[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0006-291X(92)90535-S; PubMed=1312838 [NCBI, ExPASy, EBI, Israel, Japan] Legerski R., Zhou X., Dresback J., Eberspaecher H., McKinney S., Segarini P., de Crombrugghe B.; "Molecular cloning and characterization of a novel rat activin receptor."; Biochem. Biophys. Res. Commun. 183:672-679(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).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Placenta; 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).
[4]	X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 19-119 IN COMPLEX WITH HUMAN INHBA. DOI=10.1093/emboj/cdg156; PubMed=12660162 [NCBI, ExPASy, EBI, Israel, Japan] Thompson T.B., Woodruff T.K., Jardetzky T.S.; "Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions."; EMBO J. 22:1555-1566(2003).

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 (By similarity).
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (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

L10640; AAA40772.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC097358; AAH97358.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B49193; B49193.
JQ1484; JQ1484.

RefSeq

NP_113742.1; -.

UniGene

Rn.24240

3D structure databases

PDB

1NYS; X-ray; 3.05 A; A/C=19-119.	[ExPASy / RCSB / EBI]
1NYU; X-ray; 3.10 A; A/C=19-119.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

1NYS; -.
1NYU; -.

P38445; 24-117.

Organism-specific databases

RGD

2028; Acvr2b.

GeneLynx

Acvr2b; Rattus norvegicus.

Gene expression databases

ArrayExpress

P38445; -.

GermOnline

ENSRNOG00000014477; 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

P38445.

Genome annotation databases

Ensembl

ENSRNOG00000014477; Rattus norvegicus. [Contig view]

GeneID

25366; -.

KEGG

rno:25366; -.

Phylogenomic databases

HOVERGEN

P38445; -.

Other

ProtoNet

P38445.

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 18`	`18`	`Potential.`
`CHAIN`	`19 513`	`495`	`Activin receptor type-2B.`	`PRO_0000024406`
`TOPO_DOM`	`19 137`	`119`	`Extracellular (Potential).`
`TRANSMEM`	`138 158`	`21`	`Potential.`
`TOPO_DOM`	`159 513`	`355`	`Cytoplasmic (Potential).`
`DOMAIN`	`190 481`	`292`	`Protein kinase.`
`NP_BIND`	`196 204`	`9`	`ATP (By similarity).`
`ACT_SITE`	`322 322`		`Proton acceptor (By similarity).`
`BINDING`	`217 217`		`ATP (By similarity).`
`CARBOHYD`	`42 42`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`65 65`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`29 59`		`By similarity.`
`DISULFID`	`49 77`		`By similarity.`
`DISULFID`	`84 103`		`By similarity.`
`DISULFID`	`90 102`		`By similarity.`
`DISULFID`	`104 109`		`By similarity.`
`CONFLICT`	`64 64`		`R -> P (in Ref. 1; AAA40772 and 2).`
`CONFLICT`	`255 255`		`Missing (in Ref. 2 and 3; AAH97358).`
`CONFLICT`	`488 488`		`S -> G (in Ref. 1; AAA40772 and 2).`
`CONFLICT`	`501 501`		`V -> S (in Ref. 1; AAA40772 and 2).`

Sequence information

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

Molecular weight: 57857 Da [This is the MW of the unprocessed precursor]

CRC64: 765DB33F11C64CA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 

        70         80         90        100        110        120 
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEPG 

       130        140        150        160        170        180 
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP 

       190        200        210        220        230        240 
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK 

       250        260        270        280        290        300 
HENLLQFIAA EKRGCSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS 

       310        320        330        340        350        360 
YLHEDVPWCR GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG KPPGDTHGQV 

       370        380        390        400        410        420 
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELVSR CKAADGPVDE YMLPFEEEIG 

       430        440        450        460        470        480 
QHPSLEELQE VVVHKKMRPT IKDHWLKHPG LAQLCVTIEE CWDHDAEARL SAGCVEERVS 

       490        500        510 
LIRRSVNSST SDCLVSLVTS VTNVDLLPKE SSI

P38445 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