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P38438

- TGFR2_RAT

UniProt

P38438 - TGFR2_RAT

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Protein

TGF-beta receptor type-2

Gene

Tgfbr2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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

Magnesium or manganese.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei277 – 2771ATPPROSITE-ProRule annotation
Active sitei379 – 3791Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi250 – 2589ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. activation of protein kinase activity Source: Ensembl
  2. aging Source: RGD
  3. brain development Source: Ensembl
  4. bronchus morphogenesis Source: Ensembl
  5. cartilage development Source: Ensembl
  6. common-partner SMAD protein phosphorylation Source: RGD
  7. digestive tract development Source: RGD
  8. embryo implantation Source: RGD
  9. embryonic cranial skeleton morphogenesis Source: Ensembl
  10. embryonic hemopoiesis Source: Ensembl
  11. gastrulation Source: Ensembl
  12. heart development Source: Ensembl
  13. in utero embryonic development Source: Ensembl
  14. lens development in camera-type eye Source: Ensembl
  15. lens fiber cell apoptotic process Source: Ensembl
  16. lung development Source: RGD
  17. lung lobe morphogenesis Source: Ensembl
  18. mammary gland morphogenesis Source: Ensembl
  19. myeloid dendritic cell differentiation Source: Ensembl
  20. negative regulation of cardiac muscle cell proliferation Source: RGD
  21. negative regulation of cell proliferation Source: RGD
  22. organ morphogenesis Source: RGD
  23. organ regeneration Source: RGD
  24. palate development Source: Ensembl
  25. pathway-restricted SMAD protein phosphorylation Source: Ensembl
  26. patterning of blood vessels Source: Ensembl
  27. peptidyl-serine phosphorylation Source: Ensembl
  28. peptidyl-threonine phosphorylation Source: Ensembl
  29. positive regulation of angiogenesis Source: Ensembl
  30. positive regulation of B cell tolerance induction Source: Ensembl
  31. positive regulation of epithelial cell migration Source: Ensembl
  32. positive regulation of mesenchymal cell proliferation Source: Ensembl
  33. positive regulation of NK T cell differentiation Source: Ensembl
  34. positive regulation of reactive oxygen species metabolic process Source: Ensembl
  35. positive regulation of skeletal muscle tissue regeneration Source: RGD
  36. positive regulation of smooth muscle cell proliferation Source: RGD
  37. positive regulation of T cell tolerance induction Source: Ensembl
  38. positive regulation of tolerance induction to self antigen Source: Ensembl
  39. receptor-mediated endocytosis Source: RGD
  40. response to cholesterol Source: Ensembl
  41. response to drug Source: Ensembl
  42. response to estrogen Source: RGD
  43. response to glucose Source: RGD
  44. response to hypoxia Source: RGD
  45. response to mechanical stimulus Source: RGD
  46. response to nutrient Source: RGD
  47. response to organic cyclic compound Source: RGD
  48. response to organic substance Source: RGD
  49. response to steroid hormone Source: RGD
  50. smoothened signaling pathway Source: Ensembl
  51. trachea formation Source: Ensembl
  52. transforming growth factor beta receptor signaling pathway Source: RGD
  53. vasculogenesis Source: RGD
  54. wound healing Source: RGD
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

BRENDAi2.7.10.2. 5301.
ReactomeiREACT_194641. Downregulation of TGF-beta receptor signaling.
REACT_194651. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_194652. TGFBR2 MSI Frameshift Mutants in Cancer.
REACT_194657. TGFBR1 KD Mutants in Cancer.
REACT_194661. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_194677. TGF-beta receptor signaling activates SMADs.
REACT_194682. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_198828. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 8

Organism-specific databases

RGDi69651. Tgfbr2.

Subcellular locationi

GO - Cellular componenti

  1. caveola Source: MGI
  2. cell surface Source: RGD
  3. cytoplasm Source: RGD
  4. cytosol Source: RGD
  5. external side of plasma membrane Source: Ensembl
  6. integral component of plasma membrane Source: RGD
  7. membrane raft Source: MGI
  8. transforming growth factor beta receptor homodimeric complex Source: RGD
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 – 567544TGF-beta receptor type-2PRO_0000024429Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi51 ↔ 84By similarity
Disulfide bondi54 ↔ 71By similarity
Disulfide bondi61 ↔ 67By similarity
Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi77 ↔ 101By similarity
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi121 ↔ 136By similarity
Disulfide bondi138 ↔ 143By similarity
Modified residuei548 – 5481PhosphoserineBy similarity
Modified residuei553 – 5531PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP38438.
PRIDEiP38438.

Expressioni

Gene expression databases

ExpressionAtlasiP38438. baseline.
GenevestigatoriP38438.

Interactioni

Subunit structurei

Homodimer. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGFRB1 and TGFRB2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with DAXX. Interacts with TCTEX1D4. Interacts with ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor (By similarity). Interacts with and is activated by SCUBE3; this interaction does not affect TGFB1-binding to TGFBR2 (By similarity). Interacts with VPS39; this interaction is independent of the receptor kinase activity and of the presence of TGF-beta (By similarity).By similarity

Protein-protein interaction databases

BioGridi249668. 1 interaction.
IntActiP38438. 1 interaction.
STRINGi10116.ENSRNOP00000017950.

Structurei

3D structure databases

ProteinModelPortaliP38438.
SMRiP38438. Positions 40-159.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 166143ExtracellularSequence AnalysisAdd
BLAST
Topological domaini188 – 567380CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei167 – 18721HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini244 – 546303Protein 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.
InParanoidiP38438.
KOiK04388.
OMAiWETSKPR.
OrthoDBiEOG7JHM5B.
PhylomeDBiP38438.

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.

P38438-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRGLLRGLW PLHIVLWTRI ASTIPPHVPK SVNSDLMAGD NSGAVKLPQL
60 70 80 90 100
CKFCDVTLST CDNQKSCMSN CSVTSICEKP QEVCVAVWRK NDKNITLETV
110 120 130 140 150
CHDPKFTYHG FTLEDATSPT CVMKEKKRAG ETFFMCSCNT EECNDYIIFN
160 170 180 190 200
EEYTTSSPDL LLVIIQVTGV SLLPPLGIAI AVIAIFYCYR VHRQQKLSPS
210 220 230 240 250
WESSKPRKLM DFSDNCAIIL EDDRSDISST CANNINHNTE LLPIELDTLV
260 270 280 290 300
GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYSSWKTE KDIFSDINLK
310 320 330 340 350
HENILQFLTA EERKTEMGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL
360 370 380 390 400
GSSLARGIAH LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL
410 420 430 440 450
SLRLDPTLSV DDLANSGQVG TARYMAPEVL ESRMNLENME SFKQTDVYSM
460 470 480 490 500
ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE HPCVESMKDN VLRDRGRPEI
510 520 530 540 550
PSFWLNHQGI QIVCETLTEC WDHDPEARLT AQCVAERFSE LEHPDRLSGR
560
SCSQEKIPED GSLNTTK
Length:567
Mass (Da):64,241
Last modified:October 1, 1994 - v1
Checksum:iEC1D7642A51A3B75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3892KN → RS in AAB29352. (PubMed:8264154)Curated
Sequence conflicti403 – 4031R → G in AAB29352. (PubMed:8264154)Curated
Sequence conflicti405 – 4051D → S in AAB29352. (PubMed:8264154)Curated
Sequence conflicti477 – 4771K → R in AAB29352. (PubMed:8264154)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L09653 mRNA. Translation: AAA42237.1.
S67770 mRNA. Translation: AAB29352.2.
PIRiJN0459.
RefSeqiNP_112394.3. NM_031132.3.
UniGeneiRn.9954.

Genome annotation databases

EnsembliENSRNOT00000037883; ENSRNOP00000035501; ENSRNOG00000013265.
GeneIDi81810.
KEGGirno:81810.
UCSCiRGD:69651. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L09653 mRNA. Translation: AAA42237.1 .
S67770 mRNA. Translation: AAB29352.2 .
PIRi JN0459.
RefSeqi NP_112394.3. NM_031132.3.
UniGenei Rn.9954.

3D structure databases

ProteinModelPortali P38438.
SMRi P38438. Positions 40-159.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249668. 1 interaction.
IntActi P38438. 1 interaction.
STRINGi 10116.ENSRNOP00000017950.

Proteomic databases

PaxDbi P38438.
PRIDEi P38438.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000037883 ; ENSRNOP00000035501 ; ENSRNOG00000013265 .
GeneIDi 81810.
KEGGi rno:81810.
UCSCi RGD:69651. rat.

Organism-specific databases

CTDi 7048.
RGDi 69651. Tgfbr2.

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118876.
HOGENOMi HOG000231495.
HOVERGENi HBG104975.
InParanoidi P38438.
KOi K04388.
OMAi WETSKPR.
OrthoDBi EOG7JHM5B.
PhylomeDBi P38438.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 5301.
Reactomei REACT_194641. Downregulation of TGF-beta receptor signaling.
REACT_194651. SMAD2/3 MH2 Domain Mutants in Cancer.
REACT_194652. TGFBR2 MSI Frameshift Mutants in Cancer.
REACT_194657. TGFBR1 KD Mutants in Cancer.
REACT_194661. TGFBR2 Kinase Domain Mutants in Cancer.
REACT_194677. TGF-beta receptor signaling activates SMADs.
REACT_194682. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
REACT_198828. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).

Miscellaneous databases

NextBioi 615691.
PROi P38438.

Gene expression databases

ExpressionAtlasi P38438. baseline.
Genevestigatori P38438.

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. "Molecular characterization of rat transforming growth factor-beta type II receptor."
    Tsuchida K., Lewis K.A., Mathews L.S., Vale W.W.
    Biochem. Biophys. Res. Commun. 191:790-795(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Pituitary.
  2. "Rat mesangial cell hypertrophy in response to transforming growth factor-beta 1."
    Choi M.E., Kim E.G., Huang Q., Ballermann B.J.
    Kidney Int. 44:948-958(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiTGFR2_RAT
AccessioniPrimary (citable) accession number: P38438
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 29, 2014
This is version 128 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