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   16-OCT-2013, entry version 110.
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).
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.
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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   IPI; IPI00125652; -.
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   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; RWAPLTS; -.
DR   OrthoDB; EOG4V9TS4; -.
DR   ChiTaRS; TXN2; mouse.
DR   NextBio; 312931; -.
DR   PRO; PR:P97493; -.
DR   ArrayExpress; 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:0009055; F:electron carrier activity; IEA:InterPro.
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 stimulus; IEA:Ensembl.
DR   GO; GO:0009725; P:response to hormone stimulus; 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   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   TIGRFAMs; TIGR01068; thioredoxin; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript 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 (By similarity).
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
//