Reviewed,
UniProtKB/Swiss-Prot P80204 (TGFR1_RAT)
Last modified
June 16, 2009.
Version 89.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 501 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| 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
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 22 | 22 | Potential | ||||||||
| Chain | 23 – 501 | 479 | TGF-beta receptor type-1 | PRO_0000024425 | |||||||
Regions | |||||||||||
| Topological domain | 23 – 123 | 101 | Extracellular Potential | ||||||||
| Transmembrane | 124 – 146 | 23 | Potential | ||||||||
| Topological domain | 147 – 501 | 355 | Cytoplasmic Potential | ||||||||
| Domain | 173 – 202 | 30 | GS | ||||||||
| Domain | 203 – 493 | 291 | Protein kinase | ||||||||
| Nucleotide binding | 209 – 217 | 9 | ATP By similarity | ||||||||
Sites | |||||||||||
| Active site | 331 | 1 | Proton acceptor By similarity | ||||||||
| Binding site | 230 | 1 | ATP By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 183 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 184 | 1 | Phosphothreonine By similarity | ||||||||
| Modified residue | 185 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 187 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 189 | 1 | Phosphoserine By similarity | ||||||||
| Glycosylation | 41 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 32 ↔ 50 | By similarity | |||||||||
| Disulfide bond | 34 ↔ 37 | By similarity | |||||||||
| Disulfide bond | 44 ↔ 67 | By similarity | |||||||||
| Disulfide bond | 82 ↔ 94 | By similarity | |||||||||
| Disulfide bond | 95 ↔ 100 | By similarity | |||||||||
Sequences
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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. | |
| IPI | IPI00195461. |
| UniGene | Rn.44402 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1IAS based on UniProtKB P36897. |
| SMR | P80204. Positions 199-501. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOG00000007036. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 3852. Tgfbr1. |
Phylogenomic databases | |
| HOVERGEN | P80204. |
Enzyme and pathway databases | |
| BRENDA | 2.7.10.2. 248. 2.7.11.30. 248. |
Gene expression databases | |
| ArrayExpress | P80204. |
| GermOnline | ENSRNOG00000007036. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000472. 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] |
| Pfam | PF01064. Activin_recp. 1 hit. PF00069. Pkinase. 1 hit. PF08515. TGF_beta_GS. 1 hit. [Graphical view] |
| ProDom | PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00467. GS. 1 hit. [Graphical view] |
| PROSITE | PS51256. GS. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TGFR1_RAT | ||||||||
| Accession | Primary (citable) accession number: P80204 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

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