Q9N2I8 (TRXR2_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 85.
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 2, mitochondrial EC=1.8.1.9 Alternative name(s): Thioredoxin reductase TR3 | ||||
| Gene names |
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| 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 | 511 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 | Maintains thioredoxin in a reduced state. Implicated in the defenses against oxidative stress. May play a role in redox-regulated cell signaling. Ref.1 |
| Catalytic activity | Thioredoxin + NADP+ = thioredoxin disulfide + NADPH. |
| Cofactor | FAD. Ref.1 |
| Enzyme regulation | Inhibited by 1-chloro-2,4-dinitrobenzene and by zinc, calcium, magnesium and Fe2+ ions. Ref.1 |
| Subunit structure | Homodimer. Ref.1 |
| Subcellular location | |
| Miscellaneous | The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity. UniProtKB Q9Z0J5 |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Mitochondrion |
| Coding sequence diversity | Selenocysteine |
| Domain | Redox-active center Transit peptide |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Disulfide bond |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro response to oxygen radicalTraceable author statement Ref.1. Source: UniProtKB |
| Cellular component | mitochondrion Inferred from direct assay Ref.1. Source: UniProtKB |
| Molecular function | NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activityInferred from direct assay Ref.1. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 21 | 21 | Mitochondrion Ref.1 | ||||||||
| Chain | 22 – 511 | 490 | Thioredoxin reductase 2, mitochondrial Ref.1 | PRO_0000030287 | |||||||
Regions | |||||||||||
| Nucleotide binding | 29 – 58 | 30 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 484 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Non-standard residue | 510 | 1 | Selenocysteine | ||||||||
| Modified residue | 140 | 1 | N6-acetyllysine By similarity | ||||||||
| Disulfide bond | 74 ↔ 79 | Redox-active By similarity UniProtKB P00390 | |||||||||
| Cross-link | 509 ↔ 510 | Cysteinyl-selenocysteine (Cys-Sec) By similarity | |||||||||
Sequences
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References
| [1] | "Mitochondrial thioredoxin reductase in bovine adrenal cortex. Its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine." Watabe S., Makino Y., Ogawa K., Hiroi T., Yamamoto Y., Takahashi S.Y. Eur. J. Biochem. 264:74-84(1999) [PubMed: 10447675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-35; 53-82; 160-181; 208-238; 292-316; 328-340; 420-436; 470-488 AND 499-510, SELENOCYSTEINE AT SEC-510, FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION. Tissue: Adrenal cortex. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB022283 mRNA. Translation: BAA82153.1. |
| IPI | IPI00690111. |
| RefSeq | NP_777051.1. NM_174626.2. |
| UniGene | Bt.4008. |
3D structure databases | |
| ProteinModelPortal | Q9N2I8. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q9N2I8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 282389. |
| KEGG | bta:282389. |
Organism-specific databases | |
| CTD | 10587. |
Phylogenomic databases | |
| eggNOG | maNOG16321. |
| HOVERGEN | HBG004959. |
| InParanoid | Q9N2I8. |
| OrthoDB | EOG408N7T. |
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 | TRXR2_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q9N2I8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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