OSTCN_BOVIN
ID OSTCN_BOVIN Reviewed; 100 AA.
AC P02820; A7YEW1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Osteocalcin;
DE AltName: Full=Bone Gla protein;
DE Short=BGP;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein;
DE Flags: Precursor;
GN Name=BGLAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2336375; DOI=10.1093/nar/18.7.1909;
RA Kiefer M.C., Saphire A.C.S., Bauer D.M., Barr P.J.;
RT "The cDNA and derived amino acid sequences of human and bovine bone Gla
RT protein.";
RL Nucleic Acids Res. 18:1909-1909(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Paolella M.J., Baumgaertner S., Brenzel S., Havill H., Kozlowski A.,
RA Michael F., Mitchell K., Perrelli N.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 52-100, HYDROXYLATION AT PRO-60, AND
RP GAMMA-CARBOXYGLUTAMATION AT GLU-68; GLU-72 AND GLU-75.
RX PubMed=1068450; DOI=10.1073/pnas.73.10.3374;
RA Price P.A., Poser J.W., Raman N.;
RT "Primary structure of the gamma-carboxyglutamic acid-containing protein
RT from bovine bone.";
RL Proc. Natl. Acad. Sci. U.S.A. 73:3374-3375(1976).
RN [4]
RP STRUCTURE BY NMR OF 52-100, GAMMA-CARBOXYGLUTAMATION AT GLU-68; GLU-72 AND
RP GLU-75, CALCIUM-BINDING SITES, AND DISULFIDE BOND.
RX PubMed=12820886; DOI=10.1021/bi034470s;
RA Dowd T.L., Rosen J.F., Li L., Gundberg C.M.;
RT "The three-dimensional structure of bovine calcium ion-bound osteocalcin
RT using 1H NMR spectroscopy.";
RL Biochemistry 42:7769-7779(2003).
CC -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly
CC to apatite and calcium.
CC -!- SUBCELLULAR LOCATION: Secreted.
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:1068450,
CC ECO:0000269|PubMed:12820886}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; X53699; CAA37737.1; -; mRNA.
DR EMBL; X51700; CAA35997.1; -; mRNA.
DR EMBL; EF673278; ABU88822.1; -; Genomic_DNA.
DR PIR; S12653; GEBO.
DR RefSeq; NP_776674.1; NM_174249.2.
DR PDB; 1Q3M; NMR; -; A=52-100.
DR PDB; 4MZZ; X-ray; 1.88 A; A/B=68-100.
DR PDBsum; 1Q3M; -.
DR PDBsum; 4MZZ; -.
DR AlphaFoldDB; P02820; -.
DR SMR; P02820; -.
DR STRING; 9913.ENSBTAP00000047703; -.
DR PaxDb; P02820; -.
DR PRIDE; P02820; -.
DR GeneID; 281646; -.
DR KEGG; bta:281646; -.
DR CTD; 632; -.
DR eggNOG; ENOG502S85I; Eukaryota.
DR InParanoid; P02820; -.
DR OrthoDB; 1520921at2759; -.
DR EvolutionaryTrace; P02820; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS: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:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR GO; GO:0030500; P:regulation of bone mineralization; 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 InterPro; IPR002384; Osteocalcin/MGP.
DR PANTHER; PTHR14235; PTHR14235; 1.
DR PRINTS; PR00002; GLABONE.
DR SMART; SM00069; GLA; 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 3D-structure; Biomineralization; Calcium;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT PROPEP 24..51
FT /evidence="ECO:0000305|PubMed:1068450"
FT /id="PRO_0000011084"
FT CHAIN 52..100
FT /note="Osteocalcin"
FT /evidence="ECO:0000269|PubMed:1068450"
FT /id="PRO_0000011085"
FT DOMAIN 52..98
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12820886"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12820886"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12820886"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12820886"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12820886"
FT MOD_RES 60
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:1068450"
FT MOD_RES 68
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:1068450, ECO:0000269|PubMed:12820886"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:1068450, ECO:0000269|PubMed:12820886"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:1068450, ECO:0000269|PubMed:12820886"
FT DISULFID 74..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:12820886"
FT HELIX 69..75
FT /evidence="ECO:0007829|PDB:4MZZ"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:4MZZ"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:4MZZ"
SQ SEQUENCE 100 AA; 11042 MW; 73015D1681B26219 CRC64;
MRTPMLLALL ALATLCLAGR ADAKPGDAES GKGAAFVSKQ EGSEVVKRLR RYLDHWLGAP
APYPDPLEPK REVCELNPDC DELADHIGFQ EAYRRFYGPV
