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   02-NOV-2016, entry version 140.
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/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.,
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/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
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   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
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: Important for the control of mitochondrial reactive
CC       oxygen species homeostasis, apoptosis regulation and cell
CC       viability. Possesses a dithiol-reducing activity.
CC       {ECO:0000250|UniProtKB:Q99757, ECO:0000269|PubMed:12529397}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00691}.
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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; CAM23427.1; -; Genomic_DNA.
DR   EMBL; BC068182; AAH68182.1; -; mRNA.
DR   CCDS; CCDS27606.1; -.
DR   RefSeq; NP_064297.1; NM_019913.5.
DR   UniGene; Mm.291917; -.
DR   UniGene; Mm.462887; -.
DR   ProteinModelPortal; P97493; -.
DR   SMR; P97493; -.
DR   IntAct; P97493; 1.
DR   MINT; MINT-4137662; -.
DR   STRING; 10090.ENSMUSP00000005487; -.
DR   iPTMnet; P97493; -.
DR   PhosphoSitePlus; P97493; -.
DR   EPD; P97493; -.
DR   MaxQB; P97493; -.
DR   PaxDb; P97493; -.
DR   PeptideAtlas; 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; KOG0910; Eukaryota.
DR   eggNOG; COG0526; LUCA.
DR   GeneTree; ENSGT00530000064086; -.
DR   HOGENOM; HOG000292977; -.
DR   HOVERGEN; HBG009243; -.
DR   InParanoid; P97493; -.
DR   KO; K03671; -.
DR   OMA; DYEVGSV; -.
DR   OrthoDB; EOG091G0UDG; -.
DR   PhylomeDB; P97493; -.
DR   TreeFam; TF314517; -.
DR   Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR   ChiTaRS; Txn2; mouse.
DR   PRO; PR:P97493; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000005354; -.
DR   CleanEx; MM_TXN2; -.
DR   ExpressionAtlas; P97493; baseline and differential.
DR   Genevisible; P97493; MM.
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; ISO:MGI.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central.
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:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central.
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:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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:0000103; P:sulfate assimilation; IBA:GO_Central.
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. {ECO:0000250}.
FT   CHAIN        60    166       Thioredoxin, mitochondrial.
FT                                /FTId=PRO_0000034151.
FT   DOMAIN       61    166       Thioredoxin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00691}.
FT   ACT_SITE     90     90       Nucleophile. {ECO:0000250}.
FT   ACT_SITE     93     93       Nucleophile. {ECO:0000250}.
FT   SITE         84     84       Deprotonates C-terminal active site Cys.
FT                                {ECO:0000250}.
FT   SITE         91     91       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   SITE         92     92       Contributes to redox potential value.
FT                                {ECO:0000250}.
FT   MOD_RES     152    152       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:Q99757}.
FT   MOD_RES     152    152       N6-succinyllysine; alternate.
FT                                {ECO:0000244|PubMed:23806337}.
FT   DISULFID     90     93       Redox-active. {ECO:0000255|PROSITE-
FT                                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
//