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Reviewed, UniProtKB/Swiss-Prot P38445 (AVR2B_RAT)

Last modified July 22, 2008. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Activin receptor type-2B
    EC=2.7.11.30
Alternative name(s):
    Activin receptor type IIB
      Short name(s)=ACTR-IIB
Gene names
Name: Acvr2b
Synonyms: Actriib
OrganismRattus norvegicus (Rat)
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

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 By similarity.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

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
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMGlycoprotein
   Technical term3D-structure

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 513495Activin receptor type-2B

Regions

Topological domain19 – 137119Extracellular Potential
Transmembrane138 – 15821 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 in AAH97358. Ref.2 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

Sequences

Sequence LengthMass (Da)Tools
P38445-1 [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: 1312838] [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: 7916681] [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: 15489334] [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: 12660162] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 19-119 IN COMPLEX WITH HUMAN INHBA.

Cross-references

Sequence databases

L10640 mRNA. Translation: AAA40772.1.
BC097358 mRNA. Translation: AAH97358.1.
PIRB49193.
JQ1484.
RefSeqNP_113742.1.
UniGeneRn.24240

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NYSX-ray3.05A/C19-119[»]
1NYUX-ray3.10A/C19-119[»]
SMRP38445. Positions 24-117.
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000014477. Rattus norvegicus. [Contig view]
GeneID25366.
KEGGrno:25366.

Organism-specific databases

RGD2028. Acvr2b.
GeneLynxSearch...

Phylogenomic databases

HOVERGENP38445.

Gene expression databases

ArrayExpressP38445.
GermOnlineENSRNOG00000014477. Rattus norvegicus.

Family and domain databases

InterProIPR000333. 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]
PANTHERPTHR23255:SF10. Activin_II_recpt_C. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PRINTSPR00653. ACTIVIN2R.
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00107. PROTEIN_KINASE_ATP. False negative.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
BLOCKSSearch...

Other Resources

ProtoNetSearch...

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: July 22, 2008
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

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