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

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Reviewed, UniProtKB/Swiss-Prot P27038 (AVR2A_MOUSE)

Last modified July 22, 2008. Version 90. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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(s)=ACTR-IIA

Gene names

Name:	Acvr2a
Synonyms:	Acvr2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

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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.

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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.
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.

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Ontologies

Keywords
Cellular component	Membrane
Domain	Signal Transmembrane
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Glycoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	Sertoli cell proliferation Inferred from mutant phenotype. Source: MGI anterior/posterior pattern formation Inferred from genetic interaction. Source: MGI determination of left/right symmetry Inferred from genetic interaction. Source: MGI embryonic skeletal development Inferred from mutant phenotype. Source: MGI gastrulation with mouth forming second Inferred from genetic interaction. Source: MGI mesoderm development Inferred from mutant phenotype. Source: MGI penile erection Inferred from mutant phenotype. Source: MGI regulation of BMP signaling pathway Inferred from mutant phenotype. Source: MGI regulation of nitric-oxide synthase activity Inferred from mutant phenotype. Source: MGI sperm ejaculation Inferred from mutant phenotype. Source: MGI spermatogenesis Inferred from genetic interaction. Source: MGI
Molecular function	growth factor binding Inferred from mutant phenotype. Source: MGI inhibin beta-A binding Inferred from direct assay. Source: HGNC protein self-association Inferred from physical interaction. Source: MGI
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BMP7	P18075	1	EBI-1036102,EBI-1035195	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Signal peptide

1 – 19

Potential

Chain

20 – 513

494

Activin receptor type-2A

Regions

Topological domain

20 – 135

116

Extracellular Potential

Transmembrane

136 – 161

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...

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Sequences

Sequence

Length

Mass (Da)

Tools

P27038-1 [UniParc].

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

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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: 1646080] [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: 9886286] [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: 10449041] [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: 10681527] [Abstract] Cited for: INTERACTION WITH AIP1, IDENTIFICATION IN A COMPLEX WITH ACVR1B; AIP1 AND SMAD3.

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Cross-references

Sequence databases

M65287 mRNA. Translation: AAA37171.1.

PIR

A39896.

RefSeq

NP_031422.3.

UniGene

Mm.314338

3D structure databases

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5825N.

IntAct

P27038.

PTM databases

PhosphoSite

P27038.

Genome annotation databases

Ensembl

ENSMUSG00000052155. Mus musculus. [Contig view]

GeneID

11480.

KEGG

mmu:11480.

Organism-specific databases

MGI

MGI:102806. Acvr2a.

Phylogenomic databases

HOGENOM

P27038.

HOVERGEN

P27038.

Gene expression databases

ArrayExpress

P27038.

CleanEx

MM_ACVR2A.

GermOnline

ENSMUSG00000052155. Mus musculus.

Family and domain databases

InterPro

IPR000333. Activin_II_recpt.
IPR015768. Activin_II_recpt_C.
IPR000472. Activin_rcpt.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
[Graphical view]

PANTHER

PTHR23255:SF10. Activin_II_recpt_C. 1 hit.

Pfam

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

PRINTS

PR00653. ACTIVIN2R.

ProDom

PD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

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

BLOCKS

Search...

Other Resources

LinkHub

P27038.

SOURCE

Search...

ProtoNet

Search...

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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:	July 22, 2008
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents