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Protein

Activin receptor type-2A

Gene

Acvr2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Mediates induction of adipogenesis by GDF6 (PubMed:23527555).1 Publication

Catalytic activityi

ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei219ATPPROSITE-ProRule annotation1
Active sitei322Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi198 – 206ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • activin binding Source: MGI
  • activin receptor activity, type II Source: MGI
  • ATP binding Source: UniProtKB-KW
  • BMP receptor activity Source: UniProtKB
  • coreceptor activity Source: MGI
  • growth factor binding Source: MGI
  • inhibin binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • PDZ domain binding Source: UniProtKB
  • protein self-association Source: MGI
  • protein serine/threonine kinase activity Source: MGI

GO - Biological processi

  • activin receptor signaling pathway Source: MGI
  • anterior/posterior pattern specification Source: MGI
  • BMP signaling pathway Source: UniProtKB
  • cellular response to BMP stimulus Source: MGI
  • determination of left/right symmetry Source: MGI
  • embryonic skeletal system development Source: MGI
  • gastrulation with mouth forming second Source: MGI
  • male gonad development Source: MGI
  • mesoderm development Source: MGI
  • penile erection Source: MGI
  • positive regulation of activin receptor signaling pathway Source: MGI
  • positive regulation of bone mineralization Source: MGI
  • positive regulation of erythrocyte differentiation Source: MGI
  • positive regulation of follicle-stimulating hormone secretion Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • positive regulation of transcription by RNA polymerase II Source: MGI
  • regulation of BMP signaling pathway Source: MGI
  • regulation of nitric-oxide synthase activity Source: MGI
  • regulation of signal transduction Source: MGI
  • Sertoli cell proliferation Source: MGI
  • spermatogenesis Source: MGI
  • sperm ejaculation Source: MGI

Keywordsi

Molecular functionKinase, Receptor, Serine/threonine-protein kinase, Transferase
LigandATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2 3474
ReactomeiR-MMU-1502540 Signaling by Activin
R-MMU-201451 Signaling by BMP

Names & Taxonomyi

Protein namesi
Recommended name:
Activin receptor type-2A (EC:2.7.11.30)
Alternative name(s):
Activin receptor type IIA
Short name:
ACTR-IIA
Gene namesi
Name:Acvr2a
Synonyms:Acvr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:102806 Acvr2a

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini20 – 135ExtracellularSequence analysisAdd BLAST116
Transmembranei136 – 161HelicalSequence analysisAdd BLAST26
Topological domaini162 – 513CytoplasmicSequence analysisAdd BLAST352

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000002439920 – 513Activin receptor type-2AAdd BLAST494

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi30 ↔ 601 Publication
Glycosylationi43N-linked (GlcNAc...) asparagine1
Disulfide bondi50 ↔ 781 Publication
Glycosylationi66N-linked (GlcNAc...) asparagine1
Disulfide bondi85 ↔ 1041 Publication
Disulfide bondi91 ↔ 1031 Publication
Disulfide bondi105 ↔ 1101 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP27038
PaxDbiP27038
PRIDEiP27038

PTM databases

iPTMnetiP27038
PhosphoSitePlusiP27038

Expressioni

Tissue specificityi

Brain, testis, intestine, liver and kidney.

Gene expression databases

BgeeiENSMUSG00000052155
CleanExiMM_ACVR2A
ExpressionAtlasiP27038 baseline and differential
GenevisibleiP27038 MM

Interactioni

Subunit structurei

Interacts with AIP1. Part of a complex consisting of AIP1, ACVR2A, ACVR1B and SMAD3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BMP2P126432EBI-1036102,EBI-1029262From Homo sapiens.

GO - Molecular functioni

  • growth factor binding Source: MGI
  • inhibin binding Source: BHF-UCL
  • PDZ domain binding Source: UniProtKB
  • protein self-association Source: MGI

Protein-protein interaction databases

BioGridi197955, 2 interactors
CORUMiP27038
DIPiDIP-5825N
IntActiP27038, 3 interactors
STRINGi10090.ENSMUSP00000067305

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 34Combined sources6
Helixi37 – 40Combined sources4
Beta strandi44 – 49Combined sources6
Beta strandi59 – 67Combined sources9
Beta strandi70 – 79Combined sources10
Helixi83 – 85Combined sources3
Beta strandi88 – 93Combined sources6
Beta strandi95 – 97Combined sources3
Beta strandi99 – 105Combined sources7
Helixi110 – 112Combined sources3
Beta strandi113 – 116Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BTEX-ray1.50A/B25-121[»]
1LX5X-ray3.30B20-121[»]
2GOOX-ray2.20C/F20-121[»]
ProteinModelPortaliP27038
SMRiP27038
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27038

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini192 – 485Protein kinasePROSITE-ProRule annotationAdd BLAST294

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3653 Eukaryota
ENOG410XS2Z LUCA
GeneTreeiENSGT00760000118876
HOGENOMiHOG000231495
HOVERGENiHBG054502
InParanoidiP27038
KOiK13596
OMAiRIIQMQR
OrthoDBiEOG091G03YO
PhylomeDBiP27038
TreeFamiTF352876

Family and domain databases

InterProiView protein in InterPro
IPR000472 Activin_recp
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS
IPR000333 TGFB_receptor
PANTHERiPTHR23255 PTHR23255, 1 hit
PfamiView protein in Pfam
PF01064 Activin_recp, 1 hit
PF00069 Pkinase, 1 hit
PRINTSiPR00653 ACTIVIN2R
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27038-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAAAKLAFA VFLISCSSGA ILGRSETQEC LFFNANWERD RTNQTGVEPC
60 70 80 90 100
YGDKDKRRHC FATWKNISGS IEIVKQGCWL DDINCYDRTD CIEKKDSPEV
110 120 130 140 150
YFCCCEGNMC NEKFSYFPEM EVTQPTSNPV TPKPPYYNIL LYSLVPLMLI
160 170 180 190 200
AGIVICAFWV YRHHKMAYPP VLVPTQDPGP PPPSPLLGLK PLQLLEVKAR
210 220 230 240 250
GRFGCVWKAQ LLNEYVAVKI FPIQDKQSWQ NEYEVYSLPG MKHENILQFI
260 270 280 290 300
GAEKRGTSVD VDLWLITAFH EKGSLSDFLK ANVVSWNELC HIAETMARGL
310 320 330 340 350
AYLHEDIPGL KDGHKPAISH RDIKSKNVLL KNNLTACIAD FGLALKFEAG
360 370 380 390 400
KSAGDTHGQV GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELASR
410 420 430 440 450
CTAADGPVDE YMLPFEEEIG QHPSLEDMQE VVVHKKKRPV LRDYWQKHAG
460 470 480 490 500
MAMLCETIEE CWDHDAEARL SAGCVGERIT QMQRLTNIIT TEDIVTVVTM
510
VTNVDFPPKE SSL
Length:513
Mass (Da):57,890
Last modified:August 1, 1992 - v1
Checksum:i475CD292506BAC61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65287 mRNA Translation: AAA37171.1
CCDSiCCDS16021.1
PIRiA39896
RefSeqiNP_031422.3, NM_007396.4
UniGeneiMm.314338

Genome annotation databases

EnsembliENSMUST00000063886; ENSMUSP00000067305; ENSMUSG00000052155
GeneIDi11480
KEGGimmu:11480
UCSCiuc008jpn.2 mouse

Similar proteinsi

Entry informationi

Entry nameiAVR2A_MOUSE
AccessioniPrimary (citable) accession number: P27038
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 20, 2018
This is version 179 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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