OSTC2_MOUSE
ID OSTC2_MOUSE Reviewed; 95 AA.
AC P86547; P04641;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Osteocalcin-2;
DE AltName: Full=Bone Gla protein 2;
DE Short=BGP2;
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein 2;
DE Flags: Precursor;
GN Name=Bglap2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3019668; DOI=10.1002/j.1460-2075.1986.tb04440.x;
RA Celeste A.J., Buecker J.L., Kriz R., Wang E.A., Wozney J.M.;
RT "Isolation of the human gene for bone gla protein utilizing mouse and rat
RT cDNA clones.";
RL EMBO J. 5:1885-1890(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8243336; DOI=10.1210/endo.133.6.8243336;
RA Rahman S., Oberdorf A., Montecino M., Tanhauser S.M., Lian J.B.,
RA Stein G.S., Laipis P.J., Stein J.L.;
RT "Multiple copies of the bone-specific osteocalcin gene in mouse and rat.";
RL Endocrinology 133:3050-3053(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8288580; DOI=10.1016/s0021-9258(17)42240-x;
RA Desbois C., Hogue D.A., Karsenty G.;
RT "The mouse osteocalcin gene cluster contains three genes with two separate
RT spatial and temporal patterns of expression.";
RL J. Biol. Chem. 269:1183-1190(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Constitutes 1-2% of the total bone protein. It binds strongly
CC to apatite and calcium.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Bone.
CC -!- PTM: Gamma-carboxyglutamate residues are formed by vitamin K dependent
CC carboxylation. These residues are essential for the binding of calcium.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; X04142; CAA27762.1; -; mRNA.
DR EMBL; S67455; AAB29145.1; -; Genomic_DNA.
DR EMBL; L24429; AAA39854.1; -; Genomic_DNA.
DR EMBL; AC102388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS17473.1; -.
DR PIR; B25471; B25471.
DR RefSeq; NP_001027469.2; NM_001032298.3.
DR AlphaFoldDB; P86547; -.
DR SMR; P86547; -.
DR STRING; 10090.ENSMUSP00000096555; -.
DR PaxDb; P86547; -.
DR PRIDE; P86547; -.
DR DNASU; 12097; -.
DR Ensembl; ENSMUST00000098956; ENSMUSP00000096555; ENSMUSG00000074486.
DR GeneID; 12097; -.
DR KEGG; mmu:12097; -.
DR UCSC; uc008pux.1; mouse.
DR CTD; 12097; -.
DR MGI; MGI:88157; Bglap2.
DR VEuPathDB; HostDB:ENSMUSG00000074486; -.
DR eggNOG; ENOG502S85I; Eukaryota.
DR GeneTree; ENSGT00410000026290; -.
DR HOGENOM; CLU_160110_0_0_1; -.
DR InParanoid; P86547; -.
DR OMA; PQREVCE; -.
DR OrthoDB; 1520921at2759; -.
DR PhylomeDB; P86547; -.
DR TreeFam; TF330920; -.
DR Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR BioGRID-ORCS; 12097; 2 hits in 34 CRISPR screens.
DR PRO; PR:P86547; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P86547; protein.
DR Bgee; ENSMUSG00000074486; Expressed in esophagus and 57 other tissues.
DR Genevisible; P86547; MM.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0046848; F:hydroxyapatite binding; IDA:MGI.
DR GO; GO:0008147; F:structural constituent of bone; ISO:MGI.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0060348; P:bone development; IBA:GO_Central.
DR GO; GO:0044242; P:cellular lipid catabolic process; IMP:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IBA:GO_Central.
DR GO; GO:0031016; P:pancreas development; IMP:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
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 GO; GO:0044342; P:type B pancreatic cell proliferation; IMP:MGI.
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 2: Evidence at transcript level;
KW Biomineralization; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; Gamma-carboxyglutamic acid; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000305"
FT PROPEP 24..49
FT /evidence="ECO:0000305"
FT /id="PRO_0000395312"
FT CHAIN 50..95
FT /note="Osteocalcin-2"
FT /id="PRO_0000395313"
FT DOMAIN 46..92
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
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 DISULFID 68..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT CONFLICT 23
FT /note="A -> P (in Ref. 1; CAA27762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 95 AA; 10459 MW; D4AA611134805D9B CRC64;
MRTLSLLTLL ALAALCLSDL TDAKPSGPES DKAFMSKQEG NKVVNRLRRY LGASVPSPDP
LEPTREQCEL NPACDELSDQ YGLKTAYKRI YGITI
