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)

P38445

- AVR2B_RAT

UniProt

P38445 - AVR2B_RAT

Protein

Activin receptor type-2B

Gene

Acvr2b

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (13 Nov 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.By similarity

    Catalytic activityi

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

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei217 – 2171ATPPROSITE-ProRule annotation
    Active sitei322 – 3221Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi196 – 2049ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. activation of protein kinase activity Source: Ensembl
    2. anterior/posterior pattern specification Source: Ensembl
    3. artery development Source: Ensembl
    4. blood vessel remodeling Source: Ensembl
    5. BMP signaling pathway Source: Ensembl
    6. determination of left/right symmetry Source: Ensembl
    7. embryonic foregut morphogenesis Source: Ensembl
    8. gastrulation with mouth forming second Source: Ensembl
    9. heart development Source: Ensembl
    10. insulin secretion Source: Ensembl
    11. kidney development Source: Ensembl
    12. lung development Source: Ensembl
    13. lymphangiogenesis Source: Ensembl
    14. lymphatic endothelial cell differentiation Source: Ensembl
    15. mesoderm development Source: Ensembl
    16. odontogenesis of dentin-containing tooth Source: Ensembl
    17. organ growth Source: Ensembl
    18. palate development Source: Ensembl
    19. pancreas development Source: Ensembl
    20. positive regulation of activin receptor signaling pathway Source: Ensembl
    21. positive regulation of bone mineralization Source: Ensembl
    22. positive regulation of osteoblast differentiation Source: Ensembl
    23. post-embryonic development Source: Ensembl
    24. protein phosphorylation Source: RGD
    25. response to glucose Source: Ensembl
    26. retina vasculature development in camera-type eye Source: Ensembl
    27. sexual reproduction Source: RGD
    28. skeletal system morphogenesis Source: Ensembl
    29. venous blood vessel development Source: Ensembl

    Keywords - Molecular functioni

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

    Keywords - Ligandi

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

    Enzyme and pathway databases

    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-2B (EC:2.7.11.30)
    Alternative name(s):
    Activin receptor type IIB
    Short name:
    ACTR-IIB
    Gene namesi
    Name:Acvr2b
    Synonyms:Actriib
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 8

    Organism-specific databases

    RGDi2028. Acvr2b.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 513495Activin receptor type-2BPRO_0000024406Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 59By similarity
    Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi49 ↔ 77By similarity
    Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi84 ↔ 103By similarity
    Disulfide bondi90 ↔ 102By similarity
    Disulfide bondi104 ↔ 109By similarity

    Post-translational modificationi

    Phosphorylated. Constitutive phosphorylation is in part catalyzed by its own kinase activity By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP38445.

    Expressioni

    Gene expression databases

    GenevestigatoriP38445.

    Interactioni

    Subunit structurei

    Forms an activin receptor complex with activin type II receptors such as ACVR1B. Interacts with VPS39.By similarity

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000049841.

    Structurei

    Secondary structure

    1
    513
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 336
    Turni34 – 407
    Beta strandi43 – 486
    Beta strandi57 – 659
    Beta strandi70 – 7910
    Helixi82 – 843
    Beta strandi89 – 924
    Beta strandi98 – 1047
    Helixi109 – 1113
    Beta strandi112 – 1154

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NYSX-ray3.05A/C19-119[»]
    1NYUX-ray3.10A/C19-119[»]
    ProteinModelPortaliP38445.
    SMRiP38445. Positions 26-120, 190-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38445.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 137119ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini159 – 513355CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei138 – 15821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini190 – 481292Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00560000076906.
    HOGENOMiHOG000231495.
    HOVERGENiHBG054502.
    KOiK13596.
    OrthoDBiEOG7JHM5B.

    Family and domain databases

    InterProiIPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000333. TGFB_receptor.
    [Graphical view]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PRINTSiPR00653. ACTIVIN2R.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50011. 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.

    P38445-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTAPWAALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE    50
    GEQDKRLHCY ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY 100
    FCCCEGNFCN ERFTHLPEPG GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS 150
    LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP PSPLVGLKPL QLLEIKARGR 200
    FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK HENLLQFIAA 250
    EKRGCSNLEV ELWLITAFHD KGSLTDYLKG NIITWNELCH VAETMSRGLS 300
    YLHEDVPWCR GEGHKPSIAH RDFKSKNVLL KSDLTAVLAD FGLAVRFEPG 350
    KPPGDTHGQV GTRRYMAPEV LEGAINFQRD AFLRIDMYAM GLVLWELVSR 400
    CKAADGPVDE YMLPFEEEIG QHPSLEELQE VVVHKKMRPT IKDHWLKHPG 450
    LAQLCVTIEE CWDHDAEARL SAGCVEERVS LIRRSVNSST SDCLVSLVTS 500
    VTNVDLLPKE SSI 513
    Length:513
    Mass (Da):57,857
    Last modified:November 13, 2007 - v3
    Checksum:i765DB33F11C64CA7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti64 – 641R → P in AAA40772. (PubMed:1312838)Curated
    Sequence conflicti64 – 641R → P(PubMed:7916681)Curated
    Sequence conflicti255 – 2551Missing(PubMed:7916681)Curated
    Sequence conflicti255 – 2551Missing in AAH97358. (PubMed:15489334)Curated
    Sequence conflicti488 – 4881S → G in AAA40772. (PubMed:1312838)Curated
    Sequence conflicti488 – 4881S → G(PubMed:7916681)Curated
    Sequence conflicti501 – 5011V → S in AAA40772. (PubMed:1312838)Curated
    Sequence conflicti501 – 5011V → S(PubMed:7916681)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10640 mRNA. Translation: AAA40772.1.
    BC097358 mRNA. Translation: AAH97358.1.
    PIRiB49193.
    JQ1484.
    RefSeqiNP_113742.1. NM_031554.1.
    UniGeneiRn.24240.

    Genome annotation databases

    EnsembliENSRNOT00000019777; ENSRNOP00000019777; ENSRNOG00000014477.
    GeneIDi25366.
    KEGGirno:25366.
    UCSCiRGD:2028. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L10640 mRNA. Translation: AAA40772.1 .
    BC097358 mRNA. Translation: AAH97358.1 .
    PIRi B49193.
    JQ1484.
    RefSeqi NP_113742.1. NM_031554.1.
    UniGenei Rn.24240.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NYS X-ray 3.05 A/C 19-119 [» ]
    1NYU X-ray 3.10 A/C 19-119 [» ]
    ProteinModelPortali P38445.
    SMRi P38445. Positions 26-120, 190-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000049841.

    Proteomic databases

    PaxDbi P38445.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000019777 ; ENSRNOP00000019777 ; ENSRNOG00000014477 .
    GeneIDi 25366.
    KEGGi rno:25366.
    UCSCi RGD:2028. rat.

    Organism-specific databases

    CTDi 93.
    RGDi 2028. Acvr2b.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00560000076906.
    HOGENOMi HOG000231495.
    HOVERGENi HBG054502.
    KOi K13596.
    OrthoDBi EOG7JHM5B.

    Enzyme and pathway databases

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

    Miscellaneous databases

    EvolutionaryTracei P38445.
    NextBioi 606365.
    PROi P38445.

    Gene expression databases

    Genevestigatori P38445.

    Family and domain databases

    InterProi IPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000333. TGFB_receptor.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PRINTSi PR00653. ACTIVIN2R.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 19-119 IN COMPLEX WITH HUMAN INHBA.

    Entry informationi

    Entry nameiAVR2B_RAT
    AccessioniPrimary (citable) accession number: P38445
    Secondary accession number(s): Q4V8J8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: November 13, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3