OSTCN_PIG
ID OSTCN_PIG Reviewed; 49 AA.
AC Q8HYY9;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Osteocalcin;
DE AltName: Full=Bone Gla protein;
DE Short=BGP;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein;
GN Name=BGLAP;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, HYDROXYLATION AT PRO-9, AND GAMMA-CARBOXYGLUTAMATION AT
RP GLU-17; GLU-21 AND GLU-24.
RC TISSUE=Bone;
RX PubMed=6332627;
RA Huq N.L., Teh L.-C., Christie D.L., Chapman G.E.;
RT "The amino acid sequences of goat, pig and wallaby osteocalcins.";
RL Biochem. Int. 8:521-527(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-49.
RA Laize V., Cancela M.L.;
RT "Identification of Sus scrofa osteocalcin by comparative genomics.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), GAMMA-CARBOXYGLUTAMATION AT GLU-17;
RP GLU-21 AND GLU-24, AND DISULFIDE BOND.
RX PubMed=14586470; DOI=10.1038/nature02079;
RA Hoang Q.Q., Sicheri F., Howard A.J., Yang D.S.C.;
RT "Bone recognition mechanism of porcine osteocalcin from crystal
RT structure.";
RL Nature 425:977-980(2003).
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 {ECO:0000255|PROSITE-ProRule:PRU00463, ECO:0000269|PubMed:14586470,
CC ECO:0000269|PubMed:6332627}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; AY150038; AAN73020.1; -; mRNA.
DR PDB; 1Q8H; X-ray; 2.00 A; A=1-49.
DR PDBsum; 1Q8H; -.
DR AlphaFoldDB; Q8HYY9; -.
DR SMR; Q8HYY9; -.
DR STRING; 9823.ENSSSCP00000006919; -.
DR PaxDb; Q8HYY9; -.
DR eggNOG; ENOG502S85I; Eukaryota.
DR HOGENOM; CLU_160110_0_0_1; -.
DR InParanoid; Q8HYY9; -.
DR EvolutionaryTrace; Q8HYY9; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q8HYY9; SS.
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 DisProt; DP01982; -.
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 3D-structure; Biomineralization; Calcium; Direct protein sequencing;
KW Disulfide bond; Gamma-carboxyglutamic acid; Hydroxylation; Metal-binding;
KW Reference proteome; Secreted.
FT CHAIN 1..49
FT /note="Osteocalcin"
FT /id="PRO_0000148903"
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"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 24
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 30
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:6332627"
FT MOD_RES 17
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14586470, ECO:0000269|PubMed:6332627"
FT MOD_RES 21
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14586470, ECO:0000269|PubMed:6332627"
FT MOD_RES 24
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14586470, ECO:0000269|PubMed:6332627"
FT DISULFID 23..29
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:14586470"
FT HELIX 17..25
FT /evidence="ECO:0007829|PDB:1Q8H"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:1Q8H"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:1Q8H"
SQ SEQUENCE 49 AA; 5591 MW; BABF16015806D42F CRC64;
YLDHGLGAPA PYPDPLEPRR EVCELNPDCD ELADHIGFQE AYRRFYGIA
