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P80202 (ACV1B_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. 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-1B

EC=2.7.11.30
Alternative name(s):
Activin receptor type IB
Short name=ACTR-IB
Activin receptor-like kinase 4
Short name=ALK-4
Serine/threonine-protein kinase receptor R2
Short name=SKR2
Gene names
Name:Acvr1b
Synonyms:Acvrlk4, Alk4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length505 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-1 receptor forming an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Transduces the activin signal from the cell surface to the cytoplasm and is thus regulating a 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, type-2 receptors (ACVR2A and/or ACVR2B) act as a primary activin receptors whereas 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 such as ACVR1B. 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. ACVR1B also phosphorylates TDP2 By similarity.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Enzyme regulation

Activin receptor type-2 (ACVR2A or ACVR2B) activates the type-1 receptor through phosphorylation of its regulatory GS domain By similarity.

Subunit structure

Forms an activin receptor complex with activin receptor type-2 (ACVR2A or ACVR2B). Interacts with TDP2 By similarity. Interacts with AIP1, FKBP1A, IGSF1, TDGF1, SMAD2, SMAD3 and SMAD7 By similarity.

Subcellular location

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

Tissue specificity

Urogenital ridge, testis, ovary, brain and lungs.

Domain

The GS domain is a 30-amino-acid sequence adjacent to the N-terminal boundary of the kinase domain and highly conserved in all other known type-1 receptors but not in type-2 receptors. The GS domain is the site of activation through phosphorylation by the II receptors By similarity.

Post-translational modification

Autophosphorylated. Phosphorylated by activin receptor type-2 (ACVR2A or ACVR2B) in response to activin-binding at serine and threonine residues in the GS domain. Phosphorylation of ACVR1B by activin receptor type-2 regulates association with SMAD7 By similarity.

Ubiquitinated. Level of ubiquitination is regulated by the SMAD7-SMURF1 complex By similarity.

Ubiquitinated By similarity.

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 GS domain.

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
   PTMGlycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from expression pattern PubMed 8854897. Source: RGD

development of primary female sexual characteristics

Inferred from expression pattern PubMed 11897700. Source: RGD

extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

hair follicle development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

nodal signaling pathway

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of activin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from mutant phenotype PubMed 17040568. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 17040568. Source: RGD

positive regulation of trophoblast cell migration

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from mutant phenotype PubMed 12844345. Source: RGD

signal transduction by phosphorylation

Inferred from mutant phenotype PubMed 12844345. Source: GOC

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

SMAD binding

Inferred from mutant phenotype PubMed 12844345. Source: RGD

activin receptor activity, type I

Inferred from mutant phenotype PubMed 12844345. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from mutant phenotype PubMed 12844345. Source: RGD

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 – 2323 Potential
Chain24 – 505482Activin receptor type-1B
PRO_0000024419

Regions

Topological domain24 – 126103Extracellular Potential
Transmembrane127 – 14923Helical; Potential
Topological domain150 – 505356Cytoplasmic Potential
Domain177 – 20630GS
Domain207 – 497291Protein kinase
Nucleotide binding213 – 2219ATP By similarity

Sites

Active site3351Proton acceptor By similarity
Binding site2341ATP By similarity

Amino acid modifications

Modified residue3801Phosphotyrosine By similarity
Glycosylation431N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P80202 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 377F4A5C867B3860

FASTA50556,805
        10         20         30         40         50         60 
MAESAGASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QTNYTCETDG ACMVSIFNLD 

        70         80         90        100        110        120 
GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYIDF CNKIDLRVPS GHLKEPEHPS 

       130        140        150        160        170        180 
MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ 

       190        200        210        220        230        240 
DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE 

       250        260        270        280        290        300 
ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 

       310        320        330        340        350        360 
IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH 

       370        380        390        400        410        420 
DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG 

       430        440        450        460        470        480 
GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNVPNWW QSYEALRVMG KMMRECWYAN 

       490        500 
GAARLTALRI KKTLSQLSVQ EDVKI 

« Hide

References

[1]"Developmental expression of four novel serine/threonine kinase receptors homologous to the activin/transforming growth factor-beta type II receptor family."
He W.-W., Gustafson M.L., Hirobe S., Donahoe P.K.
Dev. Dyn. 196:133-142(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Urogenital ridge.
[2]"Molecular characterization of a type I serine-threonine kinase receptor for TGF-beta and activin in the rat pituitary tumor cell line GH3."
Takumi T., Moustakas A., Lin H.Y., Lodish H.F.
Exp. Cell Res. 216:208-214(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S76466 mRNA. Translation: AAB33045.1.
RefSeqNP_954700.1. NM_199230.1.
UniGeneRn.214018.

3D structure databases

ProteinModelPortalP80202.
SMRP80202. Positions 173-501.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248033. 1 interaction.
STRING10116.ENSRNOP00000009345.

PTM databases

PhosphoSiteP80202.

Proteomic databases

PaxDbP80202.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000009345; ENSRNOP00000009345; ENSRNOG00000006934.
GeneID29381.
KEGGrno:29381.
UCSCRGD:735207. rat.

Organism-specific databases

CTD91.
RGD735207. Acvr1b.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00730000110337.
HOGENOMHOG000230587.
HOVERGENHBG054502.
InParanoidP80202.
KOK13567.
OMAQCACTSC.
OrthoDBEOG7Q8CN3.
PhylomeDBP80202.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.

Gene expression databases

GenevestigatorP80202.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR003605. TGF_beta_rcpt_GS.
IPR000333. TGFB_receptor.
[Graphical view]
PANTHERPTHR23255. PTHR23255. 1 hit.
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
SMARTSM00467. GS. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio608961.
PROP80202.

Entry information

Entry nameACV1B_RAT
AccessionPrimary (citable) accession number: P80202
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 134 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