[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Swiss; TISSUE=Embryo; DOI=10.1210/en.136.6.2652; PubMed=7750489 [NCBI, ExPASy, EBI, Israel, Japan] Dewulf N., Verschueren K., Lonnoy O., Moren A., Grimsby S., Spiegle K., Miyazono K., Huylebroeck D., ten Dijke P.; "Distinct spatial and temporal expression patterns of two type I receptors for bone morphogenetic proteins during mouse embryogenesis."; Endocrinology 136:2652-2663(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Brain; PubMed=7937936 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki A., Thies R.S., Yamaji N., Song J.J., Wozney J., Murakami K., Kung H.; "A truncated bone morphogenetic protein receptor affects dorsal-ventral patterning in the early Xenopus embryo."; Proc. Natl. Acad. Sci. U.S.A. 91:10255-10259(1994).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8065329 [NCBI, ExPASy, EBI, Israel, Japan] Koenig B.B., Cook J.S., Wolsing D.H., Ting J., Tiesman J.P., Correa P.E., Olson C.A., Pecquet A.L., Ventura F., Grant R.A., Chen G., Wrana J.L., Massague J., Rosenbaum J.S.; "Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells."; Mol. Cell. Biol. 14:5961-5974(1994).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Retina; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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 BMP-2 and BMP-4.
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
TISSUE SPECIFICITY: Widely expressed.
SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
SIMILARITY: Contains 1 GS domain.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z23154; CAA80678.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D16250; BAA03769.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U04672; AAA21514.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC042611; AAH42611.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A56238; A56238.

NP_033888.2; -.

3D structure databases

HSSP

P36894; 1ES7. [HSSP ENTRY / PDB]

SMR

P36895; 55-146.

ModBase

P36895.

Protein-protein interaction databases

DIP

DIP:5796N; -.

Organism-specific databases

MGI

MGI:1338938; Bmpr1a.

Gene expression databases

ArrayExpress

P36895; -.

CleanEx

MM_BMPR1A; -.

GermOnline

ENSMUSG00000021796; Mus musculus.

Ontologies

GO:0009952;	Biological process: anterior/posterior pattern formation (inferred from mutant phenotype from MGI).
GO:0030509;	Biological process: BMP signaling pathway (inferred from mutant phenotype from MGI).
GO:0051216;	Biological process: cartilage development (inferred from mutant phenotype from MGI).
GO:0009950;	Biological process: dorsal/ventral axis specification (inferred from mutant phenotype from MGI).
GO:0007398;	Biological process: ectoderm development (inferred from mutant phenotype from MGI).
GO:0048598;	Biological process: embryonic morphogenesis (inferred from mutant phenotype from MGI).
GO:0007507;	Biological process: heart development (inferred from mutant phenotype from MGI).
GO:0035137;	Biological process: hindlimb morphogenesis (inferred from mutant phenotype from MGI).
GO:0030324;	Biological process: lung development (inferred from mutant phenotype from MGI).
GO:0048382;	Biological process: mesendoderm development (inferred from mutant phenotype from MGI).
GO:0001707;	Biological process: mesoderm formation (inferred from mutant phenotype from MGI).
GO:0001880;	Biological process: Mullerian duct regression (inferred from mutant phenotype from MGI).
GO:0050768;	Biological process: negative regulation of neurogenesis (inferred from mutant phenotype from MGI).
GO:0042475;	Biological process: odontogenesis of dentine-containing tooth (inferred from mutant phenotype from MGI).
GO:0060021;	Biological process: palate development (inferred from mutant phenotype from MGI).
GO:0050679;	Biological process: positive regulation of epithelial cell proliferation (inferred from mutant phenotype from MGI).
GO:0002053;	Biological process: positive regulation of mesenchymal cell proliferation (inferred from mutant phenotype from MGI).
GO:0019827;	Biological process: stem cell maintenance (inferred from mutant phenotype from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR003605; TGF_beta_rcpt_GS.
Graphical view of domain structure.

Pfam

PF01064; Activin_recp; 1.
PF00069; Pkinase; 1.
PF08515; TGF_beta_GS; 1.
Pfam graphical view of domain structure.

PRINTS

PR00653; ACTIVIN2R.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00467; GS; 1.
SMART graphical view of domain structure.

PROSITE

PS51256; GS; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P36895.

Genome annotation databases

Ensembl

ENSMUSG00000021796; Mus musculus. [Contig view]

GeneID

12166; -.

KEGG

mmu:12166; -.

Phylogenomic databases

HOGENOM

P36895; -.

HOVERGEN

P36895; -.

Other

SOURCE

Bmpr1a; Mus musculus.

ProtoNet

P36895.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`	`Potential.`
`CHAIN`	`24 532`	`509`	`Bone morphogenetic protein receptor type-1A.`	`PRO_0000024411`
`TOPO_DOM`	`24 152`	`129`	`Extracellular (Potential).`
`TRANSMEM`	`153 176`	`24`	`Potential.`
`TOPO_DOM`	`177 532`	`356`	`Cytoplasmic (Potential).`
`DOMAIN`	`204 233`	`30`	`GS.`
`DOMAIN`	`234 525`	`292`	`Protein kinase.`
`NP_BIND`	`240 248`	`9`	`ATP (By similarity).`
`ACT_SITE`	`362 362`		`Proton acceptor (By similarity).`
`BINDING`	`261 261`		`ATP (By similarity).`
`MOD_RES`	`215 215`		`Phosphoserine (By similarity).`
`MOD_RES`	`216 216`		`Phosphoserine (By similarity).`
`MOD_RES`	`218 218`		`Phosphoserine (By similarity).`
`MOD_RES`	`220 220`		`Phosphoserine (By similarity).`
`CARBOHYD`	`73 73`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`61 82`		`By similarity.`
`DISULFID`	`63 67`		`By similarity.`
`DISULFID`	`76 100`		`By similarity.`
`DISULFID`	`110 124`		`By similarity.`
`DISULFID`	`125 130`		`By similarity.`

Sequence information

Length: 532 AA [This is the length of the unprocessed precursor]

Molecular weight: 60063 Da [This is the MW of the unprocessed precursor]

CRC64: 70CC83CFB07CE9D5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTQLYTYIRL LGACLFIISH VQGQNLDSML HGTGMKSDLD QKKPENGVTL APEDTLPFLK 

        70         80         90        100        110        120 
CYCSGHCPDD AINNTCITNG HCFAIIEEDD QGETTLTSGC MKYEGSDFQC KDSPKAQLRR 

       130        140        150        160        170        180 
TIECCRTNLC NQYLQPTLPP VVIGPFFDGS IRWLVVLISM AVCIVAMIIF SSCFCYKHYC 

       190        200        210        220        230        240 
KSISSRGRYN RDLEQDEAFI PVGESLKDLI DQSQSSGSGS GLPLLVQRTI AKQIQMVRQV 

       250        260        270        280        290        300 
GKGRYGEVWM GKWRGEKVAV KVFFTTEEAS WFRETEIYQT VLMRHENILG FIAADIKGTG 

       310        320        330        340        350        360 
SWTQLYLITD YHENGSLYDF LKCATLDTRA LLKLAYSAAC GLCHLHTEIY GTQGKPAIAH 

       370        380        390        400        410        420 
RDLKSKNILI KKNGSCCIAD LGLAVKFNSD TNEVDIPLNT RVGTKRYMAP EVLDESLNKN 

       430        440        450        460        470        480 
HFQPYIMADI YSFGLIIWEM ARRCITGGIV EEYQLPYYNM VPSDPSYEDM REVVCVKRLR 

       490        500        510        520        530 
PIVSNRWNSD ECLRAVLKLM SECWAHNPAS RLTALRIKKT LAKMVESQDV KI

P36895 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools