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Database: UniProt
Entry: P36895
LinkDB: P36895
Original site: P36895 
ID   BMR1A_MOUSE             Reviewed;         532 AA.
AC   P36895;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   22-JUL-2015, entry version 157.
DE   RecName: Full=Bone morphogenetic protein receptor type-1A;
DE            Short=BMP type-1A receptor;
DE            Short=BMPR-1A;
DE            EC=2.7.11.30;
DE   AltName: Full=Activin receptor-like kinase 3;
DE            Short=ALK-3;
DE   AltName: Full=BMP-2/BMP-4 receptor;
DE   AltName: Full=Serine/threonine-protein kinase receptor R5;
DE            Short=SKR5;
DE   AltName: CD_antigen=CD292;
DE   Flags: Precursor;
GN   Name=Bmpr1a; Synonyms=Acvrlk3, Bmpr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss; TISSUE=Embryo;
RX   PubMed=7750489; DOI=10.1210/endo.136.6.7750489;
RA   Dewulf N., Verschueren K., Lonnoy O., Moren A., Grimsby S.,
RA   Spiegle K., Miyazono K., Huylebroeck D., ten Dijke P.;
RT   "Distinct spatial and temporal expression patterns of two type I
RT   receptors for bone morphogenetic proteins during mouse
RT   embryogenesis.";
RL   Endocrinology 136:2652-2663(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7937936; DOI=10.1073/pnas.91.22.10255;
RA   Suzuki A., Thies R.S., Yamaji N., Song J.J., Wozney J., Murakami K.,
RA   Kung H.;
RT   "A truncated bone morphogenetic protein receptor affects dorsal-
RT   ventral patterning in the early Xenopus embryo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:10255-10259(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8065329; DOI=10.1128/MCB.14.9.5961;
RA   Koenig B.B., Cook J.S., Wolsing D.H., Ting J., Tiesman J.P.,
RA   Correa P.E., Olson C.A., Pecquet A.L., Ventura F., Grant R.A.,
RA   Chen G., Wrana J.L., Massague J., Rosenbaum J.S.;
RT   "Characterization and cloning of a receptor for BMP-2 and BMP-4 from
RT   NIH 3T3 cells.";
RL   Mol. Cell. Biol. 14:5961-5974(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=24098149; DOI=10.1371/journal.pgen.1003846;
RA   Degenkolbe E., Konig J., Zimmer J., Walther M., Reissner C.,
RA   Nickel J., Ploger F., Raspopovic J., Sharpe J., Dathe K., Hecht J.T.,
RA   Mundlos S., Doelken S.C., Seemann P.;
RT   "A GDF5 point mutation strikes twice--causing BDA1 and SYNS2.";
RL   PLoS Genet. 9:E1003846-E1003846(2013).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Receptor for BMP-2 and BMP-4.
CC       Positively regulates chondrocyte differentiation through GDF5
CC       interaction (PubMed:24098149). {ECO:0000269|PubMed:24098149}.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with low affinity with GDF5; positively
CC       regulates chondrocyte differentiation.
CC       {ECO:0000250|UniProtKB:P36894}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 GS domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00585}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; Z23154; CAA80678.1; -; mRNA.
DR   EMBL; D16250; BAA03769.1; -; mRNA.
DR   EMBL; U04672; AAA21514.1; -; mRNA.
DR   EMBL; BC042611; AAH42611.1; -; mRNA.
DR   CCDS; CCDS26938.1; -.
DR   PIR; A56238; A56238.
DR   RefSeq; NP_033888.2; NM_009758.4.
DR   RefSeq; XP_006518532.1; XM_006518469.2.
DR   RefSeq; XP_006518533.1; XM_006518470.2.
DR   UniGene; Mm.237825; -.
DR   ProteinModelPortal; P36895; -.
DR   SMR; P36895; 55-143, 204-530.
DR   BioGrid; 198371; 4.
DR   DIP; DIP-5796N; -.
DR   IntAct; P36895; 1.
DR   STRING; 10090.ENSMUSP00000035900; -.
DR   BindingDB; P36895; -.
DR   GuidetoPHARMACOLOGY; 1786; -.
DR   PhosphoSite; P36895; -.
DR   MaxQB; P36895; -.
DR   PaxDb; P36895; -.
DR   PRIDE; P36895; -.
DR   Ensembl; ENSMUST00000049005; ENSMUSP00000035900; ENSMUSG00000021796.
DR   GeneID; 12166; -.
DR   KEGG; mmu:12166; -.
DR   UCSC; uc007taw.1; mouse.
DR   CTD; 657; -.
DR   MGI; MGI:1338938; Bmpr1a.
DR   eggNOG; COG0515; -.
DR   GeneTree; ENSGT00760000118876; -.
DR   HOGENOM; HOG000230587; -.
DR   HOVERGEN; HBG054502; -.
DR   InParanoid; P36895; -.
DR   KO; K04673; -.
DR   OMA; CYNRDLE; -.
DR   OrthoDB; EOG7Q8CN3; -.
DR   PhylomeDB; P36895; -.
DR   TreeFam; TF314724; -.
DR   BRENDA; 2.7.10.2; 3474.
DR   Reactome; REACT_334226; Signaling by BMP.
DR   NextBio; 280531; -.
DR   PRO; PR:P36895; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   Bgee; P36895; -.
DR   CleanEx; MM_BMPR1A; -.
DR   ExpressionAtlas; P36895; baseline and differential.
DR   Genevisible; P36895; MM.
DR   GO; GO:0005901; C:caveola; IEA:Ensembl.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0001948; F:glycoprotein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR   GO; GO:0004702; F:receptor signaling protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:MGI.
DR   GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IGI:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
DR   GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR   GO; GO:0048598; P:embryonic morphogenesis; IMP:MGI.
DR   GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR   GO; GO:0003272; P:endocardial cushion formation; IMP:MGI.
DR   GO; GO:0007492; P:endoderm development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0060914; P:heart formation; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0006955; P:immune response; ISO:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0048368; P:lateral mesoderm development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0048382; P:mesendoderm development; IMP:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0001880; P:Mullerian duct regression; IMP:MGI.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0014032; P:neural crest cell development; IMP:MGI.
DR   GO; GO:0021998; P:neural plate mediolateral regionalization; IMP:MGI.
DR   GO; GO:0060896; P:neural plate pattern specification; IMP:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR   GO; GO:0060021; P:palate development; IMP:MGI.
DR   GO; GO:0048339; P:paraxial mesoderm development; IMP:MGI.
DR   GO; GO:0048352; P:paraxial mesoderm structural organization; IMP:MGI.
DR   GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR   GO; GO:0021983; P:pituitary gland development; IMP:MGI.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
DR   GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
DR   GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR   GO; GO:2000772; P:regulation of cellular senescence; IGI:MGI.
DR   GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IGI:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   GO; GO:0019827; P:stem cell maintenance; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR000472; TFB_recept_I/II_C.
DR   InterPro; IPR003605; TGF_beta_rcpt_GS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Disulfide bond; Glycoprotein; Kinase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Receptor; Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    532       Bone morphogenetic protein receptor type-
FT                                1A.
FT                                /FTId=PRO_0000024411.
FT   TOPO_DOM     24    152       Extracellular. {ECO:0000255}.
FT   TRANSMEM    153    176       Helical. {ECO:0000255}.
FT   TOPO_DOM    177    532       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      204    233       GS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00585}.
FT   DOMAIN      234    525       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     240    248       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      107    109       Mediates specificity for BMP ligand.
FT                                {ECO:0000250}.
FT   ACT_SITE    362    362       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     261    261       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD     73     73       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     61     82       {ECO:0000250}.
FT   DISULFID     63     67       {ECO:0000250}.
FT   DISULFID     76    100       {ECO:0000250}.
FT   DISULFID    110    124       {ECO:0000250}.
FT   DISULFID    125    130       {ECO:0000250}.
SQ   SEQUENCE   532 AA;  60063 MW;  70CC83CFB07CE9D5 CRC64;
     MTQLYTYIRL LGACLFIISH VQGQNLDSML HGTGMKSDLD QKKPENGVTL APEDTLPFLK
     CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLTSGC MKYEGSDFQC KDSPKAQLRR
     TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRWLVVLISM AVCIVAMIIF SSCFCYKHYC
     KSISSRGRYN RDLEQDEAFI PVGESLKDLI DQSQSSGSGS GLPLLVQRTI AKQIQMVRQV
     GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT VLMRHENILG FIAADIKGTG
     SWTQLYLITD YHENGSLYDF LKCATLDTRA LLKLAYSAAC GLCHLHTEIY GTQGKPAIAH
     RDLKSKNILI KKNGSCCIAD LGLAVKFNSD TNEVDIPLNT RVGTKRYMAP EVLDESLNKN
     HFQPYIMADI YSFGLIIWEM ARRCITGGIV EEYQLPYYNM VPSDPSYEDM REVVCVKRLR
     PIVSNRWNSD ECLRAVLKLM SECWAHNPAS RLTALRIKKT LAKMVESQDV KI
//
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