THIOM_MOUSE
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 03-AUG-2022, entry version 171.
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, Pancreas,
RC 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; 5.
DR IntAct; P97493; 168.
DR STRING; 10090.ENSMUSP00000005487; -.
DR iPTMnet; P97493; -.
DR PhosphoSitePlus; P97493; -.
DR EPD; P97493; -.
DR jPOST; P97493; -.
DR MaxQB; P97493; -.
DR PaxDb; P97493; -.
DR PeptideAtlas; P97493; -.
DR PRIDE; P97493; -.
DR ProteomicsDB; 258873; -.
DR Antibodypedia; 232; 395 antibodies from 35 providers.
DR DNASU; 56551; -.
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 VEuPathDB; HostDB:ENSMUSG00000005354; -.
DR eggNOG; KOG0910; Eukaryota.
DR GeneTree; ENSGT00530000064086; -.
DR HOGENOM; CLU_090389_11_1_1; -.
DR InParanoid; P97493; -.
DR OMA; CTPCKAL; -.
DR OrthoDB; 1482186at2759; -.
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 74 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 265 other tissues.
DR ExpressionAtlas; P97493; baseline and differential.
DR Genevisible; P97493; MM.
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; ISO:MGI.
DR GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; ISO:MGI.
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 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
