ID   OSTCN_LEPMA             Reviewed;          45 AA.
AC   P28317;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Lepomis macrochirus (Bluegill) (Eupomotis macrochirus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Centrarchiformes; Centrarchoidei; Centrarchidae; Lepomis.
OX   NCBI_TaxID=13106;
RN   [1]
RP   PROTEIN SEQUENCE, AND GAMMA-CARBOXYGLUTAMATION AT GLU-11; GLU-15 AND
RP   GLU-18.
RC   TISSUE=Scale;
RX   PubMed=1597487; DOI=10.1016/s0021-9258(19)49953-5;
RA   Nishimoto S.K., Araki N., Robinson F.D., Waite J.H.;
RT   "Discovery of bone gamma-carboxyglutamic acid protein in mineralized
RT   scales. The abundance and structure of Lepomis macrochirus bone gamma-
RT   carboxyglutamic acid protein.";
RL   J. Biol. Chem. 267:11600-11605(1992).
CC   -!- FUNCTION: Binds strongly to apatite and calcium.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Also found in smaller quantities in dentin.
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:1597487}.
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; A42794; A42794.
DR   AlphaFoldDB; P28317; -.
DR   SMR; P28317; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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   Gamma-carboxyglutamic acid; Metal-binding; Secreted.
FT   CHAIN           1..45
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000148910"
FT   DOMAIN          1..41
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   BINDING         11
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         15
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         18
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
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         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:1597487"
FT   MOD_RES         15
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:1597487"
FT   MOD_RES         18
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|PubMed:1597487"
FT   DISULFID        17..23
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ   SEQUENCE   45 AA;  4871 MW;  5CA46134007D0A0D CRC64;
     AAGELTLTQL ESLREVCEAN LACEDMMDAQ GIIAAYTAYY GPIPY