OSTCN_RAT
ID OSTCN_RAT Reviewed; 99 AA.
AC P04640;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 148.
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; Synonyms=Bglap2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3019668; DOI=10.1002/j.1460-2075.1986.tb04440.x;
RA Celeste A.J., Buecker J.L., Kriz R., Wang E.A., Wozney J.M.;
RT "Isolation of the human gene for bone gla protein utilizing mouse and rat
RT cDNA clones.";
RL EMBO J. 5:1885-1890(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND HYDROXYLATION AT PRO-58.
RX PubMed=3875856; DOI=10.1073/pnas.82.18.6109;
RA Pan L.C., Price P.A.;
RT "The propeptide of rat bone gamma-carboxyglutamic acid protein shares
RT homology with other vitamin K-dependent protein precursors.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6109-6113(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3265336; DOI=10.1021/bi00423a003;
RA Yoon K., Rutledge S.J.C., Buenaga R.F., Rodan G.A.;
RT "Characterization of the rat osteocalcin gene: stimulation of promoter
RT activity by 1,25-dihydroxyvitamin D3.";
RL Biochemistry 27:8521-8526(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2785907; DOI=10.1089/dna.1.1989.8.213;
RA Theofan G., Haberstroh L.M., Price P.A.;
RT "Molecular structure of the rat bone Gla protein gene and identification of
RT putative regulatory elements.";
RL DNA 8:213-221(1989).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2784002; DOI=10.1073/pnas.86.4.1143;
RA Lian J., Stewart C., Puchacz E., Mackowiak S., Shalhoub V., Collart D.,
RA Zambetti G., Stein G.;
RT "Structure of the rat osteocalcin gene and regulation of vitamin D-
RT dependent expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:1143-1147(1989).
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 -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; X04141; CAA27761.1; -; mRNA.
DR EMBL; M11777; AAA40816.1; -; mRNA.
DR EMBL; M23637; AAA41761.1; -; Genomic_DNA.
DR EMBL; M25490; AAA53280.1; -; Genomic_DNA.
DR EMBL; J04500; AAA41764.1; -; Genomic_DNA.
DR PIR; A31856; GERT.
DR RefSeq; NP_038200.1; NM_013414.1.
DR RefSeq; XP_006232656.1; XM_006232594.3.
DR AlphaFoldDB; P04640; -.
DR SMR; P04640; -.
DR STRING; 10116.ENSRNOP00000026530; -.
DR PaxDb; P04640; -.
DR Ensembl; ENSRNOT00000026530; ENSRNOP00000026530; ENSRNOG00000019607.
DR GeneID; 25295; -.
DR KEGG; rno:25295; -.
DR UCSC; RGD:2206; rat.
DR CTD; 632; -.
DR RGD; 2206; Bglap.
DR eggNOG; ENOG502S85I; Eukaryota.
DR GeneTree; ENSGT00410000026290; -.
DR HOGENOM; CLU_160110_0_0_1; -.
DR InParanoid; P04640; -.
DR OMA; PQREVCE; -.
DR OrthoDB; 1520921at2759; -.
DR PhylomeDB; P04640; -.
DR TreeFam; TF330920; -.
DR Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR PRO; PR:P04640; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000019607; Expressed in thymus and 11 other tissues.
DR Genevisible; P04640; RN.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IEP:RGD.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:0042476; P:odontogenesis; IEP:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0002076; P:osteoblast development; IEP:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:RGD.
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:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0033594; P:response to hydroxyisoflavone; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0033280; P:response to vitamin D; ISO:RGD.
DR GO; GO:0032571; P:response to vitamin K; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0010043; P:response to zinc ion; IEP:RGD.
DR GO; GO:0048863; P:stem cell differentiation; IEP:RGD.
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; 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..49
FT /evidence="ECO:0000305"
FT /id="PRO_0000011092"
FT CHAIN 50..99
FT /note="Osteocalcin"
FT /id="PRO_0000011093"
FT DOMAIN 50..96
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3875856"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P02818,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 70
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 73
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 72..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
SQ SEQUENCE 99 AA; 10927 MW; 7F18F1866D4E4388 CRC64;
MRTLSLLTLL ALTAFCLSDL AGAKPSDSES DKAFMSKQEG SKVVNRLRRY LNNGLGAPAP
YPDPLEPHRE VCELNPNCDE LADHIGFQDA YKRIYGTTV
