TGF-beta receptor type-2 precursor - Gallus gallus (Chicken)

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Q90999 (TGFR2_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	557 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Apoptosis Differentiation Growth regulation
Cellular component	Cell membrane Membrane
Domain	Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Manganese Metal-binding Nucleotide-binding
Molecular function	Kinase Receptor Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of protein kinase activity Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW brain development Inferred from electronic annotation. Source: Compara bronchus morphogenesis Inferred from electronic annotation. Source: Compara cardiac epithelial to mesenchymal transition Inferred from expression pattern PubMed 8631497. Source: AgBase cartilage development Inferred from electronic annotation. Source: Compara 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: Compara embryonic hemopoiesis Inferred from electronic annotation. Source: Compara eye development Inferred from expression pattern Ref.1. Source: AgBase gastrulation Inferred from electronic annotation. Source: Compara in utero embryonic development Inferred from electronic annotation. Source: Compara lens development in camera-type eye Inferred from electronic annotation. Source: Compara lung development Inferred from expression pattern Ref.1. Source: AgBase lung lobe morphogenesis Inferred from electronic annotation. Source: Compara mammary gland morphogenesis Inferred from electronic annotation. Source: Compara myeloid dendritic cell differentiation Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara pathway-restricted SMAD protein phosphorylation Inferred from electronic annotation. Source: Compara patterning of blood vessels Inferred from electronic annotation. Source: Compara peptidyl-serine phosphorylation Inferred from electronic annotation. Source: Compara peptidyl-threonine phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of B cell tolerance induction Inferred from electronic annotation. Source: Compara positive regulation of NK T cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of T cell tolerance induction Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from mutant phenotype PubMed 8631497. Source: AgBase positive regulation of epithelial cell migration Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara positive regulation of tolerance induction to self antigen Inferred from electronic annotation. Source: Compara regulation of growth Inferred from electronic annotation. Source: UniProtKB-KW response to cholesterol Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara signal transduction by phosphorylation Inferred from electronic annotation. Source: GOC smoothened signaling pathway Inferred from electronic annotation. Source: Compara trachea formation Inferred from electronic annotation. Source: Compara transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: InterPro vasculogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from electronic annotation. Source: Compara external side of plasma membrane Traceable author statement Ref.2. Source: AgBase integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW receptor complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycosaminoglycan binding Inferred from electronic annotation. Source: Compara 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

Potential

Chain

24 – 557

534

TGF-beta receptor type-2

PRO_5000142219

Regions

Topological domain

24 – 155

132

Extracellular Potential

Transmembrane

156 – 176

Helical; Potential

Topological domain

177 – 557

381

Cytoplasmic Potential

Domain

234 – 537

304

Protein kinase

Nucleotide binding

240 – 248

ATP By similarity

Sites

Active site

369

Proton acceptor By similarity

Binding site

267

ATP By similarity

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Disulfide bond

Secondary structure

557

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q90999 [UniParc].

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

FASTA

557

63,308

        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

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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.

IPI

IPI00595267.

PIR

I50429.

RefSeq

NP_990759.1. NM_205428.1.

UniGene

Gga.2645.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KS6	NMR	-	A	36-142	[»]

ProteinModelPortal

Q90999.

SMR

Q90999. Positions 36-142.

ModBase

Search...

Protein-protein interaction databases

STRING

9031.ENSGALP00000018634.

Proteomic databases

PaxDb

Q90999.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSGALT00000018657; ENSGALP00000018634; ENSGALG00000011442.

GeneID

396399.

KEGG

gga:396399.

Organism-specific databases

CTD

7048.

Phylogenomic databases

eggNOG

COG0515.

GeneTree

ENSGT00560000076906.

HOGENOM

HOG000231495.

HOVERGEN

HBG104975.

InParanoid

Q90999.

K04388.

OMA

MMVTDNN.

OrthoDB

EOG4FTW0J.

Gene expression databases

ArrayExpress

Q90999.

Family and domain databases

InterPro

IPR000333. Activin_II/TGFBeta-II_recpt.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
IPR017194. Transform_growth_fac-b_typ-2.
IPR015013. Transforming_GF_b_rcpt_2_ecto.
[Graphical view]

PANTHER

PTHR23255:SF11. PTHR23255:SF11. 1 hit.

Pfam

PF08917. ecTbetaR2. 1 hit.
PF00069. Pkinase. 1 hit.
[Graphical view]

PIRSF

PIRSF037393. TGFRII. 1 hit.

PRINTS

PR00653. ACTIVIN2R.

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q90999.

NextBio

20816441.

Entry information

Entry name

TGFR2_CHICK

Accession

Primary (citable) accession number: Q90999

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 16, 2008
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents