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 03-APR-2013, entry version 134.
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/en.136.6.2652;
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;
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).
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 -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC protein] phosphate.
CC -!- COFACTOR: Magnesium or manganese (By similarity).
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.
CC -!- SIMILARITY: Contains 1 GS domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 IPI; IPI00128193; -.
DR PIR; A56238; A56238.
DR RefSeq; NP_033888.2; NM_009758.4.
DR UniGene; Mm.237825; -.
DR ProteinModelPortal; P36895; -.
DR SMR; P36895; 55-143, 204-530.
DR DIP; DIP-5796N; -.
DR IntAct; P36895; 1.
DR PhosphoSite; P36895; -.
DR PaxDb; P36895; -.
DR PRIDE; P36895; -.
DR Ensembl; ENSMUST00000049005; ENSMUSP00000035900; ENSMUSG00000021796.
DR GeneID; 12166; -.
DR KEGG; mmu:12166; -.
DR CTD; 657; -.
DR MGI; MGI:1338938; Bmpr1a.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000230587; -.
DR HOVERGEN; HBG054502; -.
DR InParanoid; P36895; -.
DR KO; K04673; -.
DR OMA; LEVVCVK; -.
DR OrthoDB; EOG4F1X2X; -.
DR NextBio; 280531; -.
DR ArrayExpress; P36895; -.
DR Bgee; P36895; -.
DR CleanEx; MM_BMPR1A; -.
DR Genevestigator; P36895; -.
DR GermOnline; ENSMUSG00000021796; Mus musculus.
DR GO; GO:0005901; C:caveola; IEA:Compara.
DR GO; GO:0030425; C:dendrite; IEA:Compara.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IEA:Compara.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IDA:MGI.
DR GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IEA:InterPro.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0048589; P:developmental growth; IMP:MGI.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
DR GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR GO; GO:0048568; P:embryonic organ development; IMP:MGI.
DR GO; GO:0003272; P:endocardial cushion formation; IMP:MGI.
DR GO; GO:0060914; P:heart formation; IMP:MGI.
DR GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0006955; P:immune response; IEA:Compara.
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:0014032; P:neural crest cell development; IMP:MGI.
DR GO; GO:0021998; P:neural plate mediolateral regionalization; 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:0048352; P:paraxial mesoderm structural organization; IMP:MGI.
DR GO; GO:0021983; P:pituitary gland development; IMP:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Compara.
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; IEA:Compara.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IEA:Compara.
DR GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IEA:Compara.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA: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; IPR000472; Activin_rcpt.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_cat_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR003605; TGF_beta_rcpt_GS.
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; Kinase_like; 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 Potential.
FT CHAIN 24 532 Bone morphogenetic protein receptor type-
FT 1A.
FT /FTId=PRO_0000024411.
FT TOPO_DOM 24 152 Extracellular (Potential).
FT TRANSMEM 153 176 Helical; (Potential).
FT TOPO_DOM 177 532 Cytoplasmic (Potential).
FT DOMAIN 204 233 GS.
FT DOMAIN 234 525 Protein kinase.
FT NP_BIND 240 248 ATP (By similarity).
FT REGION 107 109 Mediates specificity for BMP ligand (By
FT similarity).
FT ACT_SITE 362 362 Proton acceptor (By similarity).
FT BINDING 261 261 ATP (By similarity).
FT CARBOHYD 73 73 N-linked (GlcNAc...) (Potential).
FT DISULFID 61 82 By similarity.
FT DISULFID 63 67 By similarity.
FT DISULFID 76 100 By similarity.
FT DISULFID 110 124 By similarity.
FT DISULFID 125 130 By similarity.
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
//
