BMPR2_MOUSE
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 03-AUG-2022, entry version 193.
DE RecName: Full=Bone morphogenetic protein receptor type-2;
DE Short=BMP type-2 receptor;
DE Short=BMPR-2;
DE EC=2.7.11.30;
DE AltName: Full=BRK-3;
DE AltName: Full=Bone morphogenetic protein receptor type II;
DE Short=BMP type II receptor;
DE Short=BMPR-II;
DE Flags: Precursor;
GN Name=Bmpr2;
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 [MRNA].
RX 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 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.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680; SER-681 AND SER-843, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION.
RX PubMed=23527555; DOI=10.1111/febs.12256;
RA Wang S.S., Huang H.Y., Chen S.Z., Li X., Zhang W.T., Tang Q.Q.;
RT "Gdf6 induces commitment of pluripotent mesenchymal C3H10T1/2 cells to the
RT adipocyte lineage.";
RL FEBS J. 280:2644-2651(2013).
CC -!- FUNCTION: On ligand binding, forms a receptor complex consisting of two
CC type II and two type I transmembrane serine/threonine kinases. Type II
CC receptors phosphorylate and activate type I receptors which
CC autophosphorylate, then bind and activate SMAD transcriptional
CC regulators. Binds to BMP7, BMP2 and, less efficiently, BMP4. Binding is
CC weak but enhanced by the presence of type I receptors for BMPs.
CC Mediates induction of adipogenesis by GDF6 (PubMed:23527555).
CC {ECO:0000269|PubMed:23527555}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-
CC L-threonyl-[receptor-protein]; Xref=Rhea:RHEA:44880, Rhea:RHEA-
CC COMP:11024, Rhea:RHEA-COMP:11025, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977,
CC ChEBI:CHEBI:456216; EC=2.7.11.30;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[receptor-protein] = ADP + H(+) + O-phospho-L-
CC seryl-[receptor-protein]; Xref=Rhea:RHEA:18673, Rhea:RHEA-COMP:11022,
CC Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC EC=2.7.11.30;
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 GDF5. Interacts with BMP4. Interacts with
CC SCUBE3. {ECO:0000250|UniProtKB:Q13873}.
CC -!- INTERACTION:
CC O35607; P0C605: Prkg1; NbExp=4; IntAct=EBI-527224, EBI-6991999;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q13873};
CC Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF003942; AAB63042.1; -; mRNA.
DR EMBL; U78048; AAB87638.1; -; mRNA.
DR CCDS; CCDS35588.1; -.
DR PIR; JC5527; JC5527.
DR RefSeq; NP_031587.1; NM_007561.4.
DR AlphaFoldDB; O35607; -.
DR BMRB; O35607; -.
DR SMR; O35607; -.
DR BioGRID; 198373; 13.
DR ELM; O35607; -.
DR IntAct; O35607; 3.
DR MINT; O35607; -.
DR STRING; 10090.ENSMUSP00000084701; -.
DR GlyConnect; 2160; 1 N-Linked glycan (1 site).
DR GlyGen; O35607; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; O35607; -.
DR PhosphoSitePlus; O35607; -.
DR SwissPalm; O35607; -.
DR MaxQB; O35607; -.
DR PaxDb; O35607; -.
DR PeptideAtlas; O35607; -.
DR PRIDE; O35607; -.
DR ProteomicsDB; 265314; -.
DR Antibodypedia; 19946; 536 antibodies from 37 providers.
DR DNASU; 12168; -.
DR Ensembl; ENSMUST00000087435; ENSMUSP00000084701; ENSMUSG00000067336.
DR GeneID; 12168; -.
DR KEGG; mmu:12168; -.
DR UCSC; uc007bdz.2; mouse.
DR CTD; 659; -.
DR MGI; MGI:1095407; Bmpr2.
DR VEuPathDB; HostDB:ENSMUSG00000067336; -.
DR eggNOG; KOG3653; Eukaryota.
DR GeneTree; ENSGT00940000156449; -.
DR HOGENOM; CLU_013015_0_0_1; -.
DR InParanoid; O35607; -.
DR OMA; RDTHVNG; -.
DR OrthoDB; 390511at2759; -.
DR PhylomeDB; O35607; -.
DR TreeFam; TF314724; -.
DR BRENDA; 2.7.10.2; 3474.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR BioGRID-ORCS; 12168; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Bmpr2; mouse.
DR PRO; PR:O35607; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O35607; protein.
DR Bgee; ENSMUSG00000067336; Expressed in cumulus cell and 235 other tissues.
DR Genevisible; O35607; MM.
DR GO; GO:0005912; C:adherens junction; ISO:MGI.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0036122; F:BMP binding; IDA:MGI.
DR GO; GO:0098821; F:BMP receptor activity; IDA:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0019838; F:growth factor binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019211; F:phosphatase activator activity; IMP:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:MGI.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR GO; GO:0030546; F:signaling receptor activator activity; IDA:MGI.
DR GO; GO:0005024; F:transforming growth factor beta receptor activity; IBA:GO_Central.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0003176; P:aortic valve development; IMP:BHF-UCL.
DR GO; GO:0060840; P:artery development; IMP:BHF-UCL.
DR GO; GO:0060413; P:atrial septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:BHF-UCL.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; ISO:MGI.
DR GO; GO:0003197; P:endocardial cushion development; IMP:BHF-UCL.
DR GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase.
DR GO; GO:0072577; P:endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0001935; P:endothelial cell proliferation; ISO:MGI.
DR GO; GO:0060173; P:limb development; IGI:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:BHF-UCL.
DR GO; GO:0001946; P:lymphangiogenesis; IMP:BHF-UCL.
DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; IMP:BHF-UCL.
DR GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR GO; GO:0003183; P:mitral valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0003252; P:negative regulation of cell proliferation involved in heart valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; ISO:MGI.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0051148; P:negative regulation of muscle cell differentiation; IDA:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0003151; P:outflow tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:BHF-UCL.
DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:BHF-UCL.
DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IMP:UniProtKB.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISO:MGI.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; IMP:BHF-UCL.
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 signal transduction; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0030166; P:proteoglycan biosynthetic process; ISS:AgBase.
DR GO; GO:0003177; P:pulmonary valve development; IMP:BHF-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0014916; P:regulation of lung blood pressure; IMP:BHF-UCL.
DR GO; GO:0061298; P:retina vasculature development in camera-type eye; IMP:BHF-UCL.
DR GO; GO:1905314; P:semi-lunar valve development; IMP:BHF-UCL.
DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; ISO:MGI.
DR GO; GO:0003186; P:tricuspid valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0060841; P:venous blood vessel development; IMP:BHF-UCL.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR Gene3D; 2.10.60.10; -; 1.
DR InterPro; IPR000472; Activin_recp.
DR InterPro; IPR015770; BMPR2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR045860; Snake_toxin-like_sf.
DR InterPro; IPR000333; TGFB_receptor.
DR PANTHER; PTHR23255; PTHR23255; 1.
DR PANTHER; PTHR23255:SF97; PTHR23255:SF97; 1.
DR Pfam; PF01064; Activin_recp; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57302; SSF57302; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Disulfide bond; Glycoprotein; Kinase;
KW Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Receptor; Reference proteome;
KW Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..1038
FT /note="Bone morphogenetic protein receptor type-2"
FT /id="PRO_0000024416"
FT TOPO_DOM 27..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..1038
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 203..504
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 593..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 209..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 230
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 280..282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 337..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13873"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13873"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..66
FT /evidence="ECO:0000250|UniProtKB:Q13873"
FT DISULFID 60..84
FT /evidence="ECO:0000250|UniProtKB:Q13873"
FT DISULFID 94..117
FT /evidence="ECO:0000250|UniProtKB:Q13873"
FT DISULFID 99..116
FT /evidence="ECO:0000250|UniProtKB:Q13873"
FT DISULFID 118..123
FT /evidence="ECO:0000250|UniProtKB:Q13873"
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
