THIOM_HUMAN
ID THIOM_HUMAN Reviewed; 166 AA.
AC Q99757; Q5JZA0; Q6FH60; Q9UH29;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Thioredoxin, mitochondrial;
DE Short=MTRX;
DE Short=Mt-Trx;
DE AltName: Full=Thioredoxin-2;
DE Flags: Precursor;
GN Name=TXN2; Synonyms=TRX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Osteosarcoma;
RX PubMed=12032145; DOI=10.1074/jbc.m202026200;
RA Chen Y., Cai J., Murphy T.J., Jones D.P.;
RT "Overexpressed human mitochondrial thioredoxin confers resistance to
RT oxidant-induced apoptosis in human osteosarcoma cells.";
RL J. Biol. Chem. 277:33242-33248(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=12080052; DOI=10.1074/jbc.m203036200;
RA Damdimopoulos A.E., Miranda-Vizuete A., Pelto-Huikko M., Gustafsson J.-A.,
RA Spyrou G.;
RT "Human mitochondrial thioredoxin. Involvement in mitochondrial membrane
RT potential and cell death.";
RL J. Biol. Chem. 277:33249-33257(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RA Reddy P.G., Bhuyan D.K., Bhuyan K.C.;
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 60-74.
RC TISSUE=Leukemic T-cell;
RX PubMed=19892738; DOI=10.1073/pnas.0908958106;
RA Xu G., Shin S.B., Jaffrey S.R.;
RT "Global profiling of protease cleavage sites by chemoselective labeling of
RT protein N-termini.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER LEU-59, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP INVOLVEMENT IN COXPD29, AND FUNCTION.
RX PubMed=26626369; DOI=10.1093/brain/awv350;
RA Holzerova E., Danhauser K., Haack T.B., Kremer L.S., Melcher M., Ingold I.,
RA Kobayashi S., Terrile C., Wolf P., Schaper J., Mayatepek E., Baertling F.,
RA Friedmann Angeli J.P., Conrad M., Strom T.M., Meitinger T., Prokisch H.,
RA Distelmaier F.;
RT "Human thioredoxin 2 deficiency impairs mitochondrial redox homeostasis and
RT causes early-onset neurodegeneration.";
RL Brain 139:346-354(2016).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 60-166, AND SUBUNIT.
RX PubMed=16195549; DOI=10.1110/ps.051632905;
RA Smeets A., Evrard C., Landtmeters M., Marchand C., Knoops B.,
RA Declercq J.-P.;
RT "Crystal structures of oxidized and reduced forms of human mitochondrial
RT thioredoxin 2.";
RL Protein Sci. 14:2610-2621(2005).
CC -!- FUNCTION: Important for the control of mitochondrial reactive oxygen
CC species homeostasis, apoptosis regulation and cell viability. Possesses
CC a dithiol-reducing activity. {ECO:0000269|PubMed:12032145,
CC ECO:0000269|PubMed:12080052, ECO:0000269|PubMed:26626369}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16195549}.
CC -!- INTERACTION:
CC Q99757; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-2932492, EBI-742038;
CC Q99757; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-2932492, EBI-741181;
CC Q99757; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-2932492, EBI-11522760;
CC Q99757; Q8N2N9-4: ANKRD36B; NbExp=3; IntAct=EBI-2932492, EBI-12170453;
CC Q99757; P63010: AP2B1; NbExp=3; IntAct=EBI-2932492, EBI-432924;
CC Q99757; P63010-2: AP2B1; NbExp=3; IntAct=EBI-2932492, EBI-11529439;
CC Q99757; O75934: BCAS2; NbExp=3; IntAct=EBI-2932492, EBI-1050106;
CC Q99757; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-2932492, EBI-11519926;
CC Q99757; Q9H6J7-2: C11orf49; NbExp=3; IntAct=EBI-2932492, EBI-13328871;
CC Q99757; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-2932492, EBI-750686;
CC Q99757; Q9BXL8: CDCA4; NbExp=3; IntAct=EBI-2932492, EBI-1773949;
CC Q99757; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2932492, EBI-739624;
CC Q99757; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-2932492, EBI-723153;
CC Q99757; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-2932492, EBI-1057156;
CC Q99757; A0PJX0: CIB4; NbExp=3; IntAct=EBI-2932492, EBI-12868028;
CC Q99757; Q8N4Y2-3: CRACR2B; NbExp=3; IntAct=EBI-2932492, EBI-11982645;
CC Q99757; P32321: DCTD; NbExp=3; IntAct=EBI-2932492, EBI-739870;
CC Q99757; P35638: DDIT3; NbExp=3; IntAct=EBI-2932492, EBI-742651;
CC Q99757; O95571: ETHE1; NbExp=3; IntAct=EBI-2932492, EBI-715318;
CC Q99757; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-2932492, EBI-10175124;
CC Q99757; Q5TD97: FHL5; NbExp=3; IntAct=EBI-2932492, EBI-750641;
CC Q99757; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-2932492, EBI-5916454;
CC Q99757; Q96D09: GPRASP2; NbExp=4; IntAct=EBI-2932492, EBI-473189;
CC Q99757; Q9BX10: GTPBP2; NbExp=5; IntAct=EBI-2932492, EBI-6115579;
CC Q99757; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-2932492, EBI-11978177;
CC Q99757; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-2932492, EBI-2514791;
CC Q99757; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-2932492, EBI-2558143;
CC Q99757; P42858: HTT; NbExp=3; IntAct=EBI-2932492, EBI-466029;
CC Q99757; Q674X7-2: KAZN; NbExp=3; IntAct=EBI-2932492, EBI-12024294;
CC Q99757; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-2932492, EBI-3044087;
CC Q99757; Q6A162: KRT40; NbExp=3; IntAct=EBI-2932492, EBI-10171697;
CC Q99757; P80188: LCN2; NbExp=3; IntAct=EBI-2932492, EBI-11911016;
CC Q99757; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-2932492, EBI-10178634;
CC Q99757; P43358: MAGEA4; NbExp=3; IntAct=EBI-2932492, EBI-743122;
CC Q99757; O15479: MAGEB2; NbExp=3; IntAct=EBI-2932492, EBI-1057615;
CC Q99757; Q15555: MAPRE2; NbExp=6; IntAct=EBI-2932492, EBI-739717;
CC Q99757; Q9UPY8: MAPRE3; NbExp=6; IntAct=EBI-2932492, EBI-726739;
CC Q99757; Q99750: MDFI; NbExp=3; IntAct=EBI-2932492, EBI-724076;
CC Q99757; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2932492, EBI-16439278;
CC Q99757; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-2932492, EBI-2548751;
CC Q99757; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-2932492, EBI-995714;
CC Q99757; Q96HT8: MRFAP1L1; NbExp=6; IntAct=EBI-2932492, EBI-748896;
CC Q99757; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-2932492, EBI-742948;
CC Q99757; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-2932492, EBI-11522433;
CC Q99757; P24844-2: MYL9; NbExp=3; IntAct=EBI-2932492, EBI-13066228;
CC Q99757; Q96M63: ODAD1; NbExp=3; IntAct=EBI-2932492, EBI-10173858;
CC Q99757; P40855: PEX19; NbExp=3; IntAct=EBI-2932492, EBI-594747;
CC Q99757; P01189: POMC; NbExp=3; IntAct=EBI-2932492, EBI-12219503;
CC Q99757; Q96CD2: PPCDC; NbExp=6; IntAct=EBI-2932492, EBI-724333;
CC Q99757; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-2932492, EBI-10293968;
CC Q99757; P61289: PSME3; NbExp=3; IntAct=EBI-2932492, EBI-355546;
CC Q99757; Q9UJ41: RABGEF1; NbExp=3; IntAct=EBI-2932492, EBI-913954;
CC Q99757; Q8IUH3: RBM45; NbExp=3; IntAct=EBI-2932492, EBI-2512147;
CC Q99757; Q8IUH3-3: RBM45; NbExp=3; IntAct=EBI-2932492, EBI-10964453;
CC Q99757; Q96HR9: REEP6; NbExp=3; IntAct=EBI-2932492, EBI-750345;
CC Q99757; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-2932492, EBI-14065960;
CC Q99757; P49247: RPIA; NbExp=6; IntAct=EBI-2932492, EBI-744831;
CC Q99757; P21673: SAT1; NbExp=3; IntAct=EBI-2932492, EBI-711613;
CC Q99757; Q8IZE3: SCYL3; NbExp=4; IntAct=EBI-2932492, EBI-1380680;
CC Q99757; Q8IZE3-2: SCYL3; NbExp=3; IntAct=EBI-2932492, EBI-11959369;
CC Q99757; P02549: SPTA1; NbExp=3; IntAct=EBI-2932492, EBI-375617;
CC Q99757; O43805: SSNA1; NbExp=6; IntAct=EBI-2932492, EBI-2515299;
CC Q99757; Q9H668: STN1; NbExp=3; IntAct=EBI-2932492, EBI-746930;
CC Q99757; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-2932492, EBI-357085;
CC Q99757; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-2932492, EBI-6872807;
CC Q99757; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-2932492, EBI-1105213;
CC Q99757; Q96CG3: TIFA; NbExp=3; IntAct=EBI-2932492, EBI-740711;
CC Q99757; Q9NZQ9: TMOD4; NbExp=3; IntAct=EBI-2932492, EBI-9393504;
CC Q99757; P19474: TRIM21; NbExp=6; IntAct=EBI-2932492, EBI-81290;
CC Q99757; Q15654: TRIP6; NbExp=3; IntAct=EBI-2932492, EBI-742327;
CC Q99757; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-2932492, EBI-8636434;
CC Q99757; Q9BRT2: UQCC2; NbExp=3; IntAct=EBI-2932492, EBI-1054584;
CC Q99757; Q8N1B4: VPS52; NbExp=6; IntAct=EBI-2932492, EBI-2799833;
CC Q99757; O43829: ZBTB14; NbExp=3; IntAct=EBI-2932492, EBI-10176632;
CC Q99757; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2932492, EBI-12030590;
CC Q99757; Q6ZN96; NbExp=3; IntAct=EBI-2932492, EBI-10255097;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:12032145,
CC ECO:0000269|PubMed:12080052}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult (at protein level) and
CC fetal tissues. {ECO:0000269|PubMed:12032145,
CC ECO:0000269|PubMed:12080052}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 29 (COXPD29)
CC [MIM:616811]: An autosomal recessive, infantile-onset,
CC neurodegenerative disorder characterized by decreased activities of
CC mitochondrial respiratory complexes I and III, severe cerebellar
CC atrophy, epilepsy, dystonia, optic atrophy, and peripheral neuropathy.
CC {ECO:0000269|PubMed:26626369}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; AF480262; AAN05576.1; -; mRNA.
DR EMBL; U78678; AAB41631.1; -; mRNA.
DR EMBL; AF276920; AAF86467.1; -; mRNA.
DR EMBL; CR456601; CAG30487.1; -; mRNA.
DR EMBL; CR541896; CAG46694.1; -; mRNA.
DR EMBL; CR541917; CAG46715.1; -; mRNA.
DR EMBL; AL022313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW60103.1; -; Genomic_DNA.
DR EMBL; BC013726; AAH13726.1; -; mRNA.
DR EMBL; BC050610; AAH50610.1; -; mRNA.
DR CCDS; CCDS13928.1; -.
DR RefSeq; NP_036605.2; NM_012473.3.
DR RefSeq; XP_006724289.1; XM_006724226.1.
DR PDB; 1UVZ; X-ray; 2.01 A; A/B/C/D/E/F=60-166.
DR PDB; 1W4V; X-ray; 1.80 A; A/B/C/D/E/F=60-166.
DR PDB; 1W89; X-ray; 2.00 A; A/B/C/D/E/F=60-166.
DR PDBsum; 1UVZ; -.
DR PDBsum; 1W4V; -.
DR PDBsum; 1W89; -.
DR AlphaFoldDB; Q99757; -.
DR SMR; Q99757; -.
DR BioGRID; 117356; 145.
DR IntAct; Q99757; 98.
DR STRING; 9606.ENSP00000216185; -.
DR BindingDB; Q99757; -.
DR ChEMBL; CHEMBL2189153; -.
DR iPTMnet; Q99757; -.
DR PhosphoSitePlus; Q99757; -.
DR BioMuta; TXN2; -.
DR DMDM; 20455529; -.
DR EPD; Q99757; -.
DR jPOST; Q99757; -.
DR MassIVE; Q99757; -.
DR MaxQB; Q99757; -.
DR PaxDb; Q99757; -.
DR PeptideAtlas; Q99757; -.
DR PRIDE; Q99757; -.
DR ProteomicsDB; 78462; -.
DR TopDownProteomics; Q99757; -.
DR Antibodypedia; 232; 395 antibodies from 35 providers.
DR DNASU; 25828; -.
DR Ensembl; ENST00000216185.7; ENSP00000216185.2; ENSG00000100348.10.
DR Ensembl; ENST00000403313.5; ENSP00000385393.1; ENSG00000100348.10.
DR GeneID; 25828; -.
DR KEGG; hsa:25828; -.
DR MANE-Select; ENST00000216185.7; ENSP00000216185.2; NM_012473.4; NP_036605.2.
DR UCSC; uc003apk.2; human.
DR CTD; 25828; -.
DR DisGeNET; 25828; -.
DR GeneCards; TXN2; -.
DR HGNC; HGNC:17772; TXN2.
DR HPA; ENSG00000100348; Low tissue specificity.
DR MalaCards; TXN2; -.
DR MIM; 609063; gene.
DR MIM; 616811; phenotype.
DR neXtProt; NX_Q99757; -.
DR OpenTargets; ENSG00000100348; -.
DR Orphanet; 478029; Combined oxidative phosphorylation defect type 29.
DR PharmGKB; PA38245; -.
DR VEuPathDB; HostDB:ENSG00000100348; -.
DR eggNOG; KOG0910; Eukaryota.
DR GeneTree; ENSGT00530000064086; -.
DR HOGENOM; CLU_090389_11_1_1; -.
DR InParanoid; Q99757; -.
DR OMA; CTPCKAL; -.
DR PhylomeDB; Q99757; -.
DR TreeFam; TF314517; -.
DR PathwayCommons; Q99757; -.
DR Reactome; R-HSA-1614558; Degradation of cysteine and homocysteine.
DR Reactome; R-HSA-3299685; Detoxification of Reactive Oxygen Species.
DR SignaLink; Q99757; -.
DR SIGNOR; Q99757; -.
DR BioGRID-ORCS; 25828; 78 hits in 1081 CRISPR screens.
DR ChiTaRS; TXN2; human.
DR EvolutionaryTrace; Q99757; -.
DR GeneWiki; TXN2; -.
DR GenomeRNAi; 25828; -.
DR Pharos; Q99757; Tbio.
DR PRO; PR:Q99757; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q99757; protein.
DR Bgee; ENSG00000100348; Expressed in right adrenal gland and 210 other tissues.
DR ExpressionAtlas; Q99757; baseline and differential.
DR Genevisible; Q99757; HS.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:Ensembl.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0009725; P:response to hormone; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR InterPro; IPR005746; Thioredoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR01068; thioredoxin; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Disulfide bond;
KW Electron transport; Mitochondrion; Neurodegeneration;
KW Primary mitochondrial disease; Redox-active center; Reference proteome;
KW Transit peptide; Transport.
FT TRANSIT 1..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:19892738,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 60..166
FT /note="Thioredoxin, mitochondrial"
FT /id="PRO_0000034150"
FT DOMAIN 61..166
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 90
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 84
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 91
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 92
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 152
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 152
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P97493"
FT DISULFID 90..93
FT /note="Redox-active"
FT CONFLICT 30
FT /note="R -> K (in Ref. 2; AAB41631 and 3; AAF86467)"
FT /evidence="ECO:0000305"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1W4V"
FT HELIX 67..73
FT /evidence="ECO:0007829|PDB:1W4V"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:1W4V"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1W4V"
FT HELIX 91..106
FT /evidence="ECO:0007829|PDB:1W4V"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1W4V"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1W4V"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:1W4V"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1W4V"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:1W4V"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:1W4V"
FT HELIX 154..165
FT /evidence="ECO:0007829|PDB:1W4V"
SQ SEQUENCE 166 AA; 18383 MW; C4CA8CDAD485D499 CRC64;
MAQRLLLRRF LASVISRKPS QGQWPPLTSR ALQTPQCSPG GLTVTPNPAR TIYTTRISLT
TFNIQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKMVAKQHGK VVMAKVDIDD
HTDLAIEYEV SAVPTVLAMK NGDVVDKFVG IKDEDQLEAF LKKLIG
