ID ANP2_PACBR Reviewed; 63 AA.
AC P12101;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 22-FEB-2023, entry version 83.
DE RecName: Full=Ice-structuring protein AB2;
DE Short=ISP AB2;
DE AltName: Full=Antifreeze peptide AB2;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S04974; S04974.
DR AlphaFoldDB; P12101; -.
DR SMR; P12101; -.
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 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 AB2"
FT /id="PRO_0000155150"
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; 7001 MW; A1E7F954598DD061 CRC64;
TKSVVANQLI PINTALTLVM MKAEEVSPKG IPAEEIPRLV GMQVNRAVYL DETLMPDMVK
NYE
//
