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P27038 (AVR2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:Acvr2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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. Ref.4

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Brain, testis, intestine, liver and kidney.

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_processBMP signaling pathway

Inferred from mutant phenotype PubMed 17472960. Source: MGI

Sertoli cell proliferation

Inferred from mutant phenotype PubMed 11416011. Source: MGI

anterior/posterior pattern specification

Inferred from genetic interaction PubMed 10452853PubMed 16991118. Source: MGI

determination of left/right symmetry

Inferred from genetic interaction PubMed 16991118. Source: MGI

embryonic skeletal system development

Inferred from mutant phenotype PubMed 7885474. Source: MGI

gastrulation with mouth forming second

Inferred from genetic interaction PubMed 10452853. Source: MGI

male gonad development

Inferred from mutant phenotype PubMed 7885474. Source: MGI

mesoderm development

Inferred from mutant phenotype PubMed 10452853. Source: MGI

penile erection

Inferred from mutant phenotype PubMed 16093358. Source: MGI

positive regulation of activin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

positive regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from sequence orthology PubMed 17472960. Source: MGI

regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 17472960. Source: MGI

regulation of nitric-oxide synthase activity

Inferred from mutant phenotype PubMed 16093358. Source: MGI

regulation of signal transduction

Inferred from direct assay PubMed 17936261. Source: MGI

sperm ejaculation

Inferred from mutant phenotype PubMed 16093358. Source: MGI

spermatogenesis

Inferred from genetic interaction PubMed 11459797. Source: MGI

   Cellular_componentcell surface

Inferred from direct assay PubMed 16648306. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: Ensembl

inhibin-betaglycan-ActRII complex

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

PDZ domain binding

Inferred from physical interaction PubMed 16648306. Source: UniProtKB

activin binding

Inferred from physical interaction Ref.1. Source: MGI

activin-activated receptor activity

Inferred from electronic annotation. Source: Ensembl

coreceptor activity

Inferred from electronic annotation. Source: Ensembl

growth factor binding

Inferred from mutant phenotype PubMed 12414726. Source: MGI

inhibin binding

Inferred from physical interaction PubMed 7890768. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 16648306. Source: UniProtKB

protein self-association

Inferred from physical interaction PubMed 8612709. Source: MGI

protein serine/threonine kinase activity

Traceable author statement. Source: Reactome

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 513494Activin receptor type-2A
PRO_0000024399

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...)
Glycosylation661N-linked (GlcNAc...)
Disulfide bond30 ↔ 60 Ref.3
Disulfide bond50 ↔ 78 Ref.3
Disulfide bond85 ↔ 104 Ref.3
Disulfide bond91 ↔ 103 Ref.3
Disulfide bond105 ↔ 110 Ref.3

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P27038 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 475CD292506BAC61

FASTA51357,890
        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 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 

« Hide

References

[1]"Expression cloning of an activin receptor, a predicted transmembrane serine kinase."
Mathews L.S., Vale W.W.
Cell 65:973-982(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Three-finger toxin fold for the extracellular ligand-binding domain of the type II activin receptor serine kinase."
Greenwald J., Fischer W.H., Vale W.W., Choe S.
Nat. Struct. Biol. 6:18-22(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 25-121.
[3]"The disulfide bond arrangement in the extracellular domain of the activin type II receptor."
Fischer W.H., Greenwald J., Park M., Craig A.G., Choe S., Vale W.
J. Protein Chem. 18:437-446(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS IN EXTRACELLULAR DOMAIN.
[4]"Identification and characterization of a PDZ protein that interacts with activin types II receptors."
Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z., Nakamura T., Sugino H.
J. Biol. Chem. 275:5485-5492(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AIP1, IDENTIFICATION IN A COMPLEX WITH ACVR1B; AIP1 AND SMAD3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65287 mRNA. Translation: AAA37171.1.
CCDSCCDS16021.1.
PIRA39896.
RefSeqNP_031422.3. NM_007396.4.
UniGeneMm.314338.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BTEX-ray1.50A/B25-121[»]
1LX5X-ray3.30B20-121[»]
2GOOX-ray2.20C/F20-121[»]
ProteinModelPortalP27038.
SMRP27038. Positions 26-119, 191-486.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197955. 2 interactions.
DIPDIP-5825N.
IntActP27038. 1 interaction.

PTM databases

PhosphoSiteP27038.

Proteomic databases

PaxDbP27038.
PRIDEP27038.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063886; ENSMUSP00000067305; ENSMUSG00000052155.
GeneID11480.
KEGGmmu:11480.
UCSCuc008jpn.2. mouse.

Organism-specific databases

CTD92.
MGIMGI:102806. Acvr2a.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000076906.
HOGENOMHOG000231495.
HOVERGENHBG054502.
InParanoidP27038.
KOK04670.
OMAEDPGNWI.
OrthoDBEOG7JHM5B.
PhylomeDBP27038.
TreeFamTF352876.

Enzyme and pathway databases

BRENDA2.7.10.2. 3474.
ReactomeREACT_188257. Signal Transduction.
REACT_188576. Developmental Biology.

Gene expression databases

ArrayExpressP27038.
BgeeP27038.
CleanExMM_ACVR2A.
GenevestigatorP27038.

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

ChiTaRSACVR2A. mouse.
EvolutionaryTraceP27038.
NextBio278828.
PROP27038.
SOURCESearch...

Entry information

Entry nameAVR2A_MOUSE
AccessionPrimary (citable) accession number: P27038
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 147 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

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot