Activin receptor type-2A precursor - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (?) or add your own

P27038 (AVR2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 133. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	513 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	BMP 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 10452853 PubMed 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 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: Compara positive regulation of bone mineralization Inferred from electronic annotation. Source: Compara positive regulation of erythrocyte differentiation Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of pathway-restricted SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara 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 signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC sperm ejaculation Inferred from mutant phenotype PubMed 16093358. Source: MGI spermatogenesis Inferred from genetic interaction PubMed 11459797. Source: MGI
Cellular_component	cell surface Inferred from direct assay PubMed 16648306. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: Compara inhibin-betaglycan-ActRII complex Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW activin-activated receptor activity Inferred from electronic annotation. Source: Compara coreceptor activity Inferred from electronic annotation. Source: Compara growth factor binding Inferred from mutant phenotype PubMed 12414726. Source: MGI 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Potential

Chain

20 – 513

494

Activin receptor type-2A

PRO_0000024399

Regions

Topological domain

20 – 135

116

Extracellular Potential

Transmembrane

136 – 161

Helical; Potential

Topological domain

162 – 513

352

Cytoplasmic Potential

Domain

192 – 485

294

Protein kinase

Nucleotide binding

198 – 206

ATP By similarity

Sites

Active site

322

Proton acceptor By similarity

Binding site

219

ATP By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...)

Glycosylation

N-linked (GlcNAc...)

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

513

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P27038 [UniParc].

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

FASTA

513

57,890

        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.

IPI

IPI00319667.

PIR

A39896.

RefSeq

NP_031422.3. NM_007396.4.

UniGene

Mm.314338.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BTE	X-ray	1.50	A/B	25-121	[»]
1LX5	X-ray	3.30	B	20-121	[»]
2GOO	X-ray	2.20	C/F	20-121	[»]

ProteinModelPortal

P27038.

SMR

P27038. Positions 26-119, 191-486.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5825N.

IntAct

P27038. 1 interaction.

PTM databases

PhosphoSite

P27038.

Proteomic databases

PaxDb

P27038.

PRIDE

P27038.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000063886; ENSMUSP00000067305; ENSMUSG00000052155.

GeneID

11480.

KEGG

mmu:11480.

Organism-specific databases

CTD

92.

MGI

MGI:102806. Acvr2a.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00560000076906.

HOGENOM

HOG000231495.

HOVERGEN

HBG054502.

InParanoid

P27038.

K04670.

OMA

ERIIQMQ.

OrthoDB

EOG47WNNH.

Enzyme and pathway databases

BRENDA

2.7.10.2. 3474.

Reactome

REACT_115202. Signal Transduction.
REACT_127416. Developmental Biology.

Gene expression databases

ArrayExpress

P27038.

Bgee

P27038.

CleanEx

MM_ACVR2A.

Genevestigator

P27038.

GermOnline

ENSMUSG00000052155. Mus musculus.

Family and domain databases

InterPro

IPR000333. Activin_II/TGFBeta-II_recpt.
IPR015768. Activin_II_recpt.
IPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR23255:SF10. PTHR23255:SF10. 1 hit.

Pfam

PF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PRINTS

PR00653. ACTIVIN2R.

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ACVR2A. mouse.

EvolutionaryTrace

P27038.

NextBio

278828.

SOURCE

Search...

Entry information

Entry name

AVR2A_MOUSE

Accession

Primary (citable) accession number: P27038

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	April 3, 2013
This is version 133 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents