[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Holstein; TISSUE=Testis; DOI=10.1016/0303-7207(94)90179-1; PubMed=7534730 [NCBI, ExPASy, EBI, Israel, Japan] Ethier J.-F., Houde A., Lussier J.G., Silversides D.W.; "Bovine activin receptor type II cDNA: cloning and tissue expression."; Mol. Cell. Endocrinol. 106:1-8(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ovary; DOI=10.1007/s003359900258; PubMed=8875905 [NCBI, ExPASy, EBI, Israel, Japan] Monteagudo L.V., Heriz A., Flavin N., Rogers M., Ennis S., Arruga M.V.; "Fluorescent in situ localization of the bovine activin receptor type IIA locus on chromosome 2 (2q2.3-2.4)."; Mamm. Genome 7:869-869(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Fetal muscle; NIH - Mammalian Gene Collection (MGC) project; Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.

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 (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
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

L21717; AAA74597.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U43208; AAC48694.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC140605; AAI40606.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I45850; I45850.

NP_776652.1; -.

3D structure databases

HSSP

P27038; 1BTE. [HSSP ENTRY / PDB]

SMR

Q28043; 26-119.

ModBase

Q28043.

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.
IPR008271; Ser_thr_pkin_AS.
Graphical view of domain structure.

PANTHER

PTHR23255:SF10; Activin_II_recpt_C; 1.

Pfam

PF01064; Activin_recp; 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).

BLOCKS

Q28043.

Genome annotation databases

Ensembl

ENSBTAG00000018114; Bos taurus. [Contig view]

GeneID

281598; -.

KEGG

bta:281598; -.

Phylogenomic databases

HOVERGEN

Q28043; -.

Other

ProtoNet

Q28043.

UniRef

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

Keywords

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_0000024397`
`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...) (Potential).`
`CARBOHYD`	`66 66`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`30 60`		`By similarity.`
`DISULFID`	`50 78`		`By similarity.`
`DISULFID`	`85 104`		`By similarity.`
`DISULFID`	`91 103`		`By similarity.`
`DISULFID`	`105 110`		`By similarity.`

Sequence information

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

Molecular weight: 57952 Da [This is the MW of the unprocessed precursor]

CRC64: C2969A54CF00617B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGAAAKLAFA VFLISCSSGA ILGRSETQEC IFYNANWERD RTNRTGVESC YGDKDKRRHC 

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

       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

Q28043 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