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   24-JAN-2024, entry version 179.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   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/2J; 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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., 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., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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 project:
RT   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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY MASS
RP   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., Zhang Y.,
RA   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: Important for the control of mitochondrial reactive oxygen
CC       species homeostasis, apoptosis regulation and cell viability. Possesses
CC       a dithiol-reducing activity. {ECO:0000250|UniProtKB:Q99757,
CC       ECO:0000269|PubMed:12529397}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC068182; AAH68182.1; -; mRNA.
DR   CCDS; CCDS27606.1; -.
DR   RefSeq; NP_064297.1; NM_019913.5.
DR   AlphaFoldDB; P97493; -.
DR   SMR; P97493; -.
DR   BioGRID; 208053; 6.
DR   IntAct; P97493; 168.
DR   STRING; 10090.ENSMUSP00000105370; -.
DR   iPTMnet; P97493; -.
DR   PhosphoSitePlus; P97493; -.
DR   SwissPalm; P97493; -.
DR   EPD; P97493; -.
DR   jPOST; P97493; -.
DR   MaxQB; P97493; -.
DR   PaxDb; 10090-ENSMUSP00000005487; -.
DR   PeptideAtlas; P97493; -.
DR   ProteomicsDB; 258873; -.
DR   Pumba; P97493; -.
DR   Antibodypedia; 232; 438 antibodies from 35 providers.
DR   DNASU; 56551; -.
DR   Ensembl; ENSMUST00000005487.12; ENSMUSP00000005487.6; ENSMUSG00000005354.17.
DR   Ensembl; ENSMUST00000109748.9; ENSMUSP00000105370.3; ENSMUSG00000005354.17.
DR   GeneID; 56551; -.
DR   KEGG; mmu:56551; -.
DR   UCSC; uc007wof.1; mouse.
DR   AGR; MGI:1929468; -.
DR   CTD; 25828; -.
DR   MGI; MGI:1929468; Txn2.
DR   VEuPathDB; HostDB:ENSMUSG00000005354; -.
DR   eggNOG; KOG0910; Eukaryota.
DR   GeneTree; ENSGT00530000064086; -.
DR   HOGENOM; CLU_090389_11_1_1; -.
DR   InParanoid; P97493; -.
DR   OMA; CKALMPR; -.
DR   OrthoDB; 45858at2759; -.
DR   PhylomeDB; P97493; -.
DR   TreeFam; TF314517; -.
DR   Reactome; R-MMU-1614558; Degradation of cysteine and homocysteine.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   BioGRID-ORCS; 56551; 18 hits in 79 CRISPR screens.
DR   ChiTaRS; Txn2; mouse.
DR   PRO; PR:P97493; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; P97493; Protein.
DR   Bgee; ENSMUSG00000005354; Expressed in right kidney and 268 other cell types or tissues.
DR   ExpressionAtlas; P97493; baseline and differential.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
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; ISO:MGI.
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   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR43601; THIOREDOXIN, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43601:SF3; THIOREDOXIN, MITOCHONDRIAL; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
DR   Genevisible; P97493; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Disulfide bond; Electron transport; Mitochondrion;
KW   Redox-active center; Reference proteome; Transit peptide; Transport.
FT   TRANSIT         1..59
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           60..166
FT                   /note="Thioredoxin, mitochondrial"
FT                   /id="PRO_0000034151"
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:0000250|UniProtKB:Q99757"
FT   MOD_RES         152
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   DISULFID        90..93
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
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
//