Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P80202

- ACV1B_RAT

UniProt

P80202 - ACV1B_RAT

Protein

Activin receptor type-1B

Gene

Acvr1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.By similarity

    Enzyme regulationi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei234 – 2341ATPPROSITE-ProRule annotation
    Active sitei335 – 3351Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi213 – 2219ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. activin receptor activity, type I Source: RGD
    2. ATP binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. receptor signaling protein serine/threonine kinase activity Source: RGD
    5. SMAD binding Source: RGD
    6. transforming growth factor beta-activated receptor activity Source: InterPro
    7. transmembrane receptor protein serine/threonine kinase activity Source: RGD

    GO - Biological processi

    1. central nervous system development Source: RGD
    2. development of primary female sexual characteristics Source: RGD
    3. extrinsic apoptotic signaling pathway Source: Ensembl
    4. G1/S transition of mitotic cell cycle Source: Ensembl
    5. hair follicle development Source: Ensembl
    6. in utero embryonic development Source: Ensembl
    7. negative regulation of cell growth Source: Ensembl
    8. nodal signaling pathway Source: Ensembl
    9. peptidyl-threonine phosphorylation Source: Ensembl
    10. positive regulation of activin receptor signaling pathway Source: Ensembl
    11. positive regulation of erythrocyte differentiation Source: Ensembl
    12. positive regulation of pathway-restricted SMAD protein phosphorylation Source: RGD
    13. positive regulation of transcription from RNA polymerase II promoter Source: RGD
    14. positive regulation of trophoblast cell migration Source: Ensembl
    15. protein autophosphorylation Source: Ensembl
    16. protein phosphorylation Source: RGD
    17. signal transduction by phosphorylation Source: GOC

    Keywords - Molecular functioni

    Kinase, Receptor, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 5301.
    ReactomeiREACT_194628. Signaling by Activin.
    REACT_194664. Signaling by NODAL.
    REACT_199248. Regulation of signaling by NODAL.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Acvr1b
    Synonyms:Acvrlk4, Alk4
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 7

    Organism-specific databases

    RGDi735207. Acvr1b.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. integral component of plasma membrane Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 505482Activin receptor type-1BPRO_0000024419Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
    Modified residuei380 – 3801PhosphotyrosineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP80202.

    PTM databases

    PhosphoSiteiP80202.

    Expressioni

    Tissue specificityi

    Urogenital ridge, testis, ovary, brain and lungs.

    Gene expression databases

    GenevestigatoriP80202.

    Interactioni

    Subunit structurei

    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.By similarity

    Protein-protein interaction databases

    BioGridi248033. 1 interaction.
    STRINGi10116.ENSRNOP00000009345.

    Structurei

    3D structure databases

    ProteinModelPortaliP80202.
    SMRiP80202. Positions 173-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 126103ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini150 – 505356CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei127 – 14923HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini177 – 20630GSPROSITE-ProRule annotationAdd
    BLAST
    Domaini207 – 497291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Contains 1 GS domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110337.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiP80202.
    KOiK13567.
    OMAiQCACTSC.
    OrthoDBiEOG7Q8CN3.
    PhylomeDBiP80202.

    Family and domain databases

    InterProiIPR000472. 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]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view]
    SMARTiSM00467. GS. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P80202-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAESAGASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QTNYTCETDG    50
    ACMVSIFNLD GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYIDF 100
    CNKIDLRVPS GHLKEPEHPS MWGPVELVGI IAGPVFLLFL IIIIVFLVIN 150
    YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ DLVYDLSTSG SGSGLPLFVQ 200
    RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE ERSWFREAEI 250
    YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT 300
    IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA 350
    IADLGLAVRH DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC 400
    ADIYALGLVY WEIARRCNSG GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ 450
    KLRPNVPNWW QSYEALRVMG KMMRECWYAN GAARLTALRI KKTLSQLSVQ 500
    EDVKI 505
    Length:505
    Mass (Da):56,805
    Last modified:October 1, 1993 - v1
    Checksum:i377F4A5C867B3860
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S76466 mRNA. Translation: AAB33045.1.
    RefSeqiNP_954700.1. NM_199230.1.
    UniGeneiRn.214018.

    Genome annotation databases

    EnsembliENSRNOT00000009345; ENSRNOP00000009345; ENSRNOG00000006934.
    GeneIDi29381.
    KEGGirno:29381.
    UCSCiRGD:735207. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S76466 mRNA. Translation: AAB33045.1 .
    RefSeqi NP_954700.1. NM_199230.1.
    UniGenei Rn.214018.

    3D structure databases

    ProteinModelPortali P80202.
    SMRi P80202. Positions 173-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248033. 1 interaction.
    STRINGi 10116.ENSRNOP00000009345.

    PTM databases

    PhosphoSitei P80202.

    Proteomic databases

    PaxDbi P80202.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000009345 ; ENSRNOP00000009345 ; ENSRNOG00000006934 .
    GeneIDi 29381.
    KEGGi rno:29381.
    UCSCi RGD:735207. rat.

    Organism-specific databases

    CTDi 91.
    RGDi 735207. Acvr1b.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110337.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi P80202.
    KOi K13567.
    OMAi QCACTSC.
    OrthoDBi EOG7Q8CN3.
    PhylomeDBi P80202.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 5301.
    Reactomei REACT_194628. Signaling by Activin.
    REACT_194664. Signaling by NODAL.
    REACT_199248. Regulation of signaling by NODAL.

    Miscellaneous databases

    NextBioi 608961.
    PROi P80202.

    Gene expression databases

    Genevestigatori P80202.

    Family and domain databases

    InterProi IPR000472. 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 ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view ]
    SMARTi SM00467. GS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiACV1B_RAT
    AccessioniPrimary (citable) accession number: P80202
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3