| IED ID | IndEnz0002010694 |
| Enzyme Type ID | protease010694 |
| Protein Name |
Thioredoxin, mitochondrial MTRX Mt-Trx Thioredoxin-2 |
| Gene Name | TXN2 TRX2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MAQRLLLRRFLASVISRKPSQGQWPPLTSRALQTPQCSPGGLTVTPNPARTIYTTRISLTTFNIQDGPDFQDRVVNSETPVVVDFHAQWCGPCKILGPRLEKMVAKQHGKVVMAKVDIDDHTDLAIEYEVSAVPTVLAMKNGDVVDKFVGIKDEDQLEAFLKKLIG |
| Enzyme Length | 166 |
| Uniprot Accession Number | Q99757 |
| Absorption | |
| Active Site | ACT_SITE 90; /note=Nucleophile; /evidence=ECO:0000250; ACT_SITE 93; /note=Nucleophile; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Important for the control of mitochondrial reactive oxygen species homeostasis, apoptosis regulation and cell viability. Possesses a dithiol-reducing activity. {ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052, ECO:0000269|PubMed:26626369}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Beta strand (5); Chain (1); Disulfide bond (1); Domain (1); Helix (4); Modified residue (2); Sequence conflict (2); Site (3); Transit peptide (1); Turn (3) |
| Keywords | 3D-structure;Acetylation;Direct protein sequencing;Disulfide bond;Electron transport;Mitochondrion;Neurodegeneration;Primary mitochondrial disease;Redox-active center;Reference proteome;Transit peptide;Transport |
| Interact With | Q9P2A4; Q6RW13; Q6RW13-2; Q8N2N9-4; P63010; P63010-2; O75934; Q6PI77; Q9H6J7-2; Q8NCU1; Q9BXL8; Q8NHQ1; Q9UFW8; Q9HD42; A0PJX0; Q8N4Y2-3; P32321; P35638; O95571; Q8IZU0; Q5TD97; A6NEM1; Q96D09; Q9BX10; Q96NT3-2; Q96CS2; Q9BT25; P42858; Q674X7-2; Q7Z3Y8; Q6A162; P80188; P43364-2; P43358; O15479; Q15555; Q9UPY8; Q99750; Q6FHY5; Q8TD10; Q9Y605; Q96HT8; Q5JR59; Q5JR59-3; P24844-2; Q96M63; P40855; P01189; Q96CD2; Q96T49; P61289; Q9UJ41; Q8IUH3; Q8IUH3-3; Q96HR9; Q96HR9-2; P49247; P21673; Q8IZE3; Q8IZE3-2; P02549; O43805; Q9H668; Q9UNE7; Q8N0S2; Q9UBB9; Q96CG3; Q9NZQ9; P19474; Q15654; Q5I0X7; Q9BRT2; Q8N1B4; O43829; Q9H0C1; Q6ZN96 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12032145, ECO:0000269|PubMed:12080052}. |
| Modified Residue | MOD_RES 152; /note=N6-acetyllysine; alternate; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 152; /note=N6-succinyllysine; alternate; /evidence=ECO:0000250|UniProtKB:P97493 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (3) |
| Cross Reference PDB | 1UVZ; 1W4V; 1W89; |
| Mapped Pubmed ID | 10514471; 10521424; 11518528; 12446202; 15046979; 15280035; 16424062; 16868544; 17220299; 17548047; 17601350; 17634480; 17707404; 17939155; 18497292; 18977241; 19124506; 19135121; 19165900; 19570036; 19885567; 20706999; 20819778; 20877624; 20929858; 21158569; 21327297; 21385867; 21557999; 21988832; 23485938; 23698001; 24295294; 24342608; 24735978; 24800864; 25416956; 26041303; 26763822; 28130258; 28356525; 28914755; 31915282; 32920833; 33763469; 34688818; 9923614; |
| Motif | |
| Gene Encoded By | |
| Mass | 18,383 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |