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Q95126 (AVR2B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 512494Activin receptor type-2B
PRO_0000024403

Regions

Topological domain19 – 137119Extracellular Potential
Transmembrane138 – 15821Helical; Potential
Topological domain159 – 512354Cytoplasmic Potential
Domain190 – 480291Protein kinase
Nucleotide binding196 – 2049ATP By similarity

Sites

Active site3211Proton 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

Sequences

Sequence LengthMass (Da)Tools
Q95126 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: D8E14D465B3EEF04

FASTA51257,569
        10         20         30         40         50         60 
MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GERDKRLHCY 

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

       130        140        150        160        170        180 
GPEVTYEPPP TAPTLLTVLA YSLLPVGGLS LIALLAFWMY RHRKPPYGHA DIHEDPGPPP 

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

       250        260        270        280        290        300 
HENLLQFIAA EKRGSSLEAE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY 

       310        320        330        340        350        360 
LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG 

       370        380        390        400        410        420 
TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ 

       430        440        450        460        470        480 
HPSLEELQEV VVHKKMRPAI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL 

       490        500        510 
IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI 

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References

[1]"Bovine activin receptor type IIB messenger ribonucleic acid displays alternative splicing involving a sequence homologous to Src-homology 3 domain binding sites."
Ethier J.-F., Lussier J.G., Silversides D.W.
Endocrinology 138:2425-2434(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Corpus luteum and Pituitary.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U57707 mRNA. Translation: AAC02647.1.
RefSeqNP_776920.1. NM_174495.2.
UniGeneBt.4990.

3D structure databases

ProteinModelPortalQ95126.
SMRQ95126. Positions 24-117, 190-484.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ95126.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID282131.
KEGGbta:282131.

Organism-specific databases

CTD93.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000231495.
HOVERGENHBG054502.
InParanoidQ95126.
KOK13596.

Enzyme and pathway databases

BRENDA2.7.10.2. 908.

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

NextBio20805966.

Entry information

Entry nameAVR2B_BOVIN
AccessionPrimary (citable) accession number: Q95126
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 112 of the entry and version 1 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