[1]	NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE. TISSUE=Embryo; DOI=10.1016/0014-5793(92)80515-I; PubMed=1318847 [NCBI, ExPASy, EBI, Israel, Japan] Ohuchi H., Noji S., Koyama E., Myokai F., Nishikawa K., Nohno T., Tashiro K., Shiokawa K., Matsuo N., Taniguchi S.; "Expression pattern of the activin receptor type IIA gene during differentiation of chick neural tissues, muscle and skin."; FEBS Lett. 303:185-189(1992).
[2]	NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND FUNCTION. TISSUE=Embryo; DOI=10.1006/dbio.1995.0015; PubMed=7589799 [NCBI, ExPASy, EBI, Israel, Japan] Stern C.D., Yu R.T., Kakizuka A., Kintner C.R., Mathews L.S., Vale W.W., Evans R.M., Umesono K.; "Activin and its receptors during gastrulation and the later phases of mesoderm development in the chick embryo."; Dev. Biol. 172:192-205(1995).
[3]	FUNCTION, AND DEVELOPMENTAL STAGE. DOI=10.1002/neu.1019; PubMed=11291100 [NCBI, ExPASy, EBI, Israel, Japan] Kos K., Fine L., Coulombe J.N.; "Activin type II receptors in embryonic dorsal root ganglion neurons of the chicken."; J. Neurobiol. 47:93-108(2001).
[4]	FUNCTION, AND DEVELOPMENTAL STAGE. DOI=10.1016/j.ydbio.2005.05.039; PubMed=16039645 [NCBI, ExPASy, EBI, Israel, Japan] Timmer J., Chesnutt C., Niswander L.; "The activin signaling pathway promotes differentiation of dI3 interneurons in the spinal neural tube."; Dev. Biol. 285:1-10(2005).
[5]	TISSUE SPECIFICITY. DOI=10.1677/joe.1.06303; PubMed=16135664 [NCBI, ExPASy, EBI, Israel, Japan] Lovell T.M., Knight P.G., Gladwell R.T.; "Variation in pituitary expression of mRNAs encoding the putative inhibin co-receptor (betaglycan) and type-I and type-II activin receptors during the chicken ovulatory cycle."; J. Endocrinol. 186:447-455(2005).
[6]	FUNCTION, AND TISSUE SPECIFICITY. DOI=10.1677/joe.1.06525; PubMed=16461550 [NCBI, ExPASy, EBI, Israel, Japan] Lovell T.M., Knight P.G., Gladwell R.T.; "Differential expression of mRNAs encoding the putative inhibin co-receptor (betaglycan) and activin type-I and type-II receptors in preovulatory and prehierarchical follicles of the laying hen ovary."; J. Endocrinol. 188:241-249(2006).

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. May modulate neuropeptide expression in dorsal root ganglia (DRG) neurons and ovarian follicle development.
CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.
COFACTOR: Magnesium or manganese (By similarity).
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein (By similarity).
TISSUE SPECIFICITY: Expressed in hen anterior pituitary during the ovulatory cycle and in the ovarian follicle.
DEVELOPMENTAL STAGE: Expressed during the differentiation of neuroepithelium, of myotomes to muscle and of surface extoderm. Expressed in the dorsal root ganglia (DRG).
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

D31899; BAA06697.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U31222; AAA87841.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S23089; S23089.

NP_990698.1; -.

3D structure databases

HSSP

P27038; 1BTE. [HSSP ENTRY / PDB]

SMR

Q90669; 26-119.

ModBase

Q90669.

Family and domain databases

InterPro

IPR000333; Activin_II_recpt.
IPR015768; Activin_II_recpt_C.
IPR000472; Activin_rcpt.
IPR000719; Prot_kinase_core.
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

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

BLOCKS

Q90669.

Genome annotation databases

Ensembl

ENSGALG00000012444; Gallus gallus. [Contig view]

GeneID

396324; -.

KEGG

gga:396324; -.

Phylogenomic databases

HOVERGEN

Q90669; -.

Other

ProtoNet

Q90669.

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_0000269545`
`TOPO_DOM`	`20 139`	`120`	`Extracellular (Potential).`
`TRANSMEM`	`140 160`	`21`	`Potential.`
`TOPO_DOM`	`161 513`	`353`	`Cytoplasmic (Potential).`
`DOMAIN`	`192 485`	`294`	`Protein kinase.`
`NP_BIND`	`198 206`	`9`	`ATP (By similarity).`
`COMPBIAS`	`178 185`	`8`	`Poly-Pro.`
`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).`
`CONFLICT`	`9 9`		`F -> L (in Ref. 1; BAA06697).`
`CONFLICT`	`43 45`		`NRS -> IAV (in Ref. 1; BAA06697).`
`CONFLICT`	`115 115`		`F -> S (in Ref. 1; BAA06697).`

Sequence information

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

Molecular weight: 58092 Da [This is the MW of the unprocessed precursor]

CRC64: 03128AB7FF732552 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGAATKLAFA VFLISCSSGA ILGRSETQEC IYYNANWEKD KTNRSGIEPC YGDKDKRRHC 

        70         80         90        100        110        120 
FATWKNISGS IEIVKQGCWL DDINCYDRND CIEKKDSPEV FFCCCEGNMC NERFFYFPEM 

       130        140        150        160        170        180 
EVTQPTSNPV TPKPPLFNTL LYSLVPIMGI AVIVLFSFWM YRHHKLAYPP VLVPTQDPGP 

       190        200        210        220        230        240 
PPPSPLMGLK PLQLLEIKAR GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEIYSLPG 

       250        260        270        280        290        300 
MKHDNILQFI GAEKRGTSID VDLWLITAFH EKGSLTDFLK ANVVSWNELC HIAQTMARGL 

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

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

       430        440        450        460        470        480 
QHPSLEDMQE VVVHKKKRPV LRECWQKHSG MAMLCETIEE CWDHDAEARL SAGCVEERII 

       490        500        510 
QMQKLTNIIT TEDIVTVVTM VTNVDFPPKE SSL

Q90669 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