[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0092-8674(91)90549-E; PubMed=1646080 [NCBI, ExPASy, EBI, Israel, Japan] Mathews L.S., Vale W.W.; "Expression cloning of an activin receptor, a predicted transmembrane serine kinase."; Cell 65:973-982(1991).
[2]	X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-121. DOI=10.1038/4887; PubMed=9886286 [NCBI, ExPASy, EBI, Israel, Japan] Greenwald J., Fischer W.H., Vale W.W., Choe S.; "Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase."; Nat. Struct. Biol. 6:18-22(1999).
[3]	DISULFIDE BONDS IN EXTRACELLULAR DOMAIN. DOI=10.1023/A:1020640725959; PubMed=10449041 [NCBI, ExPASy, EBI, Israel, Japan] Fischer W.H., Greenwald J., Park M., Craig A.G., Choe S., Vale W.; "The disulfide bond arrangement in the extracellular domain of the activin type II receptor."; J. Protein Chem. 18:437-446(1999).
[4]	INTERACTION WITH AIP1, AND IDENTIFICATION IN A COMPLEX WITH ACVR1B; AIP1 AND SMAD3. DOI=10.1074/jbc.275.8.5485; PubMed=10681527 [NCBI, ExPASy, EBI, Israel, Japan] Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z., Nakamura T., Sugino H.; "Identification and characterization of a PDZ protein that interacts with activin types II receptors."; J. Biol. Chem. 275:5485-5492(2000).

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 activin A, activin B and inhibin A.
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBUNIT: Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3.
INTERACTION:
P18075:BMP7 (xeno); NbExp=1; IntAct=EBI-1036102, EBI-1035195;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
TISSUE SPECIFICITY: Brain, testis, intestine, liver and kidney.
SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.
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

M65287; AAA37171.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A39896; A39896.

NP_031422.3; -.

3D structure databases

PDB

1BTE; X-ray; 1.50 A; A/B=25-121.	[ExPASy / RCSB / EBI]
1LX5; X-ray; 3.30 A; B=20-121.	[ExPASy / RCSB / EBI]
2GOO; X-ray; 2.20 A; C/F=20-121.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1BTE; -.
1LX5; -.
2GOO; -.

ModBase

P27038.

Protein-protein interaction databases

DIP

DIP:5825N; -.

IntAct

P27038; -.

PTM databases

PhosphoSite

P27038; -.

Organism-specific databases

MGI

MGI:102806; Acvr2a.

Gene expression databases

ArrayExpress

P27038; -.

CleanEx

MM_ACVR2A; -.

GermOnline

ENSMUSG00000052155; Mus musculus.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0048185;	Molecular function: activin binding (inferred from physical interaction from MGI).
GO:0017002;	Molecular function: activin receptor activity (inferred from electronic annotation from InterPro).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0019838;	Molecular function: growth factor binding (inferred from mutant phenotype from MGI).
GO:0048186;	Molecular function: inhibin beta-A binding (inferred from direct assay from HGNC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0043621;	Molecular function: protein self-association (inferred from physical interaction from MGI).
GO:0009952;	Biological process: anterior/posterior pattern formation (inferred from genetic interaction from MGI).
GO:0007368;	Biological process: determination of left/right symmetry (inferred from genetic interaction from MGI).
GO:0048706;	Biological process: embryonic skeletal system development (inferred from mutant phenotype from MGI).
GO:0001702;	Biological process: gastrulation with mouth forming second (inferred from genetic interaction from MGI).
GO:0007498;	Biological process: mesoderm development (inferred from mutant phenotype from MGI).
GO:0043084;	Biological process: penile erection (inferred from mutant phenotype from MGI).
GO:0006468;	Biological process: protein amino acid phosphorylation (inferred from electronic annotation from InterPro).
GO:0030510;	Biological process: regulation of BMP signaling pathway (inferred from mutant phenotype from MGI).
GO:0050999;	Biological process: regulation of nitric-oxide synthase activity (inferred from mutant phenotype from MGI).
GO:0060011;	Biological process: Sertoli cell proliferation (inferred from mutant phenotype from MGI).
GO:0042713;	Biological process: sperm ejaculation (inferred from mutant phenotype from MGI).
GO:0007283;	Biological process: spermatogenesis (inferred from genetic interaction from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR015768; Activin_II_recpt_C.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_bd_CS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.

PANTHER

PTHR23255:SF10; Activin_II_recpt_C; 1.

Pfam

PF01064; Activin_recp; 1.
PF00069; Pkinase; 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]

PROSITE

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

ProtoNet

P27038.

Genome annotation databases

Ensembl

ENSMUSG00000052155; Mus musculus. [Contig view]

GeneID

11480; -.

KEGG

mmu:11480; -.

Phylogenomic databases

HOGENOM

P27038; -.

HOVERGEN

P27038; -.

Other

LinkHub

P27038; -.

NextBio

278828; -.

SOURCE

Acvr2a; Mus musculus.

UniRef

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

Keywords

3D-structure; ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane; Metal-binding; Nucleotide-binding; Receptor; Serine/threonine-protein kinase; Signal; Transferase; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 513`	`494`	`Activin receptor type-2A.`	`PRO_0000024399`
`TOPO_DOM`	`20 135`	`116`	`Extracellular (Potential).`
`TRANSMEM`	`136 161`	`26`	`Potential.`
`TOPO_DOM`	`162 513`	`352`	`Cytoplasmic (Potential).`
`DOMAIN`	`192 485`	`294`	`Protein kinase.`
`NP_BIND`	`198 206`	`9`	`ATP (By similarity).`
`ACT_SITE`	`322 322`		`Proton acceptor (By similarity).`
`BINDING`	`219 219`		`ATP (By similarity).`
`CARBOHYD`	`43 43`		`N-linked (GlcNAc...).`
`CARBOHYD`	`66 66`		`N-linked (GlcNAc...).`
`DISULFID`	`30 60`
`DISULFID`	`50 78`
`DISULFID`	`85 104`
`DISULFID`	`91 103`
`DISULFID`	`105 110`
`STRAND`	`29 34`	`6`
`HELIX`	`37 40`	`4`
`STRAND`	`44 49`	`6`
`STRAND`	`59 67`	`9`
`STRAND`	`70 79`	`10`
`STRAND`	`88 93`	`6`
`STRAND`	`95 97`	`3`
`STRAND`	`99 105`	`7`
`HELIX`	`110 112`	`3`
`STRAND`	`113 116`	`4`

Sequence information

Length: 513 AA [This is the length of the unprocessed precursor]

Molecular weight: 57890 Da [This is the MW of the unprocessed precursor]

CRC64: 475CD292506BAC61 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWERD RTNQTGVEPC YGDKDKRRHC 

        70         80         90        100        110        120 
FATWKNISGS IEIVKQGCWL DDINCYDRTD CIEKKDSPEV YFCCCEGNMC NEKFSYFPEM 

       130        140        150        160        170        180 
EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI AGIVICAFWV YRHHKMAYPP VLVPTQDPGP 

       190        200        210        220        230        240 
PPPSPLLGLK PLQLLEVKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG 

       250        260        270        280        290        300 
MKHENILQFI GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL 

       310        320        330        340        350        360 
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG KSAGDTHGQV 

       370        380        390        400        410        420 
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR CTAADGPVDE YMLPFEEEIG 

       430        440        450        460        470        480 
QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG MAMLCETIEE CWDHDAEARL SAGCVGERIT 

       490        500        510 
QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL

P27038 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