ID   OSTCN_BISPR             Reviewed;          49 AA.
AC   P83489;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 66.
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   Bison priscus (Steppe wisent) (Steppe bison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bison.
OX   NCBI_TaxID=268291;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, HYDROXYLATION AT PRO-9, GAMMA-CARBOXYGLUTAMATION AT
RP   GLU-17; GLU-21 AND GLU-24, AND MASS SPECTROMETRY.
RC   TISSUE=Bone;
RA   Nielsen-Marsh C.M., Ostrom P.H., Gandhi H., Shapiro B., Cooper A.,
RA   Hauschka P.V., Collins M.J.;
RT   "Sequence preservation of osteocalcin protein and mitochondrial DNA in
RT   bison bones older than 55 ka.";
RL   Geology 30:1099-1102(2002).
CC   -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly
CC       to apatite and calcium (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02820}.
CC   -!- PTM: Gamma-carboxyglutamic acid residues are formed by vitamin K
CC       dependent carboxylation. These residues are essential for the binding
CC       of calcium (By similarity). {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=5590; Method=MALDI;
CC       Evidence={ECO:0000269|Ref.1};
CC   -!- MISCELLANEOUS: Sequence data obtained by MS from permafrost fossilized
CC       bones about 55.6 thousand years old.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=A small blast from the past
CC       - Issue 46 of May 2004;
CC       URL="https://web.expasy.org/spotlight/back_issues/046";
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DR   AlphaFoldDB; P83489; -.
DR   SMR; P83489; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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: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   Biomineralization; Calcium; Direct protein sequencing; Disulfide bond;
KW   Extinct organism protein; Gamma-carboxyglutamic acid; Hydroxylation;
KW   Metal-binding; Secreted.
FT   CHAIN           1..49
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000148895"
FT   DOMAIN          1..47
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   BINDING         17
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
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         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         30
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         9
FT                   /note="Hydroxyproline"
FT                   /evidence="ECO:0000269|Ref.1"
FT   MOD_RES         17
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|Ref.1"
FT   MOD_RES         21
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|Ref.1"
FT   MOD_RES         24
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT                   ECO:0000269|Ref.1"
FT   DISULFID        23..29
SQ   SEQUENCE   49 AA;  5575 MW;  718826015806CCBE CRC64;
     YLDHGLGAPA PYPDPLEPKR EVCELNPDCD ELADHIGFQE AYRRFYGPV