ID   OSTCN_CAMHE             Reviewed;          42 AA.
AC   P86312;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 24.
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};
DE   Flags: Fragments;
GN   Name=BGLAP {ECO:0000250|UniProtKB:P02820};
OS   Camelops hesternus (Western camel) (Camelus hesternus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelops.
OX   NCBI_TaxID=647691;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND HYDROXYLATION AT PRO-9.
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   -!- MISCELLANEOUS: Sequence data obtained by MS from fossilized bones of
CC       about 21 thousand years old. {ECO:0000269|Ref.1}.
CC   -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC       {ECO:0000255}.
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DR   AlphaFoldDB; P86312; -.
DR   SMR; P86312; -.
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   InterPro; IPR035972; GLA-like_dom_SF.
DR   SUPFAM; SSF57630; SSF57630; 1.
PE   1: Evidence at protein level;
KW   Biomineralization; Calcium; Direct protein sequencing;
KW   Extinct organism protein; Gamma-carboxyglutamic acid; Hydroxylation;
KW   Metal-binding; Secreted.
FT   CHAIN           1..42
FT                   /note="Osteocalcin"
FT                   /id="PRO_0000378905"
FT   DOMAIN          1..40
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         23
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   NON_CONS        22..23
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   42 AA;  4817 MW;  04A182C69A5285A0 CRC64;
     YLDHGLGAPA PYVDPLEPKR EVDELADQMG FQEAYRRFYG TT