ID BMPR2_HUMAN Reviewed; 1038 AA. AC Q13873; Q13161; Q16569; Q4ZG08; Q53SA5; Q585T8; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 26-FEB-2020, entry version 216. 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=Bone morphogenetic protein receptor type II; DE Short=BMP type II receptor; DE Short=BMPR-II; DE Flags: Precursor; GN Name=BMPR2; Synonyms=PPH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING. RC TISSUE=Kidney; RX PubMed=7791754; DOI=10.1128/mcb.15.7.3479; RA Liu F., Ventura F., Doody J., Massague J.; RT "Human type II receptor for bone morphogenic proteins (BMPs): extension of RT the two-kinase receptor model to the BMPs."; RL Mol. Cell. Biol. 15:3479-3486(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Substantia nigra; RX PubMed=7644468; DOI=10.1073/pnas.92.17.7632; RA Rosenzweig B.L., Imamura T., Okadome T., Cox G.N., Yamashita H., RA ten Dijke P., Heldin C., Miyazono K.; RT "Cloning and characterization of a human type II receptor for bone RT morphogenetic proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7632-7636(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Skin fibroblast; RX PubMed=7673243; DOI=10.1074/jbc.270.38.22522; RA Nohno T., Ishikawa T., Saito T., Hosokawa K., Noji S., Wosing D.H., RA Rosenbaum J.S.; RT "Identification of a human type II receptor for bone morphogenetic protein- RT 4 that forms differential heteromeric complexes with bone morphogenetic RT protein type I receptors."; RL J. Biol. Chem. 270:22522-22526(1995). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7890683; DOI=10.1074/jbc.270.10.5625; RA Kawabata M., Chytil A., Moses H.L.; RT "Cloning of a novel type II serine/threonine kinase receptor through RT interaction with the type I transforming growth factor-beta receptor."; RL J. Biol. Chem. 270:5625-5630(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Skin; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-379, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [10] RP INTERACTION WITH GDF5. RX PubMed=21976273; DOI=10.1002/jbmr.532; RA Schwaerzer G.K., Hiepen C., Schrewe H., Nickel J., Ploeger F., Sebald W., RA Mueller T., Knaus P.; RT "New insights into the molecular mechanism of multiple synostoses syndrome RT (SYNS): mutation within the GDF5 knuckle epitope causes noggin- RT resistance."; RL J. Bone Miner. Res. 27:429-442(2012). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 33-131, AND DISULFIDE BONDS. RX PubMed=17094948; DOI=10.1016/j.bbrc.2006.10.109; RA Mace P.D., Cutfield J.F., Cutfield S.M.; RT "High resolution structures of the bone morphogenetic protein type II RT receptor in two crystal forms: implications for ligand binding."; RL Biochem. Biophys. Res. Commun. 351:831-838(2006). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 189-517 IN COMPLEX WITH ADP. RG Structural genomics consortium (SGC); RT "Crystal structure of the BMPR2 kinase domain."; RL Submitted (FEB-2009) to the PDB data bank. RN [14] RP VARIANTS PPH1 GLN-491 AND TRP-491. RX PubMed=10903931; DOI=10.1086/303059; RA Deng Z., Morse J.H., Slager S.L., Cuervo N., Moore K.J., Venetos G., RA Kalachikov S., Cayanis E., Fischer S.G., Barst R.J., Hodge S.E., RA Knowles J.A.; RT "Familial primary pulmonary hypertension (gene PPH1) is caused by mutations RT in the bone morphogenetic protein receptor-II gene."; RL Am. J. Hum. Genet. 67:737-744(2000). RN [15] RP VARIANTS PPH1 TYR-60; TYR-117 AND ARG-483. RX PubMed=11015450; DOI=10.1136/jmg.37.10.741; RA Thomson J.R., Machado R.D., Pauciulo M.W., Morgan N.V., Humbert M., RA Elliott G.C., Ward K., Yacoub M., Mikhail G., Rogers P., Newman J.H., RA Wheeler L., Higenbottam T., Gibbs J.S.R., Egan J., Crozier A., Peacock A., RA Allcock R., Corris P., Loyd J.E., Trembath R.C., Nichols W.C.; RT "Sporadic primary pulmonary hypertension is associated with germline RT mutations of the gene encoding BMPR-II, a receptor member of the TGF-beta RT family."; RL J. Med. Genet. 37:741-745(2000). RN [16] RP VARIANTS PPH1 TRP-118; TYR-347 AND GLY-485. RX PubMed=10973254; DOI=10.1038/79226; RA Lane K.B., Machado R.D., Pauciulo M.W., Thomson J.R., Phillips J.A. III, RA Loyd J.E., Nichols W.C., Trembath R.C., Aldred M., Brannon C.A., RA Conneally P.M., Foroud T., Fretwell N., Gaddipati R., Koller D., Loyd E.J., RA Morgan N.V., Newman J.H., Prince M.A., Vilarino Gueell C., Wheeler L.; RT "Heterozygous germline mutations in BMPR2, encoding a TGF-beta receptor, RT cause familial primary pulmonary hypertension."; RL Nat. Genet. 26:81-84(2000). RN [17] RP VARIANTS PPH1 ARG-123; SER-123; ARG-420 AND THR-512, VARIANT ASP-224, AND RP CHARACTERIZATION OF VARIANT PPH1 GLY-485. RX PubMed=11115378; DOI=10.1086/316947; RA Machado R.D., Pauciulo M.W., Thomson J.R., Lane K.B., Morgan N.V., RA Wheeler L., Phillips J.A. III, Newman J.H., Williams D., Galie N., RA Manes A., McNeil K., Yacoub M., Mikhail G., Rogers P., Corris P., RA Humbert M., Donnai D., Martensson G., Tranebjaerg L., Loyd J.E., RA Trembath R.C., Nichols W.C.; RT "BMPR2 haploinsufficiency as the inherited molecular mechanism for primary RT pulmonary hypertension."; RL Am. J. Hum. Genet. 68:92-102(2001). RN [18] RP VARIANTS PPH1 HIS-82; ASP-182 AND ARG-483. RX PubMed=12358323; DOI=10.1183/09031936.02.01762002; RA Humbert M., Deng Z., Simonneau G., Barst R.J., Sitbon O., Wolf M., RA Cuervo N., Moore K.J., Hodge S.E., Knowles J.A., Morse J.H.; RT "BMPR2 germline mutations in pulmonary hypertension associated with RT fenfluramine derivatives."; RL Eur. Respir. J. 20:518-523(2002). RN [19] RP INVOLVEMENT IN PVOD1. RX PubMed=12446270; DOI=10.1164/rccm.200208-861oc; RA Runo J.R., Vnencak-Jones C.L., Prince M., Loyd J.E., Wheeler L., RA Robbins I.M., Lane K.B., Newman J.H., Johnson J., Nichols W.C., RA Phillips J.A. III; RT "Pulmonary veno-occlusive disease caused by an inherited mutation in bone RT morphogenetic protein receptor II."; RL Am. J. Respir. Crit. Care Med. 167:889-894(2003). RN [20] RP VARIANT PPH1 PRO-899, AND CHARACTERIZATION OF VARIANT PPH1 PRO-899. RX PubMed=15965979; DOI=10.1002/humu.20200; RA Sankelo M., Flanagan J.A., Machado R., Harrison R., Rudarakanchana N., RA Morrell N., Dixon M., Halme M., Puolijoki H., Kere J., Elomaa O., RA Kupari M., Raeisaenen-Sokolowski A., Trembath R.C., Laitinen T.; RT "BMPR2 mutations have short lifetime expectancy in primary pulmonary RT hypertension."; RL Hum. Mutat. 26:119-124(2005). RN [21] RP INVOLVEMENT IN PVOD1. RX PubMed=16429395; DOI=10.1002/humu.20285; RA Machado R.D., Aldred M.A., James V., Harrison R.E., Patel B., RA Schwalbe E.C., Gruenig E., Janssen B., Koehler R., Seeger W., RA Eickelberg O., Olschewski H., Elliott C.G., Glissmeyer E., Carlquist J., RA Kim M., Torbicki A., Fijalkowska A., Szewczyk G., Parma J., RA Abramowicz M.J., Galie N., Morisaki H., Kyotani S., Nakanishi N., RA Morisaki T., Humbert M., Simonneau G., Sitbon O., Soubrier F., Coulet F., RA Morrell N.W., Trembath R.C.; RT "Mutations of the TGF-beta type II receptor BMPR2 in pulmonary arterial RT hypertension."; RL Hum. Mutat. 27:121-132(2006). RN [22] RP VARIANT [LARGE SCALE ANALYSIS] ASN-775. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). RN [23] RP VARIANTS PPH1 LEU-77; PHE-84; TYR-87; LEU-92; PRO-162; ASN-264 AND MET-341, RP AND VARIANT ASN-775. RX PubMed=24936649; DOI=10.1371/journal.pone.0100261; RA Pousada G., Baloira A., Vilarino C., Cifrian J.M., Valverde D.; RT "Novel mutations in BMPR2, ACVRL1 and KCNA5 genes and hemodynamic RT parameters in patients with pulmonary arterial hypertension."; RL PLoS ONE 9:E100261-E100261(2014). RN [24] RP VARIANTS PPH1 CYS-67 AND ASN-863, CHARACTERIZATION OF VARIANTS PPH1 CYS-67 RP AND ASN-863, AND SUBCELLULAR LOCATION. RX PubMed=25187962; DOI=10.1371/journal.pone.0106703; RA Wang H., Ji R., Meng J., Cui Q., Zou W., Li L., Wang G., Sun L., Li Z., RA Huo L., Fan Y., Penny D.J.; RT "Functional changes in pulmonary arterial endothelial cells associated with RT BMPR2 mutations."; RL PLoS ONE 9:E106703-E106703(2014). RN [25] RP VARIANTS PPH1 ARG-64; PHE-84; HIS-109; ALA-138; 218-TYR--LEU-1038 DEL; RP GLY-248; 298-TRP--LEU-1038 DEL AND ARG-467, CHARACTERIZATION OF VARIANTS RP PPH1 ARG-64; LEU-77; TYR-87; LEU-92; HIS-109; ALA-138; PRO-162; RP 218-TYR--LEU-1038 DEL; GLY-248; ASN-264; 298-TRP--LEU-1038 DEL; MET-341 AND RP ARG-467, AND CHARACTERIZATION OF VARIANT ASN-775. RX PubMed=28507310; DOI=10.1038/s41598-017-02074-8; RA Pousada G., Lupo V., Castro-Sanchez S., Alvarez-Satta M., RA Sanchez-Monteagudo A., Baloira A., Espinos C., Valverde D.; RT "Molecular and functional characterization of the BMPR2 gene in Pulmonary RT Arterial Hypertension."; RL Sci. Rep. 7:1923-1923(2017). 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. CC {ECO:0000250|UniProtKB:O35607}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[receptor-protein]-L-threonine + ATP = [receptor-protein]-O- CC phospho-L-threonine + ADP + H(+); 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=[receptor-protein]-L-serine + ATP = [receptor-protein]-O- CC phospho-L-serine + ADP + H(+); Xref=Rhea:RHEA:18673, Rhea:RHEA- CC COMP:11022, Rhea:RHEA-COMP:11023, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, CC ChEBI:CHEBI:456216; 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. {ECO:0000269|PubMed:21976273}. CC -!- INTERACTION: CC P08607:C4bpa (xeno); NbExp=3; IntAct=EBI-527196, EBI-527325; CC P43026:GDF5; NbExp=4; IntAct=EBI-527196, EBI-8571476; CC P68404:Prkcb (xeno); NbExp=4; IntAct=EBI-527196, EBI-397048; CC Q13976:PRKG1; NbExp=2; IntAct=EBI-527196, EBI-3952014; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25187962}; CC Single-pass type I membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q13873-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13873-2; Sequence=VSP_054441, VSP_054442; CC -!- TISSUE SPECIFICITY: Highly expressed in heart and liver. CC -!- DISEASE: Pulmonary hypertension, primary, 1 (PPH1) [MIM:178600]: A rare CC disorder characterized by plexiform lesions of proliferating CC endothelial cells in pulmonary arterioles. The lesions lead to elevated CC pulmonary arterial pression, right ventricular failure, and death. The CC disease can occur from infancy throughout life and it has a mean age at CC onset of 36 years. Penetrance is reduced. Although familial pulmonary CC hypertension is rare, cases secondary to known etiologies are more CC common and include those associated with the appetite-suppressant CC drugs. {ECO:0000269|PubMed:10903931, ECO:0000269|PubMed:10973254, CC ECO:0000269|PubMed:11015450, ECO:0000269|PubMed:11115378, CC ECO:0000269|PubMed:12358323, ECO:0000269|PubMed:15965979, CC ECO:0000269|PubMed:24936649, ECO:0000269|PubMed:25187962, CC ECO:0000269|PubMed:28507310}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- DISEASE: Pulmonary venoocclusive disease 1, autosomal dominant (PVOD1) CC [MIM:265450]: A disease characterized by widespread fibrous obstruction CC and intimal thickening of septal veins and preseptal venules, a low CC diffusing capacity for carbon monoxide, occult alveolar hemorrhage, and CC nodular ground-glass opacities, septal lines and lymph node enlargement CC showed by high-resolution computed tomography of the chest. It is CC frequently associated with pulmonary capillary dilatation and CC proliferation, and is a rare and devastating cause of pulmonary CC hypertension. {ECO:0000269|PubMed:12446270, CC ECO:0000269|PubMed:16429395}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. 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; U25110; AAA86519.1; -; mRNA. DR EMBL; Z48923; CAA88759.1; -; mRNA. DR EMBL; D50516; BAA09094.1; -; mRNA. DR EMBL; U20165; AAC50105.1; -; mRNA. DR EMBL; AC009960; AAX76517.1; -; Genomic_DNA. DR EMBL; AC073410; AAX88941.1; -; Genomic_DNA. DR EMBL; AC064836; AAY24146.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70309.1; -; Genomic_DNA. DR EMBL; BC052985; AAH52985.1; -; mRNA. DR CCDS; CCDS33361.1; -. [Q13873-1] DR PIR; I38935; I38935. DR RefSeq; NP_001195.2; NM_001204.6. [Q13873-1] DR PDB; 2HLQ; X-ray; 1.45 A; A=33-131. DR PDB; 3G2F; X-ray; 2.35 A; A/B=189-517. DR PDBsum; 2HLQ; -. DR PDBsum; 3G2F; -. DR SMR; Q13873; -. DR BioGrid; 107127; 68. DR DIP; DIP-5794N; -. DR ELM; Q13873; -. DR IntAct; Q13873; 44. DR MINT; Q13873; -. DR STRING; 9606.ENSP00000363708; -. DR BindingDB; Q13873; -. DR ChEMBL; CHEMBL5467; -. DR DrugBank; DB11639; Dibotermin alfa. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; Q13873; -. DR GuidetoPHARMACOLOGY; 1794; -. DR GlyConnect; 1046; -. DR iPTMnet; Q13873; -. DR PhosphoSitePlus; Q13873; -. DR BioMuta; BMPR2; -. DR DMDM; 12643724; -. DR CPTAC; CPTAC-2209; -. DR EPD; Q13873; -. DR jPOST; Q13873; -. DR MassIVE; Q13873; -. DR MaxQB; Q13873; -. DR PaxDb; Q13873; -. DR PeptideAtlas; Q13873; -. DR PRIDE; Q13873; -. DR ProteomicsDB; 59705; -. [Q13873-1] DR DNASU; 659; -. DR Ensembl; ENST00000374574; ENSP00000363702; ENSG00000204217. [Q13873-2] DR Ensembl; ENST00000374580; ENSP00000363708; ENSG00000204217. [Q13873-1] DR GeneID; 659; -. DR KEGG; hsa:659; -. DR UCSC; uc002uzf.5; human. [Q13873-1] DR CTD; 659; -. DR DisGeNET; 659; -. DR GeneCards; BMPR2; -. DR GeneReviews; BMPR2; -. DR HGNC; HGNC:1078; BMPR2. DR HPA; HPA017385; -. DR HPA; HPA049014; -. DR MalaCards; BMPR2; -. DR MIM; 178600; phenotype. DR MIM; 265450; phenotype. DR MIM; 600799; gene. DR neXtProt; NX_Q13873; -. DR OpenTargets; ENSG00000204217; -. DR Orphanet; 275786; Drug- or toxin-induced pulmonary arterial hypertension. DR Orphanet; 275777; Heritable pulmonary arterial hypertension. DR Orphanet; 31837; Pulmonary venoocclusive disease. DR PharmGKB; PA25388; -. DR eggNOG; KOG3653; Eukaryota. DR eggNOG; ENOG410XS2Z; LUCA. DR GeneTree; ENSGT00940000156449; -. DR HOGENOM; CLU_013015_0_0_1; -. DR InParanoid; Q13873; -. DR KO; K04671; -. DR OMA; ECHFEEC; -. DR OrthoDB; 390511at2759; -. DR PhylomeDB; Q13873; -. DR TreeFam; TF314724; -. DR Reactome; R-HSA-201451; Signaling by BMP. DR SignaLink; Q13873; -. DR SIGNOR; Q13873; -. DR ChiTaRS; BMPR2; human. DR EvolutionaryTrace; Q13873; -. DR GeneWiki; BMPR2; -. DR GenomeRNAi; 659; -. DR Pharos; Q13873; Tchem. DR PRO; PR:Q13873; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q13873; protein. DR Bgee; ENSG00000204217; Expressed in upper lobe of lung and 219 other tissues. DR ExpressionAtlas; Q13873; baseline and differential. DR Genevisible; Q13873; HS. DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL. DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl. DR GO; GO:0009925; C:basal plasma membrane; IEA:Ensembl. DR GO; GO:0005901; C:caveola; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0043235; C:receptor complex; IBA:GO_Central. DR GO; GO:0044214; C:spanning component of plasma membrane; TAS:AgBase. DR GO; GO:0016362; F:activin receptor activity, type II; TAS:Reactome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0036122; F:BMP binding; IPI:UniProtKB. DR GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB. DR GO; GO:0045296; F:cadherin binding; IPI:ARUK-UCL. DR GO; GO:0019838; F:growth factor binding; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central. DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:ARUK-UCL. DR GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IBA:GO_Central. DR GO; GO:0009952; P:anterior/posterior pattern specification; ISS:BHF-UCL. DR GO; GO:0003176; P:aortic valve development; ISS:BHF-UCL. DR GO; GO:0060840; P:artery development; ISS:BHF-UCL. DR GO; GO:0060413; P:atrial septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0001568; P:blood vessel development; IBA:GO_Central. DR GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL. DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL. DR GO; GO:0007420; P:brain development; IEA:Ensembl. DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IBA:GO_Central. DR GO; GO:0009267; P:cellular response to starvation; IEP:BHF-UCL. DR GO; GO:0002063; P:chondrocyte development; IMP:AgBase. DR GO; GO:0003197; P:endocardial cushion development; ISS:BHF-UCL. DR GO; GO:0060350; P:endochondral bone morphogenesis; ISS:AgBase. DR GO; GO:0072577; P:endothelial cell apoptotic process; IMP:UniProtKB. DR GO; GO:0001935; P:endothelial cell proliferation; IMP:UniProtKB. DR GO; GO:0060173; P:limb development; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; ISS:BHF-UCL. DR GO; GO:0001946; P:lymphangiogenesis; ISS:BHF-UCL. DR GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL. DR GO; GO:0001893; P:maternal placenta development; IEA:Ensembl. DR GO; GO:0001707; P:mesoderm formation; ISS:BHF-UCL. DR GO; GO:0003183; P:mitral valve morphogenesis; ISS:BHF-UCL. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:0003252; P:negative regulation of cell proliferation involved in heart valve morphogenesis; ISS:BHF-UCL. DR GO; GO:1902731; P:negative regulation of chondrocyte proliferation; IMP:AgBase. DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IMP:BHF-UCL. DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IMP:BHF-UCL. DR GO; GO:0045906; P:negative regulation of vasoconstriction; ISS:BHF-UCL. DR GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL. DR GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL. DR GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISS:BHF-UCL. DR GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; IEA:Ensembl. DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:UniProtKB. DR GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL. DR GO; GO:0061036; P:positive regulation of cartilage development; ISS:AgBase. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:UniProtKB. DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IDA:UniProtKB. DR GO; GO:0045778; P:positive regulation of ossification; ISS:BHF-UCL. DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL. DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IMP:UniProtKB. 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; ISS:BHF-UCL. DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:HGNC-UCL. 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; ISS:BHF-UCL. DR GO; GO:1905314; P:semi-lunar valve development; ISS:BHF-UCL. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; IDA:BHF-UCL. DR GO; GO:0003186; P:tricuspid valve morphogenesis; ISS:BHF-UCL. DR GO; GO:0001944; P:vasculature development; IBA:GO_Central. DR GO; GO:0060841; P:venous blood vessel development; ISS:BHF-UCL. DR GO; GO:0060412; P:ventricular septum morphogenesis; ISS:BHF-UCL. 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; IPR000333; TGFB_receptor. DR PANTHER; PTHR23255; PTHR23255; 1. DR PANTHER; PTHR23255:SF63; PTHR23255:SF63; 1. DR Pfam; PF01064; Activin_recp; 1. DR Pfam; PF00069; Pkinase; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane; KW Disease mutation; Disulfide bond; Glycoprotein; Kinase; Magnesium; KW Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Polymorphism; 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_0000024415" 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 NP_BIND 209..217 FT /note="ATP" FT /evidence="ECO:0000305|Ref.13" FT NP_BIND 280..282 FT /note="ATP" FT /evidence="ECO:0000305|Ref.13" FT NP_BIND 337..338 FT /note="ATP" FT /evidence="ECO:0000305|Ref.13" FT COMPBIAS 547..550 FT /note="Poly-Ser" FT COMPBIAS 610..618 FT /note="Poly-Thr" FT COMPBIAS 901..908 FT /note="Poly-Asn" FT ACT_SITE 333 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 230 FT /note="ATP" FT /evidence="ECO:0000305|Ref.13" FT BINDING 351 FT /note="ATP" FT /evidence="ECO:0000305|Ref.13" FT MOD_RES 379 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:19369195" FT MOD_RES 586 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18691976" FT MOD_RES 680 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35607" FT MOD_RES 681 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35607" 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:0000244|PDB:2HLQ, FT ECO:0000269|PubMed:17094948" FT DISULFID 60..84 FT /evidence="ECO:0000244|PDB:2HLQ, FT ECO:0000269|PubMed:17094948" FT DISULFID 94..117 FT /evidence="ECO:0000244|PDB:2HLQ, FT ECO:0000269|PubMed:17094948" FT DISULFID 99..116 FT /evidence="ECO:0000244|PDB:2HLQ, FT ECO:0000269|PubMed:17094948" FT DISULFID 118..123 FT /evidence="ECO:0000244|PDB:2HLQ, FT ECO:0000269|PubMed:17094948" FT VAR_SEQ 530 FT /note="N -> R (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7791754" FT /id="VSP_054441" FT VAR_SEQ 531..1038 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7791754" FT /id="VSP_054442" FT VARIANT 60 FT /note="C -> Y (in PPH1; dbSNP:rs1085307172)" FT /evidence="ECO:0000269|PubMed:11015450" FT /id="VAR_013670" FT VARIANT 64 FT /note="S -> R (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079588" FT VARIANT 67 FT /note="Y -> C (in PPH1; significant decrease in nitric FT oxide synthesis by endothelial cells; dbSNP:rs1085307177)" FT /evidence="ECO:0000269|PubMed:25187962" FT /id="VAR_073041" FT VARIANT 77 FT /note="I -> L (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079589" FT VARIANT 82 FT /note="Q -> H (in PPH1; dbSNP:rs1085307185)" FT /evidence="ECO:0000269|PubMed:12358323" FT /id="VAR_033109" FT VARIANT 84 FT /note="C -> F (in PPH1; alters alternative splicing of FT BMPR2; dbSNP:rs1085307197)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079590" FT VARIANT 87 FT /note="H -> Y (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079591" FT VARIANT 92 FT /note="Q -> L (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079592" FT VARIANT 109 FT /note="Q -> H (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079593" FT VARIANT 117 FT /note="C -> Y (in PPH1; dbSNP:rs1085307215)" FT /evidence="ECO:0000269|PubMed:11015450" FT /id="VAR_013671" FT VARIANT 118 FT /note="C -> W (in PPH1; dbSNP:rs137852743)" FT /evidence="ECO:0000269|PubMed:10973254" FT /id="VAR_013672" FT VARIANT 123 FT /note="C -> R (in PPH1; dbSNP:rs137852750)" FT /evidence="ECO:0000269|PubMed:11115378" FT /id="VAR_013673" FT VARIANT 123 FT /note="C -> S (in PPH1; dbSNP:rs137852750)" FT /evidence="ECO:0000269|PubMed:11115378" FT /id="VAR_013674" FT VARIANT 138 FT /note="P -> A (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079594" FT VARIANT 162 FT /note="A -> P (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079595" FT VARIANT 182 FT /note="G -> D (in PPH1; dbSNP:rs137852754)" FT /evidence="ECO:0000269|PubMed:12358323" FT /id="VAR_033110" FT VARIANT 218..1038 FT /note="Missing (in PPH1; changed localization to the plasma FT membrane)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079596" FT VARIANT 224 FT /note="E -> D (in dbSNP:rs754343081)" FT /evidence="ECO:0000269|PubMed:11115378" FT /id="VAR_013675" FT VARIANT 248 FT /note="R -> G (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079597" FT VARIANT 264 FT /note="D -> N (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079598" FT VARIANT 298..1038 FT /note="Missing (in PPH1; loss of localization to the plasma FT membrane; localized to the cytoplasm)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079599" FT VARIANT 341 FT /note="V -> M (in PPH1; unknown pathological significance; FT unchanged subcellular localization; dbSNP:rs767882551)" FT /evidence="ECO:0000269|PubMed:24936649, FT ECO:0000269|PubMed:28507310" FT /id="VAR_079600" FT VARIANT 347 FT /note="C -> Y (in PPH1; dbSNP:rs137852744)" FT /evidence="ECO:0000269|PubMed:10973254" FT /id="VAR_013676" FT VARIANT 420 FT /note="C -> R (in PPH1; dbSNP:rs1085307324)" FT /evidence="ECO:0000269|PubMed:11115378" FT /id="VAR_013677" FT VARIANT 467 FT /note="K -> R (in PPH1; unknown pathological significance; FT unchanged subcellular localization)" FT /evidence="ECO:0000269|PubMed:28507310" FT /id="VAR_079601" FT VARIANT 483 FT /note="C -> R (in PPH1; sporadic; dbSNP:rs1085307354)" FT /evidence="ECO:0000269|PubMed:11015450, FT ECO:0000269|PubMed:12358323" FT /id="VAR_013678" FT VARIANT 485 FT /note="D -> G (in PPH1; complete loss of function; FT dbSNP:rs137852745)" FT /evidence="ECO:0000269|PubMed:10973254, FT ECO:0000269|PubMed:11115378" FT /id="VAR_013679" FT VARIANT 491 FT /note="R -> Q (in PPH1; sporadic; dbSNP:rs137852749)" FT /evidence="ECO:0000269|PubMed:10903931" FT /id="VAR_013680" FT VARIANT 491 FT /note="R -> W (in PPH1; dbSNP:rs137852746)" FT /evidence="ECO:0000269|PubMed:10903931" FT /id="VAR_013681" FT VARIANT 512 FT /note="K -> T (in PPH1; dbSNP:rs1085307364)" FT /evidence="ECO:0000269|PubMed:11115378" FT /id="VAR_013682" FT VARIANT 519 FT /note="N -> K (in PPH1; dbSNP:rs1085307365)" FT /id="VAR_013683" FT VARIANT 775 FT /note="S -> N (polymorphism; unchanged subcellular FT localization; dbSNP:rs2228545)" FT /evidence="ECO:0000269|PubMed:17344846, FT ECO:0000269|PubMed:24936649, ECO:0000269|PubMed:28507310" FT /id="VAR_019996" FT VARIANT 863 FT /note="S -> N (in PPH1; abnormal subcellular localization; FT significant increase in apoptosis of endothelial cells; FT significant decrease in proliferation of endothelial cells; FT significant decrease in nitric oxide synthesis by FT endothelial cells; significant increase in endothelin 1 FT synthesis by endothelial cells; dbSNP:rs1006246556)" FT /evidence="ECO:0000269|PubMed:25187962" FT /id="VAR_073042" FT VARIANT 899 FT /note="R -> P (in PPH1; leads to constitutive activation of FT the MAPK14 pathway; dbSNP:rs137852752)" FT /evidence="ECO:0000269|PubMed:15965979" FT /id="VAR_033111" FT CONFLICT 828 FT /note="G -> R (in Ref. 2; CAA88759)" FT /evidence="ECO:0000305" FT STRAND 33..35 FT /evidence="ECO:0000244|PDB:2HLQ" FT TURN 42..47 FT /evidence="ECO:0000244|PDB:2HLQ" FT HELIX 48..50 FT /evidence="ECO:0000244|PDB:2HLQ" FT TURN 53..56 FT /evidence="ECO:0000244|PDB:2HLQ" FT STRAND 57..59 FT /evidence="ECO:0000244|PDB:2HLQ" FT STRAND 66..73 FT /evidence="ECO:0000244|PDB:2HLQ" FT STRAND 76..84 FT /evidence="ECO:0000244|PDB:2HLQ" FT STRAND 90..92 FT /evidence="ECO:0000244|PDB:2HLQ" FT TURN 105..109 FT /evidence="ECO:0000244|PDB:2HLQ" FT STRAND 113..118 FT /evidence="ECO:0000244|PDB:2HLQ" FT HELIX 123..125 FT /evidence="ECO:0000244|PDB:2HLQ" FT STRAND 202..211 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 213..222 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 225..233 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 234..236 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 237..247 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 260..267 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 273..279 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 287..293 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 298..316 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 322..324 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 338..341 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 347..349 FT /evidence="ECO:0000244|PDB:3G2F" FT STRAND 359..362 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 380..382 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 385..388 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 394..396 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 397..417 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 421..423 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 437..440 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 446..453 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 471..483 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 488..490 FT /evidence="ECO:0000244|PDB:3G2F" FT HELIX 494..506 FT /evidence="ECO:0000244|PDB:3G2F" SQ SEQUENCE 1038 AA; 115201 MW; 1389923CE574B913 CRC64; MTSSLQRPWR VPWLPWTILL VSTAAASQNQ ERLCAFKDPY QQDLGIGESR ISHENGTILC SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV VTTTPPSIQN GTYRFCCCST DLCNVNFTEN FPPPDTTPLS PPHSFNRDET IIIALASVSV LAVLIVALCF GYRMLTGDRK QGLHSMNMME AAASEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF INEKNIYRVP LMEHDNIARF IVGDERVTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGTCVIS DFGLSMRLTG NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA LKQVDMYALG LIYWEIFMRC TDLFPGESVP EYQMAFQTEV GNHPTFEDMQ VLVSREKQRP KFPEAWKENS LAVRSLKETI EDCWDQDAEA RLTAQCAEER MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI GPYPDYSSSS YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETNL HTTNVAQSIG PTPVCLQLTE EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS STSSSLLYPL IKLAVEATGQ QDFTQTANGQ ACLIPDVLPT QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGSKHKSN LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRNHSVNSHA ATTQYANGTV LSGQTTNIVT HRAQEMLQNQ FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT NSNNNNSNPC SEQDVLAQGV PSTAADPGPS KPRRAQRPNS LDLSATNVLD GSSIQIGEST QDGKSGSGEK IKKRVKTPYS LKRWRPSTWV ISTESLDCEV NNNGSNRAVH SKSSTAVYLA EGGTATTMVS KDIGMNCL //