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P38444 (AVR2A_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Activin receptor type-2A

EC=2.7.11.30
Alternative name(s):
Activin receptor type IIA
Short name=ACTR-IIA
Gene names
Name:Acvr2a
Synonyms:Actrii, Acvr2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length513 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivin receptor signaling pathway

Inferred from direct assay PubMed 12844345. Source: GOC

positive regulation of follicle-stimulating hormone secretion

Inferred from mutant phenotype PubMed 11861519. Source: RGD

protein phosphorylation

Traceable author statement PubMed 12770730. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 12706302. Source: RGD

   Cellular_componentactivin receptor complex

Traceable author statement PubMed 12844345. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin binding

Inferred from direct assay PubMed 12385827. Source: RGD

activin receptor activity, type II

Inferred from direct assay PubMed 12844345. Source: RGD

inhibin binding

Inferred from direct assay PubMed 12385827. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta-activated receptor activity

Inferred from electronic annotation. Source: InterPro

transmembrane receptor protein serine/threonine kinase activity

Traceable author statement PubMed 12770730. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 513494Activin receptor type-2A
PRO_0000024401

Regions

Topological domain20 – 135116Extracellular Potential
Transmembrane136 – 16126Helical; Potential
Topological domain162 – 513352Cytoplasmic Potential
Domain192 – 485294Protein kinase
Nucleotide binding198 – 2069ATP By similarity

Sites

Active site3221Proton acceptor By similarity
Binding site2191ATP By similarity

Amino acid modifications

Glycosylation431N-linked (GlcNAc...) Potential
Glycosylation661N-linked (GlcNAc...) Potential
Disulfide bond30 ↔ 60 By similarity
Disulfide bond50 ↔ 78 By similarity
Disulfide bond85 ↔ 104 By similarity
Disulfide bond91 ↔ 103 By similarity
Disulfide bond105 ↔ 110 By similarity

Experimental info

Sequence conflict1651M → K in AAB23958. Ref.2
Sequence conflict2181V → I in AAB23958. Ref.2
Sequence conflict3531G → A in AAB23958. Ref.2
Sequence conflict4751L → V in AAB23958. Ref.2

Secondary structure

................. 513
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38444 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: CE3A8742EF91DD7D

FASTA51357,893
        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 

« Hide

References

[1]"Cloning and sequencing of a rat type II activin receptor."
Shinozaki H., Ito I., Hasegawa Y., Nakamura K., Igarashi S., Nakamura M., Miyamoto K., Eto Y., Ibuki Y., Minegishi T.
FEBS Lett. 312:53-56(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Ovary.
[2]"Expression of type II activin receptor genes in the male and female reproductive tissues of the rat."
Feng Z.M., Madigan M.B., Chen C.L.C.
Endocrinology 132:2593-2600(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S48190 mRNA. Translation: AAB23958.1.
L10639 mRNA. Translation: AAA40674.1.
PIRA49193.
S27258.
RefSeqNP_113759.1. NM_031571.2.
UniGeneRn.161783.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05A/C34-112[»]
1NYUX-ray3.10A/C34-112[»]
ProteinModelPortalP38444.
SMRP38444. Positions 26-119, 192-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-263218.
STRING10116.ENSRNOP00000007404.

Proteomic databases

PaxDbP38444.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29263.
KEGGrno:29263.
UCSCRGD:70911. rat.

Organism-specific databases

CTD92.
RGD70911. Acvr2a.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231495.
HOVERGENHBG054502.
InParanoidP38444.
KOK04670.
PhylomeDBP38444.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.

Gene expression databases

GenevestigatorP38444.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00653. ACTIVIN2R.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38444.
NextBio608592.
PROP38444.

Entry information

Entry nameAVR2A_RAT
AccessionPrimary (citable) accession number: P38444
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references