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Q90999 (TGFR2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.1

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

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.

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

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

Post-translational modification

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

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 term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

brain development

Inferred from electronic annotation. Source: Ensembl

bronchus morphogenesis

Inferred from electronic annotation. Source: Ensembl

cardiac epithelial to mesenchymal transition

Inferred from expression pattern PubMed 8631497. Source: AgBase

cartilage development

Inferred from electronic annotation. Source: Ensembl

cell activation

Inferred from mutant phenotype PubMed 8631497. Source: AgBase

cell migration

Traceable author statement PubMed 10885742. Source: AgBase

embryo development

Inferred from expression pattern Ref.1. Source: AgBase

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic hemopoiesis

Inferred from electronic annotation. Source: Ensembl

eye development

Inferred from expression pattern Ref.1. Source: AgBase

gastrulation

Inferred from electronic annotation. Source: Ensembl

heart development

Inferred from expression pattern Ref.1PubMed 8631497. Source: AgBase

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 Ref.1. Source: AgBase

lung lobe morphogenesis

Inferred from electronic annotation. Source: Ensembl

mammary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

mesenchymal cell differentiation

Inferred from mutant phenotype PubMed 8631497. Source: AgBase

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

patterning of blood vessels

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 cell migration

Inferred from mutant phenotype PubMed 8631497. Source: AgBase

positive regulation of epithelial cell migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from mutant phenotype PubMed 8631497. Source: AgBase

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of tolerance induction to self antigen

Inferred from electronic annotation. Source: Ensembl

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

response to cholesterol

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: InterPro

vasculogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell

Inferred from direct assay PubMed 10075204. Source: AgBase

external side of plasma membrane

Traceable author statement Ref.2. Source: AgBase

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

receptor complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

receptor signaling protein serine/threonine kinase activity

Inferred from electronic annotation. Source: InterPro

transforming growth factor beta binding

Inferred from mutant phenotype Ref.1. Source: AgBase

transforming growth factor beta receptor activity, type II

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 557534TGF-beta receptor type-2
PRO_5000142219

Regions

Topological domain24 – 155132Extracellular Potential
Transmembrane156 – 17621Helical; Potential
Topological domain177 – 557381Cytoplasmic Potential
Domain234 – 537304Protein kinase
Nucleotide binding240 – 2489ATP By similarity

Sites

Active site3691Proton acceptor By similarity
Binding site2671ATP By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential
Glycosylation841N-linked (GlcNAc...) Potential
Disulfide bond41 ↔ 74 Ref.2
Disulfide bond44 ↔ 61 Ref.2
Disulfide bond51 ↔ 57 Ref.2
Disulfide bond67 ↔ 91 Ref.2
Disulfide bond111 ↔ 126 Ref.2
Disulfide bond128 ↔ 133 Ref.2

Secondary structure

................ 557
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q90999 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 0C578ABFAB357DF1

FASTA55763,308
        10         20         30         40         50         60 
MPPRLRPLLL RVSLWVLVGS SSPALLHDRS KENGLQLPRL CKFCDVKATT CSNQDQCKSN 

        70         80         90        100        110        120 
CNITSICEKN NEVCAAVWRR NDENVTLETI CHDPQKRLYG HMLDDSSSEQ CVMKEKKDDG 

       130        140        150        160        170        180 
GLMFMCSCTG EECNDVLIFS AIDPHKPEEK DEISKVTIIS LVPLLVISVA VIVIFYAYRT 

       190        200        210        220        230        240 
HKKRKLNKAW EKNVKPKKHK DCSDVCAIML DDDHSDISST CANNINHNTE LLPIELDIVV 

       250        260        270        280        290        300 
GKGRFAEVYK AKLKQNTSEQ YETVAVKIFP YEEYASWKTE KDIFSDVNLK HENILQFLTA 

       310        320        330        340        350        360 
EERKTDLGKQ YWLITAFHAR GNLQEYLTRH IISWEDLWKL GGSLARGIAH LHSDHTPCGR 

       370        380        390        400        410        420 
PKTPIVHRDL KSSNILVKND LTCCLCDFGL SLRLDPSLSV DDLANSGQVG TARYMAPEVL 

       430        440        450        460        470        480 
ESRMNLENME SFKQTDVYSM ALVLWEMTSR CNGVGEVKEY EPPFGSKVRE HPCVESMKDN 

       490        500        510        520        530        540 
VLRDRGRPEI PSSWLNHQGI QMVCETLIEC WDHDPEARLT AQCVAERFSE FKHHDKLSGR 

       550 
SCSEEKIPED GSVTTAK 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18784 mRNA. Translation: AAA49091.1.
PIRI50429.
RefSeqNP_990759.1. NM_205428.1.
UniGeneGga.2645.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KS6NMR-A36-142[»]
ProteinModelPortalQ90999.
SMRQ90999. Positions 36-142.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ90999. 1 interaction.
STRING9031.ENSGALP00000018634.

Proteomic databases

PaxDbQ90999.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000018657; ENSGALP00000018634; ENSGALG00000011442.
ENSGALT00000037691; ENSGALP00000036896; ENSGALG00000011442.
GeneID396399.
KEGGgga:396399.

Organism-specific databases

CTD7048.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00560000076906.
HOGENOMHOG000231495.
HOVERGENHBG104975.
InParanoidQ90999.
KOK04388.
OMAWETSKPR.
OrthoDBEOG7JHM5B.
PhylomeDBQ90999.
TreeFamTF314724.

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

EvolutionaryTraceQ90999.
NextBio20816441.
PROQ90999.

Entry information

Entry nameTGFR2_CHICK
AccessionPrimary (citable) accession number: Q90999
Entry history
Integrated into UniProtKB/Swiss-Prot: December 16, 2008
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 112 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references