ID BMPR2_MOUSE Reviewed; 1038 AA. AC O35607; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 22-JUL-2008, entry version 77. DE RecName: Full=Bone morphogenetic protein receptor type-2; DE EC=2.7.11.30; DE AltName: Full=Bone morphogenetic protein receptor type II; DE AltName: Full=BMP type II receptor; DE AltName: Full=BMPR-II; DE AltName: Full=BRK-3; DE Flags: Precursor; GN Name=Bmpr2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97350808; PubMed=9207184; DOI=10.1006/bbrc.1997.6816; RA Beppu H., Minowa O., Miyazono K., Kawabata M.; RT "cDNA cloning and genomic organization of the mouse BMP type II RT receptor."; RL Biochem. Biophys. Res. Commun. 235:499-504(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Whitaker G.B., Koenig B.B., Ting J., Tiesman J.P., Limberg A.L., RA Grant R.A., Begley K.B., Rosenbaum J.S.; RT "Identification of BMP receptor complexes with differential signaling RT properties and ligand binding profiles."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. 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. Binds to BMP-7, BMP-2 and, less CC efficiently, BMP-4. Binding is weak but enhanced by the presence CC of type I receptors for BMPs. 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr CC protein kinase family. TGFB receptor subfamily. 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; AF003942; AAB63042.1; -; mRNA. DR EMBL; U78048; AAB87638.1; -; mRNA. DR PIR; JC5527; JC5527. DR RefSeq; NP_031587.1; -. DR UniGene; Mm.391654; -. DR UniGene; Mm.466857; -. DR HSSP; P36897; 1IAS. DR SMR; O35607; 33-131. DR IntAct; O35607; -. DR PhosphoSite; O35607; -. DR Ensembl; ENSMUSG00000067336; Mus musculus. DR GeneID; 12168; -. DR KEGG; mmu:12168; -. DR MGI; MGI:1095407; Bmpr2. DR HOGENOM; O35607; -. DR HOVERGEN; O35607; -. DR ArrayExpress; O35607; -. DR GermOnline; ENSMUSG00000067336; Mus musculus. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0048286; P:alveolus development; IMP:UniProtKB. DR GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI. DR GO; GO:0030509; P:BMP signaling pathway; IMP:MGI. DR GO; GO:0001707; P:mesoderm formation; IMP:MGI. DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:UniProtKB. DR GO; GO:0014916; P:regulation of lung blood pressure; IMP:UniProtKB. DR GO; GO:0048010; P:vascular endothelial growth factor receptor...; IMP:UniProtKB. DR InterPro; IPR000472; Activin_rcpt. DR InterPro; IPR015770; BMPRII. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR PANTHER; PTHR23255:SF12; BMPRII; 1. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG. PE 2: Evidence at transcript level; KW ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; KW Metal-binding; Nucleotide-binding; Receptor; KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane. FT SIGNAL 1 26 Potential. FT CHAIN 27 1038 Bone morphogenetic protein receptor type- FT 2. FT /FTId=PRO_0000024416. FT TOPO_DOM 27 150 Extracellular (Potential). FT TRANSMEM 151 171 Potential. FT TOPO_DOM 172 1038 Cytoplasmic (Potential). FT DOMAIN 203 504 Protein kinase. FT NP_BIND 209 217 ATP (By similarity). FT COMPBIAS 191 194 Poly-Ala. FT COMPBIAS 547 550 Poly-Ser. FT COMPBIAS 610 618 Poly-Thr. FT COMPBIAS 901 908 Poly-Asn. FT ACT_SITE 333 333 Proton acceptor (By similarity). FT BINDING 230 230 ATP (By similarity). FT CARBOHYD 55 55 N-linked (GlcNAc...) (Potential). FT CARBOHYD 110 110 N-linked (GlcNAc...) (Potential). FT CARBOHYD 126 126 N-linked (GlcNAc...) (Potential). FT DISULFID 34 66 By similarity. FT DISULFID 94 117 By similarity. SQ SEQUENCE 1038 AA; 115020 MW; 4106945DC63250E1 CRC64; MTSSLHRPFR VPWLLWAVLL VSTTAASQNQ ERLCAFKDPY QQDLGIGESR ISHENGTILC SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV VTTTPPSIQN GTYRFCCCST DLCNVNFTEN FPPPDTTPLS PPHSFNRDET IIIALASVSV LAVLIVALCF GYRMLTGDRK QGLHSMNMME AAAAEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF INEKNIYRVP LMEHDNIARF IVGDERLTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGACVIS DFGLSMRLTG NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA LKQVDMYALG LIYWEVFMRC TDLFPGESVP DYQMAFQTEV GNHPTFEDMQ VLVSREKQRP KFPEAWKENS LAVRSLKETI EDCWDQDAEA RLTAQCAEER MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI GPYPDYSSSS YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETHL HATNVAQSIG PTPVCLQLTE EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS STSSSLLYPL IKLAVEVTGQ QDFTQAANGQ ACLIPDVPPA QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGNKHKSN LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRSHNVNSHA ATTQYANGAV PAGQAANIVA HRSQEMLQNQ FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT NSNNNNSNPC SEQDILTQGV TSTAADPGPS KPRRAQRPNS LDLSATNILD GSSIQIGEST QDGKSGSGEK IKRRVKTPYS LKRWRPSTWV ISTEPLDCEV NNNGSDRAVH SKSSTAVYLA EGGTATTTVS KDIGMNCL //