OSTR_MOUSE
ID OSTR_MOUSE Reviewed; 95 AA.
AC P54615; Q78H72;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Osteocalcin-related protein {ECO:0000303|PubMed:8288580};
DE AltName: Full=Gamma-carboxyglutamic acid-containing protein 3 {ECO:0000305};
DE AltName: Full=Nephrocalcin {ECO:0000303|PubMed:8288580};
DE AltName: Full=OC-X {ECO:0000312|MGI:MGI:88155};
DE Flags: Precursor;
GN Name=Bglap3 {ECO:0000312|MGI:MGI:88155};
GN Synonyms=Bglap-rs1 {ECO:0000312|MGI:MGI:88155};
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
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 [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.
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Yotov W.V., St Arnaud R.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Salivary gland {ECO:0000312|EMBL:AAH31815.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Binds strongly to apatite and calcium.
CC {ECO:0000250|UniProtKB:P02820}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney and lung, but not in bone.
CC {ECO:0000269|PubMed:8288580}.
CC -!- PTM: Gamma-carboxyglutamic acid residues are formed by vitamin K
CC dependent carboxylation. These residues are essential for the binding
CC of calcium. {ECO:0000250|UniProtKB:P02820}.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000305}.
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DR EMBL; L24430; AAA39855.1; -; Genomic_DNA.
DR EMBL; S67456; AAB29146.1; -; Genomic_DNA.
DR EMBL; U11541; AAB60445.1; -; Unassigned_DNA.
DR EMBL; BC031815; AAH31815.1; -; mRNA.
DR EMBL; BC055868; AAH55868.1; -; mRNA.
DR EMBL; BC100687; AAI00688.1; -; mRNA.
DR EMBL; BC101948; AAI01949.1; -; mRNA.
DR EMBL; BC141238; AAI41239.1; -; mRNA.
DR EMBL; BC145565; AAI45566.1; -; mRNA.
DR CCDS; CCDS17472.1; -.
DR PIR; I61188; I61188.
DR RefSeq; NP_001292377.1; NM_001305448.1.
DR RefSeq; NP_001292378.1; NM_001305449.1.
DR RefSeq; NP_001292379.1; NM_001305450.1.
DR RefSeq; NP_112736.3; NM_031368.5.
DR AlphaFoldDB; P54615; -.
DR SMR; P54615; -.
DR STRING; 10090.ENSMUSP00000074965; -.
DR PaxDb; P54615; -.
DR PRIDE; P54615; -.
DR DNASU; 12095; -.
DR Ensembl; ENSMUST00000075523; ENSMUSP00000074965; ENSMUSG00000074489.
DR Ensembl; ENSMUST00000107542; ENSMUSP00000103166; ENSMUSG00000074489.
DR Ensembl; ENSMUST00000107543; ENSMUSP00000103167; ENSMUSG00000074489.
DR GeneID; 12095; -.
DR KEGG; mmu:12095; -.
DR UCSC; uc008puv.3; mouse.
DR UCSC; uc012cru.2; mouse.
DR CTD; 12095; -.
DR MGI; MGI:88155; Bglap3.
DR VEuPathDB; HostDB:ENSMUSG00000074489; -.
DR eggNOG; ENOG502S85I; Eukaryota.
DR GeneTree; ENSGT00410000026290; -.
DR HOGENOM; CLU_160110_0_0_1; -.
DR InParanoid; P54615; -.
DR OMA; CSAPLPW; -.
DR OrthoDB; 1520921at2759; -.
DR PhylomeDB; P54615; -.
DR TreeFam; TF330920; -.
DR BioGRID-ORCS; 12095; 0 hits in 53 CRISPR screens.
DR ChiTaRS; Bglap3; mouse.
DR PRO; PR:P54615; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P54615; protein.
DR Bgee; ENSMUSG00000074489; Expressed in esophagus and 73 other tissues.
DR Genevisible; P54615; 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; ISO: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; IBA:GO_Central.
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: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 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:0000255"
FT PROPEP 24..49
FT /evidence="ECO:0000305"
FT /id="PRO_0000011090"
FT CHAIN 50..95
FT /note="Osteocalcin-related protein"
FT /id="PRO_0000011091"
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|UniProtKB:P02820"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 69
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P02820"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DISULFID 68..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT CONFLICT 26
FT /note="T -> S (in Ref. 4; AAH31815/AAH55868/AAI00688/
FT AAI01949/AAI41239/AAI45566)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 95 AA; 10459 MW; 231968AA8B55848E CRC64;
MRTLSLLTLL ALAALCLSDL TDATPTGPES DKAFMSKQEG NKVVNRLRRY LGASVPSPDP
LEPTRELCEL DPACDELSNQ YGLKTAYRRI YGITI
