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Q90999

- TGFR2_CHICK

UniProt

Q90999 - TGFR2_CHICK

Protein

TGF-beta receptor type-2

Gene

TGFBR2

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Transmembrane serine/threonine kinase forming with the TGF-beta type I serine/threonine kinase receptor, TGFBR1, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFRB1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways 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 sitei267 – 2671ATPPROSITE-ProRule annotation
    Active sitei369 – 3691Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi240 – 2489ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glycosaminoglycan binding Source: Ensembl
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. receptor signaling protein serine/threonine kinase activity Source: InterPro
    6. transforming growth factor beta binding Source: AgBase
    7. transforming growth factor beta receptor activity, type II Source: InterPro

    GO - Biological processi

    1. activation of protein kinase activity Source: Ensembl
    2. brain development Source: Ensembl
    3. bronchus morphogenesis Source: Ensembl
    4. cardiac epithelial to mesenchymal transition Source: AgBase
    5. cartilage development Source: Ensembl
    6. cell activation Source: AgBase
    7. cell migration Source: AgBase
    8. embryo development Source: AgBase
    9. embryonic cranial skeleton morphogenesis Source: Ensembl
    10. embryonic hemopoiesis Source: Ensembl
    11. eye development Source: AgBase
    12. gastrulation Source: Ensembl
    13. heart development Source: AgBase
    14. in utero embryonic development Source: Ensembl
    15. lens development in camera-type eye Source: Ensembl
    16. lens fiber cell apoptotic process Source: Ensembl
    17. lung development Source: AgBase
    18. lung lobe morphogenesis Source: Ensembl
    19. mammary gland morphogenesis Source: Ensembl
    20. mesenchymal cell differentiation Source: AgBase
    21. myeloid dendritic cell differentiation Source: Ensembl
    22. palate development Source: Ensembl
    23. pathway-restricted SMAD protein phosphorylation Source: Ensembl
    24. patterning of blood vessels Source: Ensembl
    25. peptidyl-serine phosphorylation Source: Ensembl
    26. peptidyl-threonine phosphorylation Source: Ensembl
    27. positive regulation of B cell tolerance induction Source: Ensembl
    28. positive regulation of cell migration Source: AgBase
    29. positive regulation of epithelial cell migration Source: Ensembl
    30. positive regulation of epithelial to mesenchymal transition Source: AgBase
    31. positive regulation of mesenchymal cell proliferation Source: Ensembl
    32. positive regulation of NK T cell differentiation Source: Ensembl
    33. positive regulation of reactive oxygen species metabolic process Source: Ensembl
    34. positive regulation of T cell tolerance induction Source: Ensembl
    35. positive regulation of tolerance induction to self antigen Source: Ensembl
    36. regulation of growth Source: UniProtKB-KW
    37. response to cholesterol Source: Ensembl
    38. response to drug Source: Ensembl
    39. smoothened signaling pathway Source: Ensembl
    40. trachea formation Source: Ensembl
    41. transforming growth factor beta receptor signaling pathway Source: Ensembl
    42. vasculogenesis Source: Ensembl

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Apoptosis, Differentiation, Growth regulation

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_195006. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_195008. TGF-beta receptor signaling activates SMADs.
    REACT_198125. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_211903. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_214793. Downregulation of TGF-beta receptor signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TGF-beta receptor type-2 (EC:2.7.11.30)
    Short name:
    TGFR-2
    Alternative name(s):
    TGF-beta type II receptor
    Transforming growth factor-beta receptor type II
    Short name:
    TGF-beta receptor type II
    Short name:
    TbetaR-II
    Gene namesi
    Name:TGFBR2
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Chromosome 2

    Subcellular locationi

    GO - Cellular componenti

    1. caveola Source: Ensembl
    2. cell Source: AgBase
    3. external side of plasma membrane Source: AgBase
    4. integral component of membrane Source: UniProtKB-KW
    5. receptor complex Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 557534TGF-beta receptor type-2PRO_5000142219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi41 ↔ 741 Publication
    Disulfide bondi44 ↔ 611 Publication
    Disulfide bondi51 ↔ 571 Publication
    Glycosylationi62 – 621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi67 ↔ 911 Publication
    Glycosylationi84 – 841N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi111 ↔ 1261 Publication
    Disulfide bondi128 ↔ 1331 Publication

    Post-translational modificationi

    Phosphorylated on a Ser/Thr residue in the cytoplasmic domain.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ90999.

    Expressioni

    Tissue specificityi

    Detected at low levels in embryonic heart, brain and lung. Detected at high levels in hatchling heart and lung.1 Publication

    Interactioni

    Subunit structurei

    Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer.By similarity

    Protein-protein interaction databases

    IntActiQ90999. 1 interaction.
    STRINGi9031.ENSGALP00000018634.

    Structurei

    Secondary structure

    1
    557
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 485
    Beta strandi69 – 713
    Beta strandi74 – 818
    Beta strandi84 – 907
    Beta strandi106 – 1105
    Beta strandi114 – 1163
    Beta strandi119 – 13214
    Turni133 – 1353

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KS6NMR-A36-142[»]
    ProteinModelPortaliQ90999.
    SMRiQ90999. Positions 36-142.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ90999.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 155132ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini177 – 557381CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei156 – 17621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini234 – 537304Protein 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.
    HOVERGENiHBG104975.
    InParanoidiQ90999.
    KOiK04388.
    OrthoDBiEOG7JHM5B.
    PhylomeDBiQ90999.
    TreeFamiTF314724.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000333. TGFB_receptor.
    IPR017194. Transform_growth_fac-b_typ-2.
    IPR015013. Transforming_GF_b_rcpt_2_ecto.
    [Graphical view]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF08917. ecTbetaR2. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037393. TGFRII. 1 hit.
    PRINTSiPR00653. ACTIVIN2R.
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. 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.

    Q90999-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPPRLRPLLL RVSLWVLVGS SSPALLHDRS KENGLQLPRL CKFCDVKATT    50
    CSNQDQCKSN CNITSICEKN NEVCAAVWRR NDENVTLETI CHDPQKRLYG 100
    HMLDDSSSEQ CVMKEKKDDG GLMFMCSCTG EECNDVLIFS AIDPHKPEEK 150
    DEISKVTIIS LVPLLVISVA VIVIFYAYRT HKKRKLNKAW EKNVKPKKHK 200
    DCSDVCAIML DDDHSDISST CANNINHNTE LLPIELDIVV GKGRFAEVYK 250
    AKLKQNTSEQ YETVAVKIFP YEEYASWKTE KDIFSDVNLK HENILQFLTA 300
    EERKTDLGKQ YWLITAFHAR GNLQEYLTRH IISWEDLWKL GGSLARGIAH 350
    LHSDHTPCGR PKTPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPSLSV 400
    DDLANSGQVG TARYMAPEVL ESRMNLENME SFKQTDVYSM ALVLWEMTSR 450
    CNGVGEVKEY EPPFGSKVRE HPCVESMKDN VLRDRGRPEI PSSWLNHQGI 500
    QMVCETLIEC WDHDPEARLT AQCVAERFSE FKHHDKLSGR SCSEEKIPED 550
    GSVTTAK 557
    Length:557
    Mass (Da):63,308
    Last modified:November 1, 1996 - v1
    Checksum:i0C578ABFAB357DF1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18784 mRNA. Translation: AAA49091.1.
    PIRiI50429.
    RefSeqiNP_990759.1. NM_205428.1.
    UniGeneiGga.2645.

    Genome annotation databases

    EnsembliENSGALT00000018657; ENSGALP00000018634; ENSGALG00000011442.
    ENSGALT00000037691; ENSGALP00000036896; ENSGALG00000011442.
    GeneIDi396399.
    KEGGigga:396399.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L18784 mRNA. Translation: AAA49091.1 .
    PIRi I50429.
    RefSeqi NP_990759.1. NM_205428.1.
    UniGenei Gga.2645.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KS6 NMR - A 36-142 [» ]
    ProteinModelPortali Q90999.
    SMRi Q90999. Positions 36-142.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q90999. 1 interaction.
    STRINGi 9031.ENSGALP00000018634.

    Proteomic databases

    PaxDbi Q90999.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSGALT00000018657 ; ENSGALP00000018634 ; ENSGALG00000011442 .
    ENSGALT00000037691 ; ENSGALP00000036896 ; ENSGALG00000011442 .
    GeneIDi 396399.
    KEGGi gga:396399.

    Organism-specific databases

    CTDi 7048.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00560000076906.
    HOGENOMi HOG000231495.
    HOVERGENi HBG104975.
    InParanoidi Q90999.
    KOi K04388.
    OrthoDBi EOG7JHM5B.
    PhylomeDBi Q90999.
    TreeFami TF314724.

    Enzyme and pathway databases

    Reactomei REACT_195006. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_195008. TGF-beta receptor signaling activates SMADs.
    REACT_198125. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_211903. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_214793. Downregulation of TGF-beta receptor signaling.

    Miscellaneous databases

    EvolutionaryTracei Q90999.
    NextBioi 20816441.
    PROi Q90999.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR000333. TGFB_receptor.
    IPR017194. Transform_growth_fac-b_typ-2.
    IPR015013. Transforming_GF_b_rcpt_2_ecto.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF08917. ecTbetaR2. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037393. TGFRII. 1 hit.
    PRINTSi PR00653. ACTIVIN2R.
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and developmental expression of the chick type II and type III TGF beta receptors."
      Barnett J.V., Moustakas A., Lin W., Wang X.-F., Lin H.Y., Galper J.B., Maas R.L.
      Dev. Dyn. 199:12-27(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TGF-BETA, TISSUE SPECIFICITY.
      Tissue: Embryonic brain.
    2. "Solution structure of the chick TGFbeta type II receptor ligand-binding domain."
      Marlow M.S., Brown C.B., Barnett J.V., Krezel A.M.
      J. Mol. Biol. 326:989-997(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 36-142, DISULFIDE BONDS.

    Entry informationi

    Entry nameiTGFR2_CHICK
    AccessioniPrimary (citable) accession number: Q90999
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 16, 2008
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 116 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

    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