OSTCN_PANTR
ID OSTCN_PANTR Reviewed; 100 AA.
AC P84348; A2T714;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
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 {ECO:0000250|UniProtKB:P02819};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 52-100.
RC TISSUE=Bone {ECO:0000269|PubMed:15753298};
RX PubMed=15753298; DOI=10.1073/pnas.0500450102;
RA Nielsen-Marsh C.M., Richards M.P., Hauschka P.V., Thomas-Oates J.E.,
RA Trinkaus E., Pettit P.B., Karavanic I., Poinar H., Collins M.J.;
RT "Osteocalcin protein sequences of Neanderthals and modern primates.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4409-4413(2005).
CC -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly
CC to apatite and calcium. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; DQ977353; ABM91969.1; -; Genomic_DNA.
DR RefSeq; NP_001129100.1; NM_001135628.1.
DR RefSeq; XP_016784372.1; XM_016928883.1.
DR AlphaFoldDB; P84348; -.
DR SMR; P84348; -.
DR STRING; 9598.ENSPTRP00000002450; -.
DR PaxDb; P84348; -.
DR Ensembl; ENSPTRT00000002667; ENSPTRP00000002450; ENSPTRG00000041553.
DR GeneID; 100190891; -.
DR KEGG; ptr:100190891; -.
DR CTD; 632; -.
DR VGNC; VGNC:8149; BGLAP.
DR eggNOG; ENOG502S85I; Eukaryota.
DR GeneTree; ENSGT00410000026290; -.
DR HOGENOM; CLU_160110_0_0_1; -.
DR InParanoid; P84348; -.
DR OMA; PQREVCE; -.
DR OrthoDB; 1520921at2759; -.
DR TreeFam; TF330920; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000041553; Expressed in cerebellar cortex and 20 other tissues.
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 Biomineralization; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Gamma-carboxyglutamic acid;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000305"
FT PROPEP 24..51
FT /evidence="ECO:0000269|PubMed:15753298"
FT /id="PRO_0000285416"
FT CHAIN 52..100
FT /note="Osteocalcin"
FT /id="PRO_0000148902"
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 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; 4DF2A6046289CB71 CRC64;
MRALTLLALL ALAALCIAGQ AGAKPSGAES SKGAAFVSKQ EGSEVVKRPR RYLYQWLGAP
VPYPDTLEPR REVCELNPDC DELADHIGFQ EAYRRFYGPV
