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Database: UniProt
Entry: P36894
LinkDB: P36894
Original site: P36894 
ID   BMR1A_HUMAN             Reviewed;         532 AA.
AC   P36894; A8K6U9; Q8NEN8;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   01-OCT-2014, entry version 178.
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=Serine/threonine-protein kinase receptor R5;
DE            Short=SKR5;
DE   AltName: CD_antigen=CD292;
DE   Flags: Precursor;
GN   Name=BMPR1A; Synonyms=ACVRLK3, ALK3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-2.
RC   TISSUE=Placenta;
RX   PubMed=8397373;
RA   ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J.,
RA   Toyoshima H., Heldin C.-H., Miyazono K.;
RT   "Activin receptor-like kinases: a novel subclass of cell-surface
RT   receptors with predicted serine/threonine kinase activity.";
RL   Oncogene 8:2879-2887(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-2.
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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).
RN   [4]
RP   INTERACTION WITH BMP2, AND MUTAGENESIS OF 107-ASP--GLN-109.
RX   PubMed=22799562; DOI=10.1021/bi300942x;
RA   Mahlawat P., Ilangovan U., Biswas T., Sun L.Z., Hinck A.P.;
RT   "Structure of the Alk1 extracellular domain and characterization of
RT   its bone morphogenetic protein (BMP) binding properties.";
RL   Biochemistry 51:6328-6341(2012).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 55-143 IN COMPLEX WITH BMP-2.
RX   PubMed=10881198; DOI=10.1038/75903;
RA   Kirsch T., Sebald W., Dreyer M.K.;
RT   "Crystal structure of the BMP-2-BRIA ectodomain complex.";
RL   Nat. Struct. Biol. 7:492-496(2000).
RN   [6]
RP   DISEASE.
RX   PubMed=11381269; DOI=10.1038/88919;
RA   Howe J.R., Bair J.L., Sayed M.G., Anderson M.E., Mitros F.A.,
RA   Petersen G.M., Velculescu V.E., Traverso G., Vogelstein B.;
RT   "Germline mutations of the gene encoding bone morphogenetic protein
RT   receptor 1A in juvenile polyposis.";
RL   Nat. Genet. 28:184-187(2001).
RN   [7]
RP   VARIANTS JPS ARG-124; ASP-338 AND TYR-376.
RX   PubMed=11536076; DOI=10.1086/323703;
RA   Zhou X.-P., Woodford-Richens K., Lehtonen R., Kurose K., Aldred M.,
RA   Hampel H., Launonen V., Virta S., Pilarski R., Salovaara R.,
RA   Bodmer W.F., Conrad B.A., Dunlop M., Hodgson S.V., Iwama T.,
RA   Jaervinen H., Kellokumpu I., Kim J.C., Leggett B., Markie D.,
RA   Mecklin J.-P., Neale K., Phillips R., Piris J., Rozen P.,
RA   Houlston R.S., Aaltonen L.A., Tomlinson I.P.M., Eng C.;
RT   "Germline mutations in BMPR1A/ALK3 cause a subset of cases of juvenile
RT   polyposis syndrome and of Cowden and Bannayan-Riley-Ruvalcaba
RT   syndromes.";
RL   Am. J. Hum. Genet. 69:704-711(2001).
RN   [8]
RP   VARIANTS JPS ASP-62; TYR-82 AND CYS-443.
RX   PubMed=12417513; DOI=10.1007/BF02557528;
RA   Sayed M.G., Ahmed A.F., Ringold J.R., Anderson M.E., Bair J.L.,
RA   Mitros F.A., Lynch H.T., Tinley S.T., Petersen G.M., Giardiello F.M.,
RA   Vogelstein B., Howe J.R.;
RT   "Germline SMAD4 or BMPR1A mutations and phenotype of juvenile
RT   polyposis.";
RL   Ann. Surg. Oncol. 9:901-906(2002).
RN   [9]
RP   VARIANT JPS ARG-130.
RX   PubMed=12136244; DOI=10.1007/s00439-002-0748-9;
RA   Friedl W., Uhlhaas S., Schulmann K., Stolte M., Loff S., Back W.,
RA   Mangold E., Stern M., Knaebel H.P., Sutter C., Weber R.G.,
RA   Pistorius S., Burger B., Propping P.;
RT   "Juvenile polyposis: massive gastric polyposis is more common in MADH4
RT   mutation carriers than in BMPR1A mutation carriers.";
RL   Hum. Genet. 111:108-111(2002).
RN   [10]
RP   VARIANT JPS THR-470.
RX   PubMed=12630959; DOI=10.1034/j.1399-0004.2003.00008.x;
RA   Kim I.J., Park J.H., Kang H.C., Kim K.H., Kim J.H., Ku J.L.,
RA   Kang S.B., Park S.Y., Lee J.S., Park J.G.;
RT   "Identification of a novel BMPR1A germline mutation in a Korean
RT   juvenile polyposis patient without SMAD4 mutation.";
RL   Clin. Genet. 63:126-130(2003).
RN   [11]
RP   INVOLVEMENT IN JUVENILE POLYPOSIS OF INFANCY.
RX   PubMed=16685657; DOI=10.1086/504301;
RA   Delnatte C., Sanlaville D., Mougenot J.-F., Vermeesch J.-R.,
RA   Houdayer C., Blois M.-C., Genevieve D., Goulet O., Fryns J.-P.,
RA   Jaubert F., Vekemans M., Lyonnet S., Romana S., Eng C.,
RA   Stoppa-Lyonnet D.;
RT   "Contiguous gene deletion within chromosome arm 10q is associated with
RT   juvenile polyposis of infancy, reflecting cooperation between the
RT   BMPR1A and PTEN tumor-suppressor genes.";
RL   Am. J. Hum. Genet. 78:1066-1074(2006).
RN   [12]
RP   INVOLVEMENT IN HEREDITARY MIXED POLYPOSIS SYNDROME 2.
RX   PubMed=16525031; DOI=10.1136/jmg.2005.034827;
RA   Cao X., Eu K.W., Kumarasinghe M.P., Li H.H., Loi C., Cheah P.Y.;
RT   "Mapping of hereditary mixed polyposis syndrome (HMPS) to chromosome
RT   10q23 by genomewide high-density single nucleotide polymorphism (SNP)
RT   scan and identification of BMPR1A loss of function.";
RL   J. Med. Genet. 43:E13-E13(2006).
RN   [13]
RP   VARIANTS [LARGE SCALE ANALYSIS] THR-2; TYR-58; CYS-443; MET-450 AND
RP   GLN-486.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
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. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P12643:BMP2; NbExp=13; IntAct=EBI-1029237, EBI-1029262;
CC       P12644:BMP4; NbExp=2; IntAct=EBI-1029237, EBI-1998134;
CC       P43026:GDF5; NbExp=2; IntAct=EBI-1029237, EBI-8571476;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
CC   -!- DISEASE: Juvenile polyposis syndrome (JPS) [MIM:174900]: Autosomal
CC       dominant gastrointestinal hamartomatous polyposis syndrome in
CC       which patients are at risk for developing gastrointestinal
CC       cancers. The lesions are typified by a smooth histological
CC       appearance, predominant stroma, cystic spaces and lack of a smooth
CC       muscle core. Multiple juvenile polyps usually occur in a number of
CC       Mendelian disorders. Sometimes, these polyps occur without
CC       associated features as in JPS; here, polyps tend to occur in the
CC       large bowel and are associated with an increased risk of colon and
CC       other gastrointestinal cancers. {ECO:0000269|PubMed:11536076,
CC       ECO:0000269|PubMed:12136244, ECO:0000269|PubMed:12417513,
CC       ECO:0000269|PubMed:12630959}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Polyposis syndrome, mixed hereditary 2 (HMPS2)
CC       [MIM:610069]: A disease is characterized by atypical juvenile
CC       polyps, colonic adenomas, and colorectal carcinomas. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Note=A microdeletion of chromosome 10q23 involving BMPR1A
CC       and PTEN is a cause of chromosome 10q23 deletion syndrome, which
CC       shows overlapping features of the following three disorders:
CC       Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis
CC       syndrome. {ECO:0000269|PubMed:11381269,
CC       ECO:0000269|PubMed:16525031}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 GS domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00585}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; Z22535; CAA80257.1; -; mRNA.
DR   EMBL; AK291764; BAF84453.1; -; mRNA.
DR   EMBL; BC028383; AAH28383.1; -; mRNA.
DR   CCDS; CCDS7378.1; -.
DR   PIR; I37163; I37163.
DR   RefSeq; NP_004320.2; NM_004329.2.
DR   UniGene; Hs.524477; -.
DR   PDB; 1ES7; X-ray; 2.90 A; B/D=55-143.
DR   PDB; 1REW; X-ray; 1.86 A; C/D=24-152.
DR   PDB; 2GOO; X-ray; 2.20 A; B/E=24-152.
DR   PDB; 2H62; X-ray; 1.85 A; C=24-152.
DR   PDB; 2H64; X-ray; 1.92 A; B=24-152.
DR   PDB; 2K3G; NMR; -; A=51-152.
DR   PDB; 2QJ9; X-ray; 2.44 A; C/D=24-152.
DR   PDB; 2QJA; X-ray; 2.60 A; C/D=24-152.
DR   PDB; 2QJB; X-ray; 2.50 A; C/D=24-152.
DR   PDB; 3NH7; X-ray; 2.70 A; A/B/C/D=24-152.
DR   PDB; 3QB4; X-ray; 2.28 A; B/D=24-152.
DR   PDBsum; 1ES7; -.
DR   PDBsum; 1REW; -.
DR   PDBsum; 2GOO; -.
DR   PDBsum; 2H62; -.
DR   PDBsum; 2H64; -.
DR   PDBsum; 2K3G; -.
DR   PDBsum; 2QJ9; -.
DR   PDBsum; 2QJA; -.
DR   PDBsum; 2QJB; -.
DR   PDBsum; 3NH7; -.
DR   PDBsum; 3QB4; -.
DR   ProteinModelPortal; P36894; -.
DR   SMR; P36894; 57-140, 204-530.
DR   BioGrid; 107125; 34.
DR   DIP; DIP-5793N; -.
DR   IntAct; P36894; 7.
DR   MINT; MINT-124304; -.
DR   STRING; 9606.ENSP00000224764; -.
DR   BindingDB; P36894; -.
DR   ChEMBL; CHEMBL5275; -.
DR   GuidetoPHARMACOLOGY; 1786; -.
DR   PhosphoSite; P36894; -.
DR   DMDM; 61252444; -.
DR   MaxQB; P36894; -.
DR   PaxDb; P36894; -.
DR   PRIDE; P36894; -.
DR   DNASU; 657; -.
DR   Ensembl; ENST00000372037; ENSP00000361107; ENSG00000107779.
DR   GeneID; 657; -.
DR   KEGG; hsa:657; -.
DR   UCSC; uc001kdy.3; human.
DR   CTD; 657; -.
DR   GeneCards; GC10P088506; -.
DR   GeneReviews; BMPR1A; -.
DR   HGNC; HGNC:1076; BMPR1A.
DR   HPA; CAB019398; -.
DR   MIM; 174900; phenotype.
DR   MIM; 601299; gene.
DR   MIM; 610069; phenotype.
DR   MIM; 612242; phenotype.
DR   neXtProt; NX_P36894; -.
DR   Orphanet; 329971; Generalized juvenile polyposis/juvenile polyposis coli.
DR   Orphanet; 157794; Hereditary mixed polyposis syndrome.
DR   Orphanet; 144; Hereditary nonpolyposis colon cancer.
DR   Orphanet; 79076; Juvenile polyposis of infancy.
DR   PharmGKB; PA25386; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000230587; -.
DR   HOVERGEN; HBG054502; -.
DR   InParanoid; P36894; -.
DR   KO; K04673; -.
DR   OMA; CYNRDLE; -.
DR   OrthoDB; EOG7Q8CN3; -.
DR   PhylomeDB; P36894; -.
DR   TreeFam; TF314724; -.
DR   BRENDA; 2.7.10.2; 2681.
DR   Reactome; REACT_12034; Signaling by BMP.
DR   SignaLink; P36894; -.
DR   EvolutionaryTrace; P36894; -.
DR   GeneWiki; BMPR1A; -.
DR   GenomeRNAi; 657; -.
DR   NextBio; 2672; -.
DR   PRO; PR:P36894; -.
DR   Bgee; P36894; -.
DR   CleanEx; HS_BMPR1A; -.
DR   Genevestigator; P36894; -.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:HGNC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC.
DR   GO; GO:0004702; F:receptor signaling protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0000981; F:sequence-specific DNA binding RNA polymerase II transcription factor activity; IEA:Ensembl.
DR   GO; GO:0046332; F:SMAD binding; IDA:HGNC.
DR   GO; GO:0005024; F:transforming growth factor beta-activated receptor activity; IEA:InterPro.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:Reactome.
DR   GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR   GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl.
DR   GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR   GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
DR   GO; GO:0003272; P:endocardial cushion formation; ISS:BHF-UCL.
DR   GO; GO:0060914; P:heart formation; IEA:Ensembl.
DR   GO; GO:0035137; P:hindlimb morphogenesis; IEA:Ensembl.
DR   GO; GO:0006955; P:immune response; IMP:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0048368; P:lateral mesoderm development; IEA:Ensembl.
DR   GO; GO:0030324; P:lung development; IEA:Ensembl.
DR   GO; GO:0048382; P:mesendoderm development; IEA:Ensembl.
DR   GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
DR   GO; GO:0001880; P:Mullerian duct regression; IEA:Ensembl.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
DR   GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR   GO; GO:0021998; P:neural plate mediolateral regionalization; IEA:Ensembl.
DR   GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR   GO; GO:0060021; P:palate development; IEA:Ensembl.
DR   GO; GO:0048352; P:paraxial mesoderm structural organization; IEA:Ensembl.
DR   GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
DR   GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
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; IDA:BHF-UCL.
DR   GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IDA:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:HGNC.
DR   GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0019827; P:stem cell maintenance; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR003605; TGF_beta_rcpt_GS.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255; PTHR23255; 1.
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; SSF56112; 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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Disease mutation;
KW   Disulfide bond; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Polymorphism; Receptor;
KW   Reference proteome; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24    532       Bone morphogenetic protein receptor type-
FT                                1A.
FT                                /FTId=PRO_0000024410.
FT   TOPO_DOM     24    152       Extracellular. {ECO:0000255}.
FT   TRANSMEM    153    176       Helical. {ECO:0000255}.
FT   TOPO_DOM    177    532       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      204    233       GS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00585}.
FT   DOMAIN      234    525       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     240    248       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   REGION      107    109       Mediates specificity for BMP ligand.
FT   ACT_SITE    362    362       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     261    261       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   CARBOHYD     73     73       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     61     82
FT   DISULFID     63     67
FT   DISULFID     76    100
FT   DISULFID    110    124
FT   DISULFID    125    130
FT   VARIANT       2      2       P -> T (in dbSNP:rs11528010).
FT                                {ECO:0000269|PubMed:14702039,
FT                                ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:8397373}.
FT                                /FTId=VAR_041397.
FT   VARIANT      58     58       F -> Y (in a renal clear cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041398.
FT   VARIANT      62     62       Y -> D (in JPS).
FT                                {ECO:0000269|PubMed:12417513}.
FT                                /FTId=VAR_022828.
FT   VARIANT      82     82       C -> Y (in JPS).
FT                                {ECO:0000269|PubMed:12417513}.
FT                                /FTId=VAR_022829.
FT   VARIANT     124    124       C -> R (in JPS).
FT                                {ECO:0000269|PubMed:11536076}.
FT                                /FTId=VAR_015533.
FT   VARIANT     130    130       C -> R (in JPS).
FT                                {ECO:0000269|PubMed:12136244}.
FT                                /FTId=VAR_022830.
FT   VARIANT     338    338       A -> D (in JPS).
FT                                {ECO:0000269|PubMed:11536076}.
FT                                /FTId=VAR_015534.
FT   VARIANT     376    376       C -> Y (in JPS).
FT                                {ECO:0000269|PubMed:11536076}.
FT                                /FTId=VAR_015535.
FT   VARIANT     443    443       R -> C (in JPS; dbSNP:rs35619497).
FT                                {ECO:0000269|PubMed:12417513,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_022831.
FT   VARIANT     450    450       V -> M (in dbSNP:rs55932635).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041399.
FT   VARIANT     470    470       M -> T (in JPS).
FT                                {ECO:0000269|PubMed:12630959}.
FT                                /FTId=VAR_022832.
FT   VARIANT     486    486       R -> Q (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_041400.
FT   MUTAGEN     107    109       DFQ->REL: Affinity for BMP2 decreased by
FT                                over 200-fold.
FT                                {ECO:0000269|PubMed:22799562}.
FT   STRAND       59     62
FT   STRAND       64     66
FT   STRAND       75     88
FT   STRAND       90     92
FT   STRAND       94    101
FT   HELIX       106    111
FT   STRAND      116    118
FT   STRAND      120    125
FT   HELIX       130    133
SQ   SEQUENCE   532 AA;  60198 MW;  00CE2DDDA3A44170 CRC64;
     MPQLYIYIRL LGAYLFIISR VQGQNLDSML HGTGMKSDSD QKKSENGVTL APEDTLPFLK
     CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLASGC MKYEGSDFQC KDSPKAQLRR
     TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRWLVLLISM AVCIIAMIIF SSCFCYKHYC
     KSISSRRRYN RDLEQDEAFI PVGESLKDLI DQSQSSGSGS GLPLLVQRTI AKQIQMVRQV
     GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT VLMRHENILG FIAADIKGTG
     SWTQLYLITD YHENGSLYDF LKCATLDTRA LLKLAYSAAC GLCHLHTEIY GTQGKPAIAH
     RDLKSKNILI KKNGSCCIAD LGLAVKFNSD TNEVDVPLNT RVGTKRYMAP EVLDESLNKN
     HFQPYIMADI YSFGLIIWEM ARRCITGGIV EEYQLPYYNM VPSDPSYEDM REVVCVKRLR
     PIVSNRWNSD ECLRAVLKLM SECWAHNPAS RLTALRIKKT LAKMVESQDV KI
//
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