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Q90999

- TGFR2_CHICK

UniProt

Q90999 - TGFR2_CHICK

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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

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

Mg2+By similarity, Mn2+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. receptor signaling protein serine/threonine kinase activity Source: InterPro
  5. transforming growth factor beta binding Source: AgBase
  6. 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. lens development in camera-type eye Source: Ensembl
  15. lens fiber cell apoptotic process Source: Ensembl
  16. lung development Source: AgBase
  17. lung lobe morphogenesis Source: Ensembl
  18. mesenchymal cell differentiation Source: AgBase
  19. myeloid dendritic cell differentiation Source: Ensembl
  20. palate development Source: Ensembl
  21. pathway-restricted SMAD protein phosphorylation Source: Ensembl
  22. patterning of blood vessels Source: Ensembl
  23. peptidyl-serine phosphorylation Source: Ensembl
  24. peptidyl-threonine phosphorylation Source: Ensembl
  25. positive regulation of angiogenesis Source: Ensembl
  26. positive regulation of B cell tolerance induction Source: Ensembl
  27. positive regulation of cell migration Source: AgBase
  28. positive regulation of epithelial cell migration Source: Ensembl
  29. positive regulation of epithelial to mesenchymal transition Source: AgBase
  30. positive regulation of mesenchymal cell proliferation Source: Ensembl
  31. positive regulation of NK T cell differentiation Source: Ensembl
  32. positive regulation of reactive oxygen species metabolic process Source: Ensembl
  33. positive regulation of T cell tolerance induction Source: Ensembl
  34. positive regulation of tolerance induction to self antigen Source: Ensembl
  35. regulation of growth Source: UniProtKB-KW
  36. response to cholesterol Source: Ensembl
  37. response to drug Source: Ensembl
  38. smoothened signaling pathway Source: Ensembl
  39. trachea formation Source: Ensembl
  40. transforming growth factor beta receptor signaling pathway Source: Ensembl
  41. vasculogenesis Source: Ensembl
Complete GO annotation...

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 groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Chromosome 2

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 155132ExtracellularSequence AnalysisAdd
BLAST
Transmembranei156 – 17621HelicalSequence AnalysisAdd
BLAST
Topological domaini177 – 557381CytoplasmicSequence AnalysisAdd
BLAST

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
Complete GO annotation...

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 – 485Combined sources
Beta strandi69 – 713Combined sources
Beta strandi74 – 818Combined sources
Beta strandi84 – 907Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 13214Combined sources
Turni133 – 1353Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ90999.

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.
GeneTreeiENSGT00760000118876.
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

        10         20         30         40         50
MPPRLRPLLL RVSLWVLVGS SSPALLHDRS KENGLQLPRL CKFCDVKATT
60 70 80 90 100
CSNQDQCKSN CNITSICEKN NEVCAAVWRR NDENVTLETI CHDPQKRLYG
110 120 130 140 150
HMLDDSSSEQ CVMKEKKDDG GLMFMCSCTG EECNDVLIFS AIDPHKPEEK
160 170 180 190 200
DEISKVTIIS LVPLLVISVA VIVIFYAYRT HKKRKLNKAW EKNVKPKKHK
210 220 230 240 250
DCSDVCAIML DDDHSDISST CANNINHNTE LLPIELDIVV GKGRFAEVYK
260 270 280 290 300
AKLKQNTSEQ YETVAVKIFP YEEYASWKTE KDIFSDVNLK HENILQFLTA
310 320 330 340 350
EERKTDLGKQ YWLITAFHAR GNLQEYLTRH IISWEDLWKL GGSLARGIAH
360 370 380 390 400
LHSDHTPCGR PKTPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPSLSV
410 420 430 440 450
DDLANSGQVG TARYMAPEVL ESRMNLENME SFKQTDVYSM ALVLWEMTSR
460 470 480 490 500
CNGVGEVKEY EPPFGSKVRE HPCVESMKDN VLRDRGRPEI PSSWLNHQGI
510 520 530 540 550
QMVCETLIEC WDHDPEARLT AQCVAERFSE FKHHDKLSGR SCSEEKIPED

GSVTTAK
Length:557
Mass (Da):63,308
Last modified:November 1, 1996 - v1
Checksum:i0C578ABFAB357DF1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000118876.
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: November 26, 2014
This is version 118 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