OSTCN_CYPCA
ID OSTCN_CYPCA Reviewed; 48 AA.
AC Q7LZI4;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Osteocalcin;
DE AltName: Full=Bone Gla protein;
DE Short=BGP;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein;
GN Name=bglap;
OS Cyprinus carpio (Common carp).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Cyprinus.
OX NCBI_TaxID=7962;
RN [1]
RP PROTEIN SEQUENCE, DISULFIDE BOND, AND GAMMA-CARBOXYGLUTAMATION AT GLU-14;
RP GLU-18 AND GLU-21.
RC TISSUE=Bone;
RX PubMed=12517753; DOI=10.1074/jbc.m211449200;
RA Nishimoto S.K., Waite J.H., Nishimoto M., Kriwacki R.W.;
RT "Structure, activity, and distribution of fish osteocalcin.";
RL J. Biol. Chem. 278:11843-11848(2003).
CC -!- FUNCTION: Binds strongly to apatite and calcium. Comprise over 35% of
CC the total extractable proteins of rib bones.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:12517753}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {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; A59458; A59458.
DR AlphaFoldDB; Q7LZI4; -.
DR SMR; Q7LZI4; -.
DR Proteomes; UP000694384; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IEA:InterPro.
DR GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:InterPro.
DR GO; GO:0032571; P:response to vitamin K; IEA:InterPro.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR039176; Osteocalcin.
DR PANTHER; PTHR14235; PTHR14235; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
PE 1: Evidence at protein level;
KW Biomineralization; Calcium; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Gamma-carboxyglutamic acid; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..48
FT /note="Osteocalcin"
FT /id="PRO_0000148908"
FT DOMAIN 1..44
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 18
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 14
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12517753"
FT MOD_RES 18
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12517753"
FT MOD_RES 21
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12517753"
FT DISULFID 20..26
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12517753"
SQ SEQUENCE 48 AA; 5063 MW; D39D77F2C7F8FFC1 CRC64;
AGTAPADLTV AQLESLKEVC EANLACEHMM DVSGIIAAYT AYYGPIPY
