Activin receptor type-2B precursor

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Q95126 (AVR2B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 105. History...

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

Documents (1) |

Third-party data

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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-2B
EC=2.7.11.30

Alternative name(s):
Activin receptor type IIB
Short name=ACTR-IIB

Gene names

Name:

ACVR2B

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane 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 Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW activin-activated receptor activity Inferred from electronic annotation. Source: InterPro 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 – 18

Potential

Chain

19 – 512

494

Activin receptor type-2B

PRO_0000024403

Regions

Topological domain

19 – 137

119

Extracellular Potential

Transmembrane

138 – 158

Helical; Potential

Topological domain

159 – 512

354

Cytoplasmic Potential

Domain

190 – 480

291

Protein kinase

Nucleotide binding

196 – 204

ATP By similarity

Sites

Active site

321

Proton acceptor By similarity

Binding site

217

ATP By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 59

By similarity

Disulfide bond

49 ↔ 77

By similarity

Disulfide bond

84 ↔ 103

By similarity

Disulfide bond

90 ↔ 102

By similarity

Disulfide bond

104 ↔ 109

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q95126 [UniParc].

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

512

57,569

        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.
IPI	IPI00706908.
RefSeq	NP_776920.1. NM_174495.2.
UniGene	Bt.4990.
3D structure databases
ProteinModelPortal	Q95126.
SMR	Q95126. Positions 24-117, 190-484.
ModBase	Search...
Proteomic databases
PRIDE	Q95126.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	282131.
KEGG	bta:282131.
Organism-specific databases
CTD	93.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000231495.
HOVERGEN	HBG054502.
InParanoid	Q95126.
KO	K13596.
OrthoDB	EOG4XPQFN.
Enzyme and pathway databases
BRENDA	2.7.10.2. 908.
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
NextBio	20805966.

Entry information

Entry name

AVR2B_BOVIN

Accession

Primary (citable) accession number: Q95126

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 105 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

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents