OSTCN_LAMGU
ID OSTCN_LAMGU Reviewed; 49 AA.
AC P86315;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Osteocalcin {ECO:0000303|Ref.1};
DE AltName: Full=Bone Gla protein {ECO:0000250|UniProtKB:P02820};
DE Short=BGP {ECO:0000250|UniProtKB:P02820};
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein {ECO:0000250|UniProtKB:P02820};
GN Name=BGLAP {ECO:0000250|UniProtKB:P02820};
OS Lama guanicoe (Guanaco) (Lama glama guanicoe).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Lama.
OX NCBI_TaxID=9840;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, HYDROXYLATION AT PRO-9, AND DISULFIDE BOND.
RC TISSUE=Bone {ECO:0000269|Ref.1};
RA Humpula J.F., Ostrom P.H., Gandhi H., Strahler J.R., Walker A.K.,
RA Stafford T.W. Jr., Smith J.J., Voorhies M.R., Corner R.G., Andrews P.C.;
RT "Investigation of the protein osteocalcin of Camelops hesternus: Sequence,
RT structure and phylogenetic implications.";
RL Geochim. Cosmochim. Acta 71:5956-5967(2007).
CC -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly
CC to apatite and calcium (By similarity). {ECO:0000250|UniProtKB:P02820}.
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|UniProtKB:P02820}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000255}.
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DR AlphaFoldDB; P86315; -.
DR SMR; P86315; -.
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 Gamma-carboxyglutamic acid; Hydroxylation; Metal-binding; Secreted.
FT CHAIN 1..49
FT /note="Osteocalcin"
FT /id="PRO_0000378906"
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|UniProtKB:P02820"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT MOD_RES 9
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|Ref.1"
FT MOD_RES 17
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P02818,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 21
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 24
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P83489,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 23..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|Ref.1"
SQ SEQUENCE 49 AA; 5592 MW; 72EEE6015DF99823 CRC64;
YLDHGLGAPA PYVDPLEPKR EVCELNPDCD ELADQMGFQE AYRRFYGTT
