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P38445 (AVR2B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. 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-2B

EC=2.7.11.30
Alternative name(s):
Activin receptor type IIB
Short name=ACTR-IIB
Gene names
Name:Acvr2b
Synonyms:Actriib
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

Transmembrane serine/threonine kinase activin type-2 receptor forming an activin receptor complex with activin type-1 serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating many physiological and pathological processes including neuronal differentiation and neuronal survival, hair follicle development and cycling, FSH production by the pituitary gland, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. Activin is also thought to have a paracrine or autocrine role in follicular development in the ovary. Within the receptor complex, the type-2 receptors act as a primary activin receptors (binds activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA). The type-1 receptors like ACVR1B act as downstream transducers of activin signals. Activin binds to type-2 receptor at the plasma membrane and activates its serine-threonine kinase. The activated receptor type-2 then phosphorylates and activates the type-1 receptor. Once activated, the type-1 receptor binds and phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine residues of the C-terminal tail. Soon after their association with the activin receptor and subsequent phosphorylation, SMAD2 and SMAD3 are released into the cytoplasm where they interact with the common partner SMAD4. This SMAD complex translocates into the nucleus where it mediates activin-induced transcription. Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can prevent the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. Activin signal transduction is also antagonized by the binding to the receptor of inhibin-B via the IGSF1 inhibin coreceptor By similarity.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Forms an activin receptor complex with activin type II receptors such as ACVR1B By similarity. Interacts with VPS39 By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity By similarity.

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 componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Inferred from electronic annotation. Source: Ensembl

activation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

artery development

Inferred from electronic annotation. Source: Ensembl

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

determination of left/right symmetry

Inferred from electronic annotation. Source: Ensembl

embryonic foregut morphogenesis

Inferred from electronic annotation. Source: Ensembl

gastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

insulin secretion

Inferred from electronic annotation. Source: Ensembl

kidney development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

lymphangiogenesis

Inferred from electronic annotation. Source: Ensembl

lymphatic endothelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

mesoderm development

Inferred from electronic annotation. Source: Ensembl

odontogenesis of dentin-containing tooth

Inferred from electronic annotation. Source: Ensembl

organ growth

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

pancreas development

Inferred from electronic annotation. Source: Ensembl

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 osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement PubMed 12770730. Source: RGD

response to glucose

Inferred from electronic annotation. Source: Ensembl

retina vasculature development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

sexual reproduction

Non-traceable author statement Ref.2. Source: RGD

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

venous blood vessel development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

activin binding

Inferred from direct assay PubMed 12385827. Source: RGD

inhibin binding

Inferred from direct assay PubMed 12385827. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine/tyrosine kinase activity

Inferred from electronic annotation. Source: Ensembl

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 – 1818 Potential
Chain19 – 513495Activin receptor type-2B
PRO_0000024406

Regions

Topological domain19 – 137119Extracellular Potential
Transmembrane138 – 15821Helical; Potential
Topological domain159 – 513355Cytoplasmic Potential
Domain190 – 481292Protein kinase
Nucleotide binding196 – 2049ATP By similarity

Sites

Active site3221Proton acceptor By similarity
Binding site2171ATP By similarity

Amino acid modifications

Glycosylation421N-linked (GlcNAc...) Potential
Glycosylation651N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 59 By similarity
Disulfide bond49 ↔ 77 By similarity
Disulfide bond84 ↔ 103 By similarity
Disulfide bond90 ↔ 102 By similarity
Disulfide bond104 ↔ 109 By similarity

Experimental info

Sequence conflict641R → P in AAA40772. Ref.1
Sequence conflict641R → P Ref.2
Sequence conflict2551Missing Ref.2
Sequence conflict2551Missing in AAH97358. Ref.3
Sequence conflict4881S → G in AAA40772. Ref.1
Sequence conflict4881S → G Ref.2
Sequence conflict5011V → S in AAA40772. Ref.1
Sequence conflict5011V → S Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P38445 [UniParc].

Last modified November 13, 2007. Version 3.
Checksum: 765DB33F11C64CA7

FASTA51357,857
        10         20         30         40         50         60 
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY 

        70         80         90        100        110        120 
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEPG 

       130        140        150        160        170        180 
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP 

       190        200        210        220        230        240 
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK 

       250        260        270        280        290        300 
HENLLQFIAA EKRGCSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS 

       310        320        330        340        350        360 
YLHEDVPWCR GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG KPPGDTHGQV 

       370        380        390        400        410        420 
GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELVSR CKAADGPVDE YMLPFEEEIG 

       430        440        450        460        470        480 
QHPSLEELQE VVVHKKMRPT IKDHWLKHPG LAQLCVTIEE CWDHDAEARL SAGCVEERVS 

       490        500        510 
LIRRSVNSST SDCLVSLVTS VTNVDLLPKE SSI 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a novel rat activin receptor."
Legerski R., Zhou X., Dresback J., Eberspaecher H., McKinney S., Segarini P., de Crombrugghe B.
Biochem. Biophys. Res. Commun. 183:672-679(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[4]"Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions."
Thompson T.B., Woodruff T.K., Jardetzky T.S.
EMBO J. 22:1555-1566(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 19-119 IN COMPLEX WITH HUMAN INHBA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10640 mRNA. Translation: AAA40772.1.
BC097358 mRNA. Translation: AAH97358.1.
PIRB49193.
JQ1484.
RefSeqNP_113742.1. NM_031554.1.
UniGeneRn.24240.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05A/C19-119[»]
1NYUX-ray3.10A/C19-119[»]
ProteinModelPortalP38445.
SMRP38445. Positions 26-120, 190-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000049841.

Proteomic databases

PaxDbP38445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019777; ENSRNOP00000019777; ENSRNOG00000014477.
GeneID25366.
KEGGrno:25366.
UCSCRGD:2028. rat.

Organism-specific databases

CTD93.
RGD2028. Acvr2b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000076906.
HOGENOMHOG000231495.
HOVERGENHBG054502.
KOK13596.
OrthoDBEOG7JHM5B.

Gene expression databases

GenevestigatorP38445.

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:SF10. PTHR23255:SF10. 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

EvolutionaryTraceP38445.
NextBio606365.
PROP38445.

Entry information

Entry nameAVR2B_RAT
AccessionPrimary (citable) accession number: P38445
Secondary accession number(s): Q4V8J8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 13, 2007
Last modified: April 16, 2014
This is version 127 of the entry and version 3 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