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Bone morphogenetic protein receptor type-2 (BMP type-2 receptor) (BMPR-2) (EC 2.7.11.30) (BRK-3) (Bone morphogenetic protein receptor type II) (BMP type II receptor) (BMPR-II)

 BMPR2_MOUSE             Reviewed;        1038 AA.
O35607;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
18-JUL-2018, entry version 169.
RecName: Full=Bone morphogenetic protein receptor type-2;
Short=BMP type-2 receptor;
Short=BMPR-2;
EC=2.7.11.30;
AltName: Full=BRK-3;
AltName: Full=Bone morphogenetic protein receptor type II;
Short=BMP type II receptor;
Short=BMPR-II;
Flags: Precursor;
Name=Bmpr2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9207184; DOI=10.1006/bbrc.1997.6816;
Beppu H., Minowa O., Miyazono K., Kawabata M.;
"cDNA cloning and genomic organization of the mouse BMP type II
receptor.";
Biochem. Biophys. Res. Commun. 235:499-504(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Whitaker G.B., Koenig B.B., Ting J., Tiesman J.P., Limberg A.L.,
Grant R.A., Begley K.B., Rosenbaum J.S.;
"Identification of BMP receptor complexes with differential signaling
properties and ligand binding profiles.";
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; SER-681 AND
SER-843, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[4]
FUNCTION.
PubMed=23527555; DOI=10.1111/febs.12256;
Wang S.S., Huang H.Y., Chen S.Z., Li X., Zhang W.T., Tang Q.Q.;
"Gdf6 induces commitment of pluripotent mesenchymal C3H10T1/2 cells to
the adipocyte lineage.";
FEBS J. 280:2644-2651(2013).
-!- FUNCTION: On ligand binding, forms a receptor complex consisting
of two type II and two type I transmembrane serine/threonine
kinases. Type II receptors phosphorylate and activate type I
receptors which autophosphorylate, then bind and activate SMAD
transcriptional regulators. Binds to BMP7, BMP2 and, less
efficiently, BMP4. Binding is weak but enhanced by the presence of
type I receptors for BMPs. Mediates induction of adipogenesis by
GDF6 (PubMed:23527555). {ECO:0000269|PubMed:23527555}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with GDF5. {ECO:0000250|UniProtKB:Q13873}.
-!- INTERACTION:
P0C605:Prkg1; NbExp=4; IntAct=EBI-527224, EBI-6991999;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q13873}; Single-pass type I membrane
protein.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF003942; AAB63042.1; -; mRNA.
EMBL; U78048; AAB87638.1; -; mRNA.
CCDS; CCDS35588.1; -.
PIR; JC5527; JC5527.
RefSeq; NP_031587.1; NM_007561.4.
UniGene; Mm.391654; -.
UniGene; Mm.7106; -.
ProteinModelPortal; O35607; -.
SMR; O35607; -.
BioGrid; 198373; 4.
ELM; O35607; -.
IntAct; O35607; 4.
MINT; O35607; -.
STRING; 10090.ENSMUSP00000084701; -.
iPTMnet; O35607; -.
PhosphoSitePlus; O35607; -.
SwissPalm; O35607; -.
MaxQB; O35607; -.
PaxDb; O35607; -.
PeptideAtlas; O35607; -.
PRIDE; O35607; -.
DNASU; 12168; -.
Ensembl; ENSMUST00000087435; ENSMUSP00000084701; ENSMUSG00000067336.
GeneID; 12168; -.
KEGG; mmu:12168; -.
UCSC; uc007bdz.2; mouse.
CTD; 659; -.
MGI; MGI:1095407; Bmpr2.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000043088; -.
HOVERGEN; HBG050705; -.
InParanoid; O35607; -.
KO; K04671; -.
OMA; STEPLDC; -.
OrthoDB; EOG091G03YO; -.
PhylomeDB; O35607; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-201451; Signaling by BMP.
PRO; PR:O35607; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000067336; -.
Genevisible; O35607; MM.
GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0030425; C:dendrite; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0036122; F:BMP binding; ISO:MGI.
GO; GO:0098821; F:BMP receptor activity; IMP:UniProtKB.
GO; GO:0019838; F:growth factor binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
GO; GO:0060840; P:artery development; IMP:BHF-UCL.
GO; GO:0060413; P:atrial septum morphogenesis; IMP:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IMP:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
GO; GO:0002063; P:chondrocyte development; ISO:MGI.
GO; GO:0003197; P:endocardial cushion development; IMP:BHF-UCL.
GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase.
GO; GO:0072577; P:endothelial cell apoptotic process; ISO:MGI.
GO; GO:0001935; P:endothelial cell proliferation; ISO:MGI.
GO; GO:0060173; P:limb development; IGI:MGI.
GO; GO:0048286; P:lung alveolus development; IMP:BHF-UCL.
GO; GO:0001946; P:lymphangiogenesis; IMP:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
GO; GO:0001893; P:maternal placenta development; IMP:MGI.
GO; GO:0001707; P:mesoderm formation; IMP:MGI.
GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0003252; P:negative regulation of cell proliferation involved in heart valve morphogenesis; IMP:BHF-UCL.
GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISO:MGI.
GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:BHF-UCL.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:BHF-UCL.
GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase.
GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:0045778; P:positive regulation of ossification; IMP:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:MGI.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:AgBase.
GO; GO:0042127; P:regulation of cell proliferation; ISO:MGI.
GO; GO:0014916; P:regulation of lung blood pressure; IMP:BHF-UCL.
GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:BHF-UCL.
GO; GO:1905314; P:semi-lunar valve development; IMP:BHF-UCL.
GO; GO:0006366; P:transcription by RNA polymerase II; ISO:MGI.
GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:MGI.
GO; GO:0003186; P:tricuspid valve morphogenesis; IMP:BHF-UCL.
GO; GO:0060841; P:venous blood vessel development; IMP:BHF-UCL.
GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR015770; BMPR2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
PANTHER; PTHR23255:SF63; PTHR23255:SF63; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome;
Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1038 Bone morphogenetic protein receptor type-
2.
/FTId=PRO_0000024416.
TOPO_DOM 27 150 Extracellular. {ECO:0000255}.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TOPO_DOM 172 1038 Cytoplasmic. {ECO:0000255}.
DOMAIN 203 504 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 209 217 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 280 282 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 337 338 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 191 194 Poly-Ala.
COMPBIAS 547 550 Poly-Ser.
COMPBIAS 610 618 Poly-Thr.
COMPBIAS 901 908 Poly-Asn.
ACT_SITE 333 333 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 230 230 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 351 351 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 379 379 Phosphothreonine.
{ECO:0000250|UniProtKB:Q13873}.
MOD_RES 586 586 Phosphoserine.
{ECO:0000250|UniProtKB:Q13873}.
MOD_RES 680 680 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 681 681 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 843 843 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 55 55 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 126 126 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 34 66 {ECO:0000250|UniProtKB:Q13873}.
DISULFID 60 84 {ECO:0000250|UniProtKB:Q13873}.
DISULFID 94 117 {ECO:0000250|UniProtKB:Q13873}.
DISULFID 99 116 {ECO:0000250|UniProtKB:Q13873}.
DISULFID 118 123 {ECO:0000250|UniProtKB:Q13873}.
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


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