ID THIOM_MOUSE Reviewed; 166 AA. AC P97493; A2A440; Q545D5; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 11-JUN-2014, entry version 118. DE RecName: Full=Thioredoxin, mitochondrial; DE Short=MTRX; DE Short=Mt-Trx; DE AltName: Full=Thioredoxin-2; DE Flags: Precursor; GN Name=Txn2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Miranda-Vizuete A., Gustafsson J.-A., Spyrou G.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and DBA/2; TISSUE=Bone marrow, Kidney, and Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION. RX PubMed=12529397; DOI=10.1128/MCB.23.3.916-922.2003; RA Nonn L., Williams R.R., Erickson R.P., Powis G.; RT "The absence of mitochondrial thioredoxin 2 causes massive apoptosis, RT exencephaly, and early embryonic lethality in homozygous mice."; RL Mol. Cell. Biol. 23:916-922(2003). RN [6] RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- FUNCTION: Has an anti-apoptotic function and plays an important CC role in the regulation of mitochondrial membrane potential (By CC similarity). Possesses a dithiol-reducing activity. CC -!- SUBCELLULAR LOCATION: Mitochondrion. CC -!- SIMILARITY: Belongs to the thioredoxin family. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U85089; AAB41900.1; -; mRNA. DR EMBL; AK002358; BAB22037.1; -; mRNA. DR EMBL; AK010917; BAB27267.1; -; mRNA. DR EMBL; AK147164; BAE27729.1; -; mRNA. DR EMBL; AK149855; BAE29126.1; -; mRNA. DR EMBL; AK167754; BAE39789.1; -; mRNA. DR EMBL; AK167925; BAE39930.1; -; mRNA. DR EMBL; AK168322; BAE40261.1; -; mRNA. DR EMBL; AL583886; CAM23427.1; -; Genomic_DNA. DR EMBL; BC068182; AAH68182.1; -; mRNA. DR RefSeq; NP_064297.1; NM_019913.5. DR UniGene; Mm.291917; -. DR UniGene; Mm.462887; -. DR ProteinModelPortal; P97493; -. DR SMR; P97493; 60-166. DR IntAct; P97493; 1. DR MINT; MINT-4137662; -. DR STRING; 10090.ENSMUSP00000105370; -. DR PhosphoSite; P97493; -. DR MaxQB; P97493; -. DR PaxDb; P97493; -. DR PRIDE; P97493; -. DR Ensembl; ENSMUST00000005487; ENSMUSP00000005487; ENSMUSG00000005354. DR Ensembl; ENSMUST00000109748; ENSMUSP00000105370; ENSMUSG00000005354. DR GeneID; 56551; -. DR KEGG; mmu:56551; -. DR UCSC; uc007wof.1; mouse. DR CTD; 25828; -. DR MGI; MGI:1929468; Txn2. DR eggNOG; COG0526; -. DR GeneTree; ENSGT00530000064086; -. DR HOGENOM; HOG000292977; -. DR HOVERGEN; HBG009243; -. DR InParanoid; A2A440; -. DR KO; K03671; -. DR OMA; SFNVQDH; -. DR PhylomeDB; P97493; -. DR TreeFam; TF314517; -. DR ChiTaRS; TXN2; mouse. DR NextBio; 312931; -. DR PRO; PR:P97493; -. DR Bgee; P97493; -. DR CleanEx; MM_TXN2; -. DR Genevestigator; P97493; -. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:Ensembl. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR GO; GO:0048678; P:response to axon injury; IEA:Ensembl. DR GO; GO:0042493; P:response to drug; 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:0007584; P:response to nutrient; 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 Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR InterPro; IPR017937; Thioredoxin_CS. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR10438; PTHR10438; 1. 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 Acetylation; Complete proteome; Disulfide bond; Electron transport; KW Mitochondrion; Redox-active center; Reference proteome; KW Transit peptide; Transport. FT TRANSIT 1 59 Mitochondrion (By similarity). FT CHAIN 60 166 Thioredoxin, mitochondrial. FT /FTId=PRO_0000034151. FT DOMAIN 61 166 Thioredoxin. FT ACT_SITE 90 90 Nucleophile (By similarity). FT ACT_SITE 93 93 Nucleophile (By similarity). FT SITE 84 84 Deprotonates C-terminal active site Cys FT (By similarity). FT SITE 91 91 Contributes to redox potential value (By FT similarity). FT SITE 92 92 Contributes to redox potential value (By FT similarity). FT MOD_RES 152 152 N6-acetyllysine; alternate (By FT similarity). FT MOD_RES 152 152 N6-succinyllysine; alternate. FT DISULFID 90 93 Redox-active (By similarity). SQ SEQUENCE 166 AA; 18255 MW; C9A803DF571F3A7D CRC64; MAQRLLLGRF LTSVISRKPP QGVWASLTSK TLQTPQYNAG GLTVMPSPAR TVHTTRVCLT TFNVQDGPDF QDRVVNSETP VVVDFHAQWC GPCKILGPRL EKMVAKQHGK VVMAKVDIDD HTDLAIEYEV SAVPTVLAIK NGDVVDKFVG IKDEDQLEAF LKKLIG //