[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Ovary; DOI=10.1016/0014-5793(92)81408-E; PubMed=1385212 [NCBI, ExPASy, EBI, Israel, Japan] Shinozaki H., Ito I., Hasegawa Y., Nakamura K., Igarashi S., Nakamura M., Miyamoto K., Eto Y., Ibuki Y., Minegishi T.; "Cloning and sequencing of a rat type II activin receptor."; FEBS Lett. 312:53-56(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; TISSUE=Testis; DOI=10.1210/en.132.6.2593; PubMed=7916681 [NCBI, ExPASy, EBI, Israel, Japan] Feng Z.M., Madigan M.B., Chen C.L.C.; "Expression of type II activin receptor genes in the male and female reproductive tissues of the rat."; Endocrinology 132:2593-2600(1993).

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

S48190; AAB23958.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L10639; AAA40674.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49193; A49193.
S27258; S27258.

RefSeq

NP_113759.1; -.

UniGene

Rn.161783

3D structure databases

PDB

1NYS; X-ray; 3.05 A; A/C=34-114.	[ExPASy / RCSB / EBI]
1NYU; X-ray; 3.10 A; A/C=34-114.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1NYS; -.
1NYU; -.

P38444; 26-119.

Organism-specific databases

RGD

70911; Acvr2a.

GeneLynx

Acvr2a; Rattus norvegicus.

Gene expression databases

ArrayExpress

P38444; -.

GermOnline

ENSRNOG00000005334; Rattus norvegicus.

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

P38444.

Genome annotation databases

Ensembl

ENSRNOG00000005334; Rattus norvegicus. [Contig view]

GeneID

29263; -.

KEGG

rno:29263; -.

Phylogenomic databases

HOVERGEN

P38444; -.

Other

ProtoNet

P38444.

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_0000024401`
`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.`
`CONFLICT`	`165 165`		`M -> K (in Ref. 2; AAB23958).`
`CONFLICT`	`218 218`		`V -> I (in Ref. 2; AAB23958).`
`CONFLICT`	`353 353`		`G -> A (in Ref. 2; AAB23958).`
`CONFLICT`	`475 475`		`L -> V (in Ref. 2; AAB23958).`
`TURN`	`35 41`	`7`
`STRAND`	`44 49`	`6`
`STRAND`	`58 66`	`9`
`STRAND`	`71 80`	`10`
`HELIX`	`83 85`	`3`
`STRAND`	`90 93`	`4`
`STRAND`	`99 105`	`7`
`HELIX`	`110 112`	`3`

Sequence information

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

Molecular weight: 57893 Da [This is the MW of the unprocessed precursor]

CRC64: CE3A8742EF91DD7D [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 YRHHMMAYPP 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 KSGGDTHGQV 

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

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

       490        500        510 
QMQRLTNIIT TEDIVTVVTM VTNVDFPPKE SSL

P38444 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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