OSTCN_MACMU
ID OSTCN_MACMU Reviewed; 100 AA.
AC A2D670;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; DQ976876; ABM55163.1; -; Genomic_DNA.
DR RefSeq; NP_001074237.1; NM_001080768.1.
DR AlphaFoldDB; A2D670; -.
DR SMR; A2D670; -.
DR STRING; 9544.ENSMMUP00000000113; -.
DR Ensembl; ENSMMUT00000000124; ENSMMUP00000000113; ENSMMUG00000004902.
DR GeneID; 718296; -.
DR KEGG; mcc:718296; -.
DR CTD; 632; -.
DR VEuPathDB; HostDB:ENSMMUG00000004902; -.
DR eggNOG; ENOG502S85I; Eukaryota.
DR GeneTree; ENSGT00940000155399; -.
DR HOGENOM; CLU_160110_0_0_1; -.
DR InParanoid; A2D670; -.
DR OMA; PQREVCE; -.
DR OrthoDB; 1520921at2759; -.
DR TreeFam; TF330920; -.
DR Proteomes; UP000006718; Chromosome 1.
DR Bgee; ENSMMUG00000004902; Expressed in olfactory segment of nasal mucosa and 22 other tissues.
DR ExpressionAtlas; A2D670; baseline.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000818; C:nuclear MIS12/MIND complex; IBA:GO_Central.
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:0007059; P:chromosome segregation; 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 3: Inferred from homology;
KW Biomineralization; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000305"
FT PROPEP 24..51
FT /evidence="ECO:0000250"
FT /id="PRO_0000285412"
FT CHAIN 52..100
FT /note="Osteocalcin"
FT /id="PRO_0000285413"
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="3"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 60
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 68
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P02818,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 74..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 100 AA; 10967 MW; 1A19C5A6FCE2D255 CRC64;
MRALTLLALL ALATLCITGQ AGAKPSGAES SKGAAFVSKQ EGSEVVKRPR RYLYQWLGAP
APYPDPLEPK REVCELNPDC DELADHIGFQ EAYRRFYGPV
