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Bone morphogenetic protein receptor type-1A (BMP type-1A receptor) (BMPR-1A) (EC 2.7.11.30) (Activin receptor-like kinase 3) (ALK-3) (Serine/threonine-protein kinase receptor R5) (SKR5) (CD antigen CD292)

 BMR1A_HUMAN             Reviewed;         532 AA.
P36894; A8K6U9; Q8NEN8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 2.
22-NOV-2017, entry version 209.
RecName: Full=Bone morphogenetic protein receptor type-1A;
Short=BMP type-1A receptor;
Short=BMPR-1A;
EC=2.7.11.30;
AltName: Full=Activin receptor-like kinase 3;
Short=ALK-3;
AltName: Full=Serine/threonine-protein kinase receptor R5;
Short=SKR5;
AltName: CD_antigen=CD292;
Flags: Precursor;
Name=BMPR1A; Synonyms=ACVRLK3, ALK3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-2.
TISSUE=Placenta;
PubMed=8397373;
ten Dijke P., Ichijo H., Franzen P., Schulz P., Saras J.,
Toyoshima H., Heldin C.-H., Miyazono K.;
"Activin receptor-like kinases: a novel subclass of cell-surface
receptors with predicted serine/threonine kinase activity.";
Oncogene 8:2879-2887(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-2.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH BMP2, AND MUTAGENESIS OF 107-ASP--GLN-109.
PubMed=22799562; DOI=10.1021/bi300942x;
Mahlawat P., Ilangovan U., Biswas T., Sun L.Z., Hinck A.P.;
"Structure of the Alk1 extracellular domain and characterization of
its bone morphogenetic protein (BMP) binding properties.";
Biochemistry 51:6328-6341(2012).
[5]
INTERACTION WITH GDF5.
PubMed=24098149; DOI=10.1371/journal.pgen.1003846;
Degenkolbe E., Konig J., Zimmer J., Walther M., Reissner C.,
Nickel J., Ploger F., Raspopovic J., Sharpe J., Dathe K., Hecht J.T.,
Mundlos S., Doelken S.C., Seemann P.;
"A GDF5 point mutation strikes twice--causing BDA1 and SYNS2.";
PLoS Genet. 9:E1003846-E1003846(2013).
[6]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 55-143 IN COMPLEX WITH BMP2,
DISULFIDE BOND, AND INTERACTION WITH BMP2.
PubMed=10881198; DOI=10.1038/75903;
Kirsch T., Sebald W., Dreyer M.K.;
"Crystal structure of the BMP-2-BRIA ectodomain complex.";
Nat. Struct. Biol. 7:492-496(2000).
[7]
DISEASE.
PubMed=11381269; DOI=10.1038/88919;
Howe J.R., Bair J.L., Sayed M.G., Anderson M.E., Mitros F.A.,
Petersen G.M., Velculescu V.E., Traverso G., Vogelstein B.;
"Germline mutations of the gene encoding bone morphogenetic protein
receptor 1A in juvenile polyposis.";
Nat. Genet. 28:184-187(2001).
[8]
STRUCTURE BY NMR OF 51-152, DISULFIDE BONDS, AND INTERACTION WITH
BMP2.
PubMed=18937504; DOI=10.1021/bi801059j;
Klages J., Kotzsch A., Coles M., Sebald W., Nickel J., Muller T.,
Kessler H.;
"The solution structure of BMPR-IA reveals a local disorder-to-order
transition upon BMP-2 binding.";
Biochemistry 47:11930-11939(2008).
[9]
VARIANTS JPS ARG-124; ASP-338 AND TYR-376.
PubMed=11536076; DOI=10.1086/323703;
Zhou X.-P., Woodford-Richens K., Lehtonen R., Kurose K., Aldred M.,
Hampel H., Launonen V., Virta S., Pilarski R., Salovaara R.,
Bodmer W.F., Conrad B.A., Dunlop M., Hodgson S.V., Iwama T.,
Jaervinen H., Kellokumpu I., Kim J.C., Leggett B., Markie D.,
Mecklin J.-P., Neale K., Phillips R., Piris J., Rozen P.,
Houlston R.S., Aaltonen L.A., Tomlinson I.P.M., Eng C.;
"Germline mutations in BMPR1A/ALK3 cause a subset of cases of juvenile
polyposis syndrome and of Cowden and Bannayan-Riley-Ruvalcaba
syndromes.";
Am. J. Hum. Genet. 69:704-711(2001).
[10]
VARIANTS JPS ASP-62; TYR-82 AND CYS-443.
PubMed=12417513; DOI=10.1007/BF02557528;
Sayed M.G., Ahmed A.F., Ringold J.R., Anderson M.E., Bair J.L.,
Mitros F.A., Lynch H.T., Tinley S.T., Petersen G.M., Giardiello F.M.,
Vogelstein B., Howe J.R.;
"Germline SMAD4 or BMPR1A mutations and phenotype of juvenile
polyposis.";
Ann. Surg. Oncol. 9:901-906(2002).
[11]
VARIANT JPS ARG-130.
PubMed=12136244; DOI=10.1007/s00439-002-0748-9;
Friedl W., Uhlhaas S., Schulmann K., Stolte M., Loff S., Back W.,
Mangold E., Stern M., Knaebel H.P., Sutter C., Weber R.G.,
Pistorius S., Burger B., Propping P.;
"Juvenile polyposis: massive gastric polyposis is more common in MADH4
mutation carriers than in BMPR1A mutation carriers.";
Hum. Genet. 111:108-111(2002).
[12]
VARIANT JPS THR-470.
PubMed=12630959; DOI=10.1034/j.1399-0004.2003.00008.x;
Kim I.J., Park J.H., Kang H.C., Kim K.H., Kim J.H., Ku J.L.,
Kang S.B., Park S.Y., Lee J.S., Park J.G.;
"Identification of a novel BMPR1A germline mutation in a Korean
juvenile polyposis patient without SMAD4 mutation.";
Clin. Genet. 63:126-130(2003).
[13]
INVOLVEMENT IN JUVENILE POLYPOSIS OF INFANCY.
PubMed=16685657; DOI=10.1086/504301;
Delnatte C., Sanlaville D., Mougenot J.-F., Vermeesch J.-R.,
Houdayer C., Blois M.-C., Genevieve D., Goulet O., Fryns J.-P.,
Jaubert F., Vekemans M., Lyonnet S., Romana S., Eng C.,
Stoppa-Lyonnet D.;
"Contiguous gene deletion within chromosome arm 10q is associated with
juvenile polyposis of infancy, reflecting cooperation between the
BMPR1A and PTEN tumor-suppressor genes.";
Am. J. Hum. Genet. 78:1066-1074(2006).
[14]
INVOLVEMENT IN HEREDITARY MIXED POLYPOSIS SYNDROME 2.
PubMed=16525031; DOI=10.1136/jmg.2005.034827;
Cao X., Eu K.W., Kumarasinghe M.P., Li H.H., Loi C., Cheah P.Y.;
"Mapping of hereditary mixed polyposis syndrome (HMPS) to chromosome
10q23 by genomewide high-density single nucleotide polymorphism (SNP)
scan and identification of BMPR1A loss of function.";
J. Med. Genet. 43:E13-E13(2006).
[15]
VARIANTS [LARGE SCALE ANALYSIS] THR-2; TYR-58; CYS-443; MET-450 AND
GLN-486.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[16]
VARIANT THR-460.
PubMed=25860647; DOI=10.1007/s10689-015-9803-2;
Hansen M.F., Johansen J., Bjoernevoll I., Sylvander A.E.,
Steinsbekk K.S., Saetrom P., Sandvik A.K., Drabloes F., Sjursen W.;
"A novel POLE mutation associated with cancers of colon, pancreas,
ovaries and small intestine.";
Fam. Cancer 14:437-448(2015).
-!- 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. Receptor for BMP2, BMP4, GDF5 and
GDF6. Positively regulates chondrocyte differentiation through
GDF5 interaction. Mediates induction of adipogenesis by GDF6.
{ECO:0000250|UniProtKB:P36895}.
-!- 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 BMP2 (PubMed:10881198, PubMed:18937504).
Interacts with low affinity with GDF5; positively regulates
chondrocyte differentiation (PubMed:24098149).
{ECO:0000269|PubMed:10881198, ECO:0000269|PubMed:18937504,
ECO:0000269|PubMed:24098149}.
-!- INTERACTION:
P12643:BMP2; NbExp=17; IntAct=EBI-1029237, EBI-1029262;
P12644:BMP4; NbExp=2; IntAct=EBI-1029237, EBI-1998134;
P43026:GDF5; NbExp=3; IntAct=EBI-1029237, EBI-8571476;
Q8WYB5:KAT6B; NbExp=4; IntAct=EBI-1029237, EBI-948029;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle.
-!- DISEASE: Juvenile polyposis syndrome (JPS) [MIM:174900]: Autosomal
dominant gastrointestinal hamartomatous polyposis syndrome in
which patients are at risk for developing gastrointestinal
cancers. The lesions are typified by a smooth histological
appearance, predominant stroma, cystic spaces and lack of a smooth
muscle core. Multiple juvenile polyps usually occur in a number of
Mendelian disorders. Sometimes, these polyps occur without
associated features as in JPS; here, polyps tend to occur in the
large bowel and are associated with an increased risk of colon and
other gastrointestinal cancers. {ECO:0000269|PubMed:11536076,
ECO:0000269|PubMed:12136244, ECO:0000269|PubMed:12417513,
ECO:0000269|PubMed:12630959}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Polyposis syndrome, mixed hereditary 2 (HMPS2)
[MIM:610069]: A disease is characterized by atypical juvenile
polyps, colonic adenomas, and colorectal carcinomas. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=A microdeletion of chromosome 10q23 involving BMPR1A
and PTEN is a cause of chromosome 10q23 deletion syndrome, which
shows overlapping features of the following three disorders:
Bannayan-Zonana syndrome, Cowden disease and juvenile polyposis
syndrome. {ECO:0000269|PubMed:11381269,
ECO:0000269|PubMed:16525031}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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EMBL; Z22535; CAA80257.1; -; mRNA.
EMBL; AK291764; BAF84453.1; -; mRNA.
EMBL; BC028383; AAH28383.1; -; mRNA.
CCDS; CCDS7378.1; -.
PIR; I37163; I37163.
RefSeq; NP_004320.2; NM_004329.2.
RefSeq; XP_011538405.1; XM_011540103.2.
RefSeq; XP_011538406.1; XM_011540104.2.
UniGene; Hs.524477; -.
PDB; 1ES7; X-ray; 2.90 A; B/D=55-143.
PDB; 1REW; X-ray; 1.86 A; C/D=24-152.
PDB; 2GOO; X-ray; 2.20 A; B/E=24-152.
PDB; 2H62; X-ray; 1.85 A; C=24-152.
PDB; 2H64; X-ray; 1.92 A; B=24-152.
PDB; 2K3G; NMR; -; A=51-152.
PDB; 2QJ9; X-ray; 2.44 A; C/D=24-152.
PDB; 2QJA; X-ray; 2.60 A; C/D=24-152.
PDB; 2QJB; X-ray; 2.50 A; C/D=24-152.
PDB; 3NH7; X-ray; 2.70 A; A/B/C/D=24-152.
PDB; 3QB4; X-ray; 2.28 A; B/D=24-152.
PDBsum; 1ES7; -.
PDBsum; 1REW; -.
PDBsum; 2GOO; -.
PDBsum; 2H62; -.
PDBsum; 2H64; -.
PDBsum; 2K3G; -.
PDBsum; 2QJ9; -.
PDBsum; 2QJA; -.
PDBsum; 2QJB; -.
PDBsum; 3NH7; -.
PDBsum; 3QB4; -.
ProteinModelPortal; P36894; -.
SMR; P36894; -.
BioGrid; 107125; 76.
CORUM; P36894; -.
DIP; DIP-5793N; -.
IntAct; P36894; 31.
MINT; MINT-124304; -.
STRING; 9606.ENSP00000224764; -.
BindingDB; P36894; -.
ChEMBL; CHEMBL5275; -.
GuidetoPHARMACOLOGY; 1786; -.
iPTMnet; P36894; -.
PhosphoSitePlus; P36894; -.
BioMuta; BMPR1A; -.
DMDM; 61252444; -.
EPD; P36894; -.
MaxQB; P36894; -.
PaxDb; P36894; -.
PeptideAtlas; P36894; -.
PRIDE; P36894; -.
DNASU; 657; -.
Ensembl; ENST00000372037; ENSP00000361107; ENSG00000107779.
Ensembl; ENST00000635816; ENSP00000489707; ENSG00000107779.
Ensembl; ENST00000636056; ENSP00000490273; ENSG00000107779.
Ensembl; ENST00000638429; ENSP00000492290; ENSG00000107779.
GeneID; 657; -.
KEGG; hsa:657; -.
UCSC; uc001kdy.4; human.
CTD; 657; -.
DisGeNET; 657; -.
EuPathDB; HostDB:ENSG00000107779.11; -.
GeneCards; BMPR1A; -.
GeneReviews; BMPR1A; -.
HGNC; HGNC:1076; BMPR1A.
HPA; CAB019398; -.
MalaCards; BMPR1A; -.
MIM; 174900; phenotype.
MIM; 601299; gene.
MIM; 610069; phenotype.
MIM; 612242; phenotype.
neXtProt; NX_P36894; -.
OpenTargets; ENSG00000107779; -.
Orphanet; 329971; Generalized juvenile polyposis/juvenile polyposis coli.
Orphanet; 157794; Hereditary mixed polyposis syndrome.
Orphanet; 144; Hereditary nonpolyposis colon cancer.
Orphanet; 79076; Juvenile polyposis of infancy.
PharmGKB; PA25386; -.
eggNOG; KOG2052; Eukaryota.
eggNOG; ENOG410XQT0; LUCA.
GeneTree; ENSGT00760000118876; -.
HOGENOM; HOG000230587; -.
HOVERGEN; HBG054502; -.
InParanoid; P36894; -.
KO; K04673; -.
OMA; EVVCVKG; -.
OrthoDB; EOG091G0BIU; -.
PhylomeDB; P36894; -.
TreeFam; TF314724; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-201451; Signaling by BMP.
SignaLink; P36894; -.
SIGNOR; P36894; -.
ChiTaRS; BMPR1A; human.
EvolutionaryTrace; P36894; -.
GeneWiki; BMPR1A; -.
GenomeRNAi; 657; -.
PRO; PR:P36894; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000107779; -.
CleanEx; HS_BMPR1A; -.
ExpressionAtlas; P36894; baseline and differential.
Genevisible; P36894; HS.
GO; GO:0030425; C:dendrite; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
GO; GO:1990712; C:HFE-transferrin receptor complex; IC:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:HGNC.
GO; GO:0098821; F:BMP receptor activity; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:HGNC.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0046332; F:SMAD binding; IDA:HGNC.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; TAS:Reactome.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0061312; P:BMP signaling pathway involved in heart development; IC:BHF-UCL.
GO; GO:0003161; P:cardiac conduction system development; ISS:BHF-UCL.
GO; GO:0003215; P:cardiac right ventricle morphogenesis; ISS:BHF-UCL.
GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0048589; P:developmental growth; IEA:Ensembl.
GO; GO:0035912; P:dorsal aorta morphogenesis; ISS:BHF-UCL.
GO; GO:0009950; P:dorsal/ventral axis specification; IEA:Ensembl.
GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
GO; GO:0048568; P:embryonic organ development; IEA:Ensembl.
GO; GO:0003272; P:endocardial cushion formation; ISS:BHF-UCL.
GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:BHF-UCL.
GO; GO:1905285; P:fibrous ring of heart morphogenesis; ISS:BHF-UCL.
GO; GO:0060914; P:heart formation; IEA:Ensembl.
GO; GO:0035137; P:hindlimb morphogenesis; IEA:Ensembl.
GO; GO:0006955; P:immune response; IMP:BHF-UCL.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0048368; P:lateral mesoderm development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0048382; P:mesendoderm development; IEA:Ensembl.
GO; GO:0001707; P:mesoderm formation; IEA:Ensembl.
GO; GO:0003183; P:mitral valve morphogenesis; ISS:BHF-UCL.
GO; GO:0001880; P:Mullerian duct regression; IEA:Ensembl.
GO; GO:0050768; P:negative regulation of neurogenesis; IEA:Ensembl.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IMP:BHF-UCL.
GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
GO; GO:0021998; P:neural plate mediolateral regionalization; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0003151; P:outflow tract morphogenesis; ISS:BHF-UCL.
GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:BHF-UCL.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0048352; P:paraxial mesoderm structural organization; IEA:Ensembl.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; ISS:BHF-UCL.
GO; GO:0021983; P:pituitary gland development; IEA:Ensembl.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:1904414; P:positive regulation of cardiac ventricle development; ISS:BHF-UCL.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IMP:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:HGNC.
GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
GO; GO:2000772; P:regulation of cellular senescence; IEA:Ensembl.
GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IEA:Ensembl.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:ProtInc.
GO; GO:0003186; P:tricuspid valve morphogenesis; ISS:BHF-UCL.
GO; GO:0003223; P:ventricular compact myocardium morphogenesis; ISS:BHF-UCL.
GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; ISS:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR003605; GS_dom.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF08515; TGF_beta_GS; 1.
SMART; SM00467; GS; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51256; GS; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
Metal-binding; Nucleotide-binding; Polymorphism; Receptor;
Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 532 Bone morphogenetic protein receptor type-
1A.
/FTId=PRO_0000024410.
TOPO_DOM 24 152 Extracellular. {ECO:0000255}.
TRANSMEM 153 176 Helical. {ECO:0000255}.
TOPO_DOM 177 532 Cytoplasmic. {ECO:0000255}.
DOMAIN 204 233 GS. {ECO:0000255|PROSITE-
ProRule:PRU00585}.
DOMAIN 234 525 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 240 248 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 107 109 Mediates specificity for BMP ligand.
{ECO:0000269|PubMed:22799562}.
ACT_SITE 362 362 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 261 261 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 61 82 {ECO:0000269|PubMed:10881198,
ECO:0000269|PubMed:18937504}.
DISULFID 63 67 {ECO:0000269|PubMed:10881198,
ECO:0000269|PubMed:18937504}.
DISULFID 76 100 {ECO:0000269|PubMed:10881198,
ECO:0000269|PubMed:18937504}.
DISULFID 110 124 {ECO:0000269|PubMed:10881198,
ECO:0000269|PubMed:18937504}.
DISULFID 125 130 {ECO:0000269|PubMed:10881198,
ECO:0000269|PubMed:18937504}.
VARIANT 2 2 P -> T (in dbSNP:rs11528010).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:8397373}.
/FTId=VAR_041397.
VARIANT 58 58 F -> Y (in a renal clear cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041398.
VARIANT 62 62 Y -> D (in JPS).
{ECO:0000269|PubMed:12417513}.
/FTId=VAR_022828.
VARIANT 82 82 C -> Y (in JPS).
{ECO:0000269|PubMed:12417513}.
/FTId=VAR_022829.
VARIANT 124 124 C -> R (in JPS; dbSNP:rs199476087).
{ECO:0000269|PubMed:11536076}.
/FTId=VAR_015533.
VARIANT 130 130 C -> R (in JPS).
{ECO:0000269|PubMed:12136244}.
/FTId=VAR_022830.
VARIANT 338 338 A -> D (in JPS; dbSNP:rs199476086).
{ECO:0000269|PubMed:11536076}.
/FTId=VAR_015534.
VARIANT 376 376 C -> Y (in JPS; dbSNP:rs199476088).
{ECO:0000269|PubMed:11536076}.
/FTId=VAR_015535.
VARIANT 443 443 R -> C (in JPS; dbSNP:rs35619497).
{ECO:0000269|PubMed:12417513,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_022831.
VARIANT 450 450 V -> M (in dbSNP:rs55932635).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041399.
VARIANT 460 460 M -> T (found in a patient with tubular
adenoma and rectal neuroendocrine tumor;
unknown pathological significance;
dbSNP:rs758309022).
{ECO:0000269|PubMed:25860647}.
/FTId=VAR_077353.
VARIANT 470 470 M -> T (in JPS; dbSNP:rs199476089).
{ECO:0000269|PubMed:12630959}.
/FTId=VAR_022832.
VARIANT 486 486 R -> Q (in a gastric adenocarcinoma
sample; somatic mutation;
dbSNP:rs752802257).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041400.
MUTAGEN 107 109 DFQ->REL: Affinity for BMP2 decreased by
over 200-fold.
{ECO:0000269|PubMed:22799562}.
STRAND 59 62 {ECO:0000244|PDB:2H62}.
STRAND 64 66 {ECO:0000244|PDB:2H62}.
STRAND 75 88 {ECO:0000244|PDB:2H62}.
STRAND 90 92 {ECO:0000244|PDB:2H62}.
STRAND 94 101 {ECO:0000244|PDB:2H62}.
HELIX 106 111 {ECO:0000244|PDB:2H62}.
STRAND 116 118 {ECO:0000244|PDB:2QJA}.
STRAND 120 125 {ECO:0000244|PDB:2H62}.
HELIX 130 133 {ECO:0000244|PDB:2H62}.
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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