O62768 (TRXR1_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Thioredoxin reductase 1, cytoplasmic Short name=TR EC=1.8.1.9 Alternative name(s): Thioredoxin reductase TR1 | ||
| Gene names |
| ||
| Organism | Bos taurus (Bovine) | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Protein attributes
| Sequence length | 499 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Coding sequence diversity | Selenocysteine |
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Disulfide bond Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 499 | 499 | Thioredoxin reductase 1, cytoplasmic | PRO_0000067981 | |||||||
Regions | |||||||||||
| Nucleotide binding | 42 – 59 | 18 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 472 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Non-standard residue | 498 | 1 | Selenocysteine | ||||||||
| Modified residue | 11 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 13 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 131 | 1 | Phosphotyrosine By similarity | ||||||||
| Modified residue | 255 | 1 | N6-acetyllysine By similarity | ||||||||
| Modified residue | 422 | 1 | Phosphotyrosine By similarity | ||||||||
| Disulfide bond | 59 ↔ 64 | Redox-active By similarity | |||||||||
| Cross-link | 497 ↔ 498 | Cysteinyl-selenocysteine (Cys-Sec) By similarity | |||||||||
Sequences
| ||||||||||||||||||
References
| [1] | Terashima H. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Small intestine. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF053984 mRNA. Translation: AAC13914.1. |
| IPI | IPI00685161. |
| RefSeq | NP_777050.1. NM_174625.3. |
| UniGene | Bt.5534. |
3D structure databases | |
| ProteinModelPortal | O62768. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | O62768. |
Proteomic databases | |
| PRIDE | O62768. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 282388. |
| KEGG | bta:282388. |
Organism-specific databases | |
| CTD | 7296. |
Phylogenomic databases | |
| eggNOG | maNOG06865. |
| HOVERGEN | HBG004959. |
| InParanoid | O62768. |
| OrthoDB | EOG4H463K. |
| PhylomeDB | O62768. |
Family and domain databases | |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. IPR006338. Thioredoxin/glutathione_Rdtase. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| KO | K00384. |
| PANTHER | PTHR22912:SF23. Reduct_Se. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| TIGRFAMs | TIGR01438. TGR. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TRXR1_BOVIN | ||||||||
| Accession | Primary (citable) accession number: O62768 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with