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P38551 (TGFR2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length297 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – ›297›274TGF-beta receptor type-2
PRO_0000024428

Regions

Topological domain24 – 166143Extracellular Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – ›297›110Cytoplasmic Potential
Domain244 – ›297›54Protein kinase
Nucleotide binding250 – 2589ATP By similarity

Sites

Binding site2771ATP By similarity

Amino acid modifications

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

Non-terminal residue2971

Sequences

Sequence LengthMass (Da)Tools
P38551 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: F9869D3079B66A15

FASTA29733,302
        10         20         30         40         50         60 
MGRGLLGGLW PLHVVLWTRI ASTIPPHVPK SVNSDMMVTD SNGAVKLPQL CKFCDVRSST 

        70         80         90        100        110        120 
CDNQKSCLSN CSITAICEKP QEVCVAVWRK NDENITIETV CDDPKIAYHG FVLDDAASSK 

       130        140        150        160        170        180 
CIMKERKGSG ETFFMCSCSS DECNDHIIFS EEYATNNPDL LLVIFQVTGV SLLPPLGIAI 

       190        200        210        220        230        240 
AVIITFYCYR VHRQQKLSPS WDSGKPRKLM EFSEHLAIIL EDDRSDISST CANNINHNTE 

       250        260        270        280        290 
LLPIELDTLV GKGRFAEVYK AKLRQNTSEQ FETVAVKIFP YEEYASWKTE KDIFSDL 

« Hide

References

[1]"Expression cloning of the TGF-beta type II receptor, a functional transmembrane serine/threonine kinase."
Lin H.Y., Wang X.-F., Ng-Eaton E., Weinberg R.A., Lodish H.F.
Cell 68:775-785(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.

Cross-references

3D structure databases

ProteinModelPortalP38551.
SMRP38551. Positions 38-159.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG104975.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR000333. TGFB_receptor.
IPR015013. Transforming_GF_b_rcpt_2_ecto.
[Graphical view]
PANTHERPTHR23255:SF10. PTHR23255:SF10. 1 hit.
PfamPF08917. ecTbetaR2. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTGFR2_PIG
AccessionPrimary (citable) accession number: P38551
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 16, 2014
This is version 98 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