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P38438 (TGFR2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
TGF-beta receptor type-2

Short name=TGFR-2
EC=2.7.11.30
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 names
Name:Tgfbr2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length567 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

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.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Post-translational modification

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

Sequence similarities

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. TGFB receptor subfamily.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Growth regulation
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from expression pattern PubMed 12051734. Source: RGD

brain development

Inferred from electronic annotation. Source: Ensembl

bronchus morphogenesis

Inferred from electronic annotation. Source: Ensembl

cartilage development

Inferred from electronic annotation. Source: Ensembl

common-partner SMAD protein phosphorylation

Inferred from direct assay PubMed 14729511. Source: RGD

digestive tract development

Inferred from expression pattern PubMed 12815632. Source: RGD

embryo development

Inferred from expression pattern PubMed 17428384. Source: RGD

embryo implantation

Inferred from expression pattern PubMed 16426643. Source: RGD

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

gastrulation

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

lens development in camera-type eye

Inferred from electronic annotation. Source: Ensembl

lens fiber cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from expression pattern PubMed 7573476. Source: RGD

lung lobe morphogenesis

Inferred from electronic annotation. Source: Ensembl

mammary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of cardiac muscle cell proliferation

Inferred from mutant phenotype PubMed 15537505. Source: RGD

negative regulation of cell proliferation

Inferred from mutant phenotype PubMed 15958511. Source: RGD

organ morphogenesis

Inferred from mutant phenotype PubMed 10767079. Source: RGD

organ regeneration

Inferred from expression pattern PubMed 9699514. Source: RGD

palate development

Inferred from electronic annotation. Source: Ensembl

pathway-restricted SMAD protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of B cell tolerance induction

Inferred from electronic annotation. Source: Ensembl

positive regulation of NK T cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell tolerance induction

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of skeletal muscle tissue regeneration

Inferred from expression pattern PubMed 10672325. Source: RGD

positive regulation of smooth muscle cell proliferation

Inferred from mutant phenotype PubMed 11178962. Source: RGD

positive regulation of tolerance induction to self antigen

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Inferred from direct assay PubMed 14729511. Source: RGD

response to cholesterol

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estrogen

Inferred from expression pattern PubMed 8759618. Source: RGD

response to glucose

Inferred from expression pattern PubMed 11178962. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 18760335. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 10432381. Source: RGD

response to nutrient

Inferred from expression pattern PubMed 11675406. Source: RGD

response to organic cyclic compound

Inferred from expression pattern PubMed 16009107. Source: RGD

response to organic substance

Inferred from expression pattern PubMed 12223100. Source: RGD

response to steroid hormone

Inferred from expression pattern PubMed 9144876. Source: RGD

smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

trachea formation

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype PubMed 18684975. Source: RGD

vasculogenesis

Inferred from expression pattern PubMed 9507219. Source: RGD

wound healing

Inferred from expression pattern PubMed 11381048. Source: RGD

   Cellular_componentcaveola

Inferred from direct assay PubMed 17878231. Source: MGI

cell surface

Inferred from direct assay PubMed 14729511. Source: RGD

cytoplasm

Inferred from direct assay PubMed 10207840PubMed 12815632. Source: RGD

cytosol

Inferred from direct assay PubMed 14729511. Source: RGD

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from direct assay PubMed 10207840. Source: RGD

membrane raft

Inferred from direct assay PubMed 17878231. Source: MGI

transforming growth factor beta receptor homodimeric complex

Inferred by curator PubMed 18684975. Source: RGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycosaminoglycan binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

mitogen-activated protein kinase kinase kinase binding

Inferred from physical interaction PubMed 16360132. Source: RGD

protein heterodimerization activity

Traceable author statement PubMed 14729511. Source: RGD

protein homodimerization activity

Traceable author statement PubMed 14729511. Source: RGD

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta receptor activity, type II

Inferred from mutant phenotype PubMed 18684975. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 567544TGF-beta receptor type-2
PRO_0000024429

Regions

Topological domain24 – 166143Extracellular Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – 567380Cytoplasmic Potential
Domain244 – 546303Protein kinase
Nucleotide binding250 – 2589ATP By similarity

Sites

Active site3791Proton acceptor By similarity
Binding site2771ATP By similarity

Amino acid modifications

Modified residue5481Phosphoserine By similarity
Modified residue5531Phosphoserine By similarity
Glycosylation701N-linked (GlcNAc...) Potential
Glycosylation941N-linked (GlcNAc...) Potential
Disulfide bond51 ↔ 84 By similarity
Disulfide bond54 ↔ 71 By similarity
Disulfide bond61 ↔ 67 By similarity
Disulfide bond77 ↔ 101 By similarity
Disulfide bond121 ↔ 136 By similarity
Disulfide bond138 ↔ 143 By similarity

Experimental info

Sequence conflict388 – 3892KN → RS in AAB29352. Ref.2
Sequence conflict4031R → G in AAB29352. Ref.2
Sequence conflict4051D → S in AAB29352. Ref.2
Sequence conflict4771K → R in AAB29352. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P38438 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: EC1D7642A51A3B75

FASTA56764,241
        10         20         30         40         50         60 
MGRGLLRGLW PLHIVLWTRI ASTIPPHVPK SVNSDLMAGD NSGAVKLPQL CKFCDVTLST 

        70         80         90        100        110        120 
CDNQKSCMSN CSVTSICEKP QEVCVAVWRK NDKNITLETV CHDPKFTYHG FTLEDATSPT 

       130        140        150        160        170        180 
CVMKEKKRAG ETFFMCSCNT EECNDYIIFN EEYTTSSPDL LLVIIQVTGV SLLPPLGIAI 

       190        200        210        220        230        240 
AVIAIFYCYR VHRQQKLSPS WESSKPRKLM DFSDNCAIIL EDDRSDISST CANNINHNTE 

       250        260        270        280        290        300 
LLPIELDTLV GKGRFAEVYK AKLKQNTSEQ FETVAVKIFP YEEYSSWKTE KDIFSDINLK 

       310        320        330        340        350        360 
HENILQFLTA EERKTEMGKQ YWLITAFHAK GNLQEYLTRH VISWEDLRKL GSSLARGIAH 

       370        380        390        400        410        420 
LHSDHTPCGR PKMPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPTLSV DDLANSGQVG 

       430        440        450        460        470        480 
TARYMAPEVL ESRMNLENME SFKQTDVYSM ALVLWEMTSR CNAVGEVKDY EPPFGSKVRE 

       490        500        510        520        530        540 
HPCVESMKDN VLRDRGRPEI PSFWLNHQGI QIVCETLTEC WDHDPEARLT AQCVAERFSE 

       550        560 
LEHPDRLSGR SCSQEKIPED GSLNTTK 

« Hide

References

[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09653 mRNA. Translation: AAA42237.1.
S67770 mRNA. Translation: AAB29352.2.
PIRJN0459.
RefSeqNP_112394.3. NM_031132.3.
UniGeneRn.9954.

3D structure databases

ProteinModelPortalP38438.
SMRP38438. Positions 40-159.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249668. 1 interaction.
IntActP38438. 1 interaction.
STRING10116.ENSRNOP00000017950.

Proteomic databases

PaxDbP38438.
PRIDEP38438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000037883; ENSRNOP00000035501; ENSRNOG00000013265.
GeneID81810.
KEGGrno:81810.
UCSCRGD:69651. rat.

Organism-specific databases

CTD7048.
RGD69651. Tgfbr2.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000076906.
HOGENOMHOG000231495.
HOVERGENHBG104975.
KOK04388.
OMAWETSKPR.
OrthoDBEOG7JHM5B.
PhylomeDBP38438.

Enzyme and pathway databases

BRENDA2.7.10.2. 5301.

Gene expression databases

ArrayExpressP38438.
GenevestigatorP38438.

Family and domain databases

InterProIPR011009. 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]
PANTHERPTHR23255:SF10. PTHR23255:SF10. 1 hit.
PfamPF08917. ecTbetaR2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFPIRSF037393. TGFRII. 1 hit.
PRINTSPR00653. ACTIVIN2R.
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615691.
PROP38438.

Entry information

Entry nameTGFR2_RAT
AccessionPrimary (citable) accession number: P38438
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families