
CC {ECO:0000269|PubMed:2752054}.
CC -!- SIMILARITY: Belongs to the type-III AFP family. {ECO:0000305}.
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DR PIR; S04973; S04973.
DR AlphaFoldDB; P12100; -.
DR SMR; P12100; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR CDD; cd11617; Antifreeze_III; 1.
DR Gene3D; 3.90.1210.10; Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain; 1.
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; AFP III-like domain; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
PE 1: Evidence at protein level;
KW Antifreeze protein; Direct protein sequencing; Secreted.
FT CHAIN 1..63
FT /note="Ice-structuring protein AB1"
FT /id="PRO_0000155149"
FT DOMAIN 3..62
FT /note="AFP-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00021"
FT SITE 8
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT SITE 13
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT SITE 17
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
FT SITE 43
FT /note="Important for ice-binding"
FT /evidence="ECO:0000250"
SQ SEQUENCE 63 AA; 6846 MW; AC84FD14247193B4 CRC64;
TKSVVASQLI PINTALTPAM MKAKEVSPKG IPAEEMSKIV GMQVNRAVNL DETLMPDMVK
TYQ
//
