OSTCN_HOMNE
ID OSTCN_HOMNE Reviewed; 24 AA.
AC P84351;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Osteocalcin;
DE AltName: Full=Bone Gla protein;
DE Short=BGP;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein;
DE Flags: Fragment;
GN Name=BGLAP {ECO:0000250|UniProtKB:P02819};
OS Homo sapiens neanderthalensis (Neanderthal).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=63221;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE.
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 AlphaFoldDB; P84351; -.
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 InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR SUPFAM; SSF57630; SSF57630; 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; Metal-binding;
KW Secreted.
FT CHAIN <1..>24
FT /note="Osteocalcin"
FT /id="PRO_0000148899"
FT DOMAIN <1..>24
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 2
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 5
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 5
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 5
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 4..10
FT /evidence="ECO:0000250|UniProtKB:P02819,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:15753298"
FT NON_TER 24
FT /evidence="ECO:0000303|PubMed:15753298"
SQ SEQUENCE 24 AA; 2823 MW; 4882FA3A71F29E89 CRC64;
REVCELNPDC DELADHIGFQ EAYR