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Reviewed, UniProtKB/Swiss-Prot P80204 (TGFR1_RAT)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    TGF-beta receptor type-1
    EC=2.7.11.30
Alternative name(s):
    Transforming growth factor-beta receptor type I
      Short name=TGF-beta receptor type I
    TGF-beta type I receptor
    TbetaR-I
    TGFR-1
    Serine/threonine-protein kinase receptor R4
      Short name=SKR4
Gene names
Name: Tgfbr1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for TGF-beta.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with CD109. The unphosphorylated protein interacts with FKBP1A and is stabilized the inactive conformation. Phosphorylation of the GS region abrogates FKBP1A binding. Interacts with SMAD2 when phosphorylated on several residues in the GS region By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Urogenital ridge, testis, ovary, brain and lungs.

Post-translational modification

Phosphorylated at basal levels in the absence of ligand binding. Activated by multiple phosphorylation, mainly in the GS region By similarity.

Sequence similarities

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

Contains 1 GS domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentMembrane
   DomainSignal
Transmembrane
   LigandATP-binding
Magnesium
Manganese
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Gene Ontology (GO)
   Biological processaging

Inferred from expression pattern. Source: RGD

embryo implantation

Inferred from expression pattern. Source: RGD

gut development

Inferred from expression pattern. Source: RGD

lung development

Inferred from expression pattern. Source: RGD

negative regulation of endothelial cell differentiation

Inferred from mutant phenotype. Source: RGD

organ regeneration

Inferred from expression pattern. Source: RGD

protein amino acid autophosphorylation

Inferred from mutant phenotype. Source: RGD

response to electrical stimulus

Inferred from expression pattern. Source: RGD

response to estrogen stimulus

Inferred from direct assay. Source: RGD

response to hypoxia

Inferred from expression pattern. Source: RGD

response to organic cyclic substance

Inferred from expression pattern. Source: RGD

response to prostaglandin E stimulus

Inferred from expression pattern. Source: RGD

response to toxin

Inferred from expression pattern. Source: RGD

transforming growth factor beta receptor signaling pathway

Inferred from mutant phenotype. Source: RGD

   Cellular componentapical plasma membrane

Inferred from direct assay. Source: RGD

basolateral plasma membrane

Inferred from direct assay. Source: RGD

transforming growth factor beta receptor complex

Inferred by curator. Source: RGD

   Molecular functionATP binding

Inferred from mutant phenotype. Source: RGD

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein complex binding

Inferred from physical interaction. Source: RGD

protein heterodimerization activity

Inferred from mutant phenotype. Source: RGD

transforming growth factor beta binding

Inferred from direct assay. Source: RGD

transforming growth factor beta receptor activity, type I

Inferred from mutant phenotype. Source: RGD

ubiquitin protein ligase binding

Inferred from physical interaction. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 501479TGF-beta receptor type-1
PRO_0000024425

Regions

Topological domain23 – 123101Extracellular Potential
Transmembrane124 – 14623 Potential
Topological domain147 – 501355Cytoplasmic Potential
Domain173 – 20230GS
Domain203 – 493291Protein kinase
Nucleotide binding209 – 2179ATP By similarity

Sites

Active site3311Proton acceptor By similarity
Binding site2301ATP By similarity

Amino acid modifications

Modified residue1831Phosphothreonine By similarity
Modified residue1841Phosphothreonine By similarity
Modified residue1851Phosphoserine By similarity
Modified residue1871Phosphoserine By similarity
Modified residue1891Phosphoserine By similarity
Glycosylation411N-linked (GlcNAc...) Potential
Disulfide bond32 ↔ 50 By similarity
Disulfide bond34 ↔ 37 By similarity
Disulfide bond44 ↔ 67 By similarity
Disulfide bond82 ↔ 94 By similarity
Disulfide bond95 ↔ 100 By similarity

Sequences

Sequence LengthMass (Da)Tools
P80204-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: EAD7F8D37E456102

FASTA50156,000
        10         20         30         40         50         60 
MEAASAALRR CLLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC FVSVTETTDK 

        70         80         90        100        110        120 
VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTYCCNQDHC NKIELPTTGP FSEKQSAGLG 

       130        140        150        160        170        180 
PVELAAVIAG PVCFVCIALM LMVYICHNRT VIHHRVPNEE DPSLDRPFIS EGTTLKDLIY 

       190        200        210        220        230        240 
DMTTSGSGSG LPLLVQRTIA RTIVLQESIG KGRFGEVWRG KWRGEEVAVK IFSSREERSW 

       250        260        270        280        290        300 
FREAEIYQTV MLRHENILGF IAADNKDNGT WTQLWLVSDY HEHGSLFDYL NRYTVTVEGM 

       310        320        330        340        350        360 
IKLALSTASG LAHLHMEIVG TQGKPAIAHR DLKSKNILVK KNGTCCIADL GLAVRHDSAT 

       370        380        390        400        410        420 
DTIDIAPNHR VGTKRYMAPE VLDDSINMKH FESFKRADIY AMGLVFWEIA RRCSIGGIHE 

       430        440        450        460        470        480 
DYQLPYYDLV PSDPSVEEMR KVVCEQKLRP NIPNRWQSCE ALRVMAKIMR ECWYANGAAR 

       490        500 
LTALRIKKTL SQLSQQEGIK M 

« Hide

References

[1]"Developmental expression of four novel serine/threonine kinase receptors homologous to the activin/transforming growth factor-beta type II receptor family."
He W.-W., Gustafson M.L., Hirobe S., Donahoe P.K.
Dev. Dyn. 196:133-142(1993) [PubMed: 8395914] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Urogenital ridge.
+Additional computationally mapped references.

Cross-references

Sequence databases

L26110 mRNA. Translation: AAA83216.1.
IPIIPI00195461.
UniGeneRn.44402

3D structure databases

HSSPHSSP built from PDB template 1IAS based on UniProtKB P36897.
SMRP80204. Positions 199-501.
ModBaseSearch...

Genome annotation databases

EnsemblENSRNOG00000007036. Rattus norvegicus. [Contig view]

Organism-specific databases

RGD3852. Tgfbr1.

Phylogenomic databases

HOVERGENP80204.

Enzyme and pathway databases

BRENDA2.7.10.2. 248.
2.7.11.30. 248.

Gene expression databases

ArrayExpressP80204.
GermOnlineENSRNOG00000007036. Rattus norvegicus.

Family and domain databases

InterProIPR000472. Activin_rcpt.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR003605. TGF_beta_rcpt_GS.
[Graphical view]
PfamPF01064. Activin_recp. 1 hit.
PF00069. Pkinase. 1 hit.
PF08515. TGF_beta_GS. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00467. GS. 1 hit.
[Graphical view]
PROSITEPS51256. GS. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTGFR1_RAT
AccessionPrimary (citable) accession number: P80204
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents