ID   OSTCN_DANRE             Reviewed;          45 AA.
AC   P83238;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Osteocalcin;
DE   AltName: Full=Bone Gla protein;
DE            Short=BGP;
DE   AltName: Full=Gamma-carboxyglutamic acid-containing protein;
DE   Flags: Fragment;
GN   Name=bglap;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Cartilage;
RA   Simes D.C., Cancela M.L.;
RL   Submitted (JAN-2002) to UniProtKB.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 1-21, AND GAMMA-CARBOXYGLUTAMATION AT GLU-14; GLU-18
RP   AND GLU-21.
RC   TISSUE=Cartilage;
RX   PubMed=14668966; DOI=10.1007/s00223-003-0079-4;
RA   Simes D.C., Williamson M.K., Schaff B.J., Gavaia P.J., Ingleton P.M.,
RA   Price P.A., Cancela M.L.;
RT   "Characterization of osteocalcin (BGP) and matrix Gla protein (MGP) fish
RT   specific antibodies: validation for immunodetection studies in lower
RT   vertebrates.";
RL   Calcif. Tissue Int. 74:170-180(2004).
CC   -!- FUNCTION: Binds strongly to apatite and calcium. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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:14668966,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
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DR   ZFIN; ZDB-GENE-050113-4; bglap.
DR   InParanoid; P83238; -.
DR   PhylomeDB; P83238; -.
DR   Reactome; R-DRE-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-DRE-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0046848; F:hydroxyapatite binding; IBA:GO_Central.
DR   GO; GO:0008147; F:structural constituent of bone; IBA:GO_Central.
DR   GO; GO:0060348; P:bone development; IBA:GO_Central.
DR   GO; GO:0030282; P:bone mineralization; TAS:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR   GO; GO:1900076; P:regulation of cellular response to insulin stimulus; IEA:InterPro.
DR   GO; GO:0009612; P:response to mechanical stimulus; IDA:ZFIN.
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   Gamma-carboxyglutamic acid; Metal-binding; Reference proteome; Secreted.
FT   CHAIN           1..>45
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000148907"
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:14668966"
FT   MOD_RES         18
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:14668966"
FT   MOD_RES         21
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:14668966"
FT   DISULFID        20..26
FT                   /evidence="ECO:0000250|UniProtKB:P02823,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   NON_TER         45
SQ   SEQUENCE   45 AA;  4838 MW;  E4DC09036FEE75D0 CRC64;
     AGTAXGDLTP FQLESLREVC EVNLACEHMA DTXGIVAAYT AYYGY