THIO_MOUSE
ID THIO_MOUSE Reviewed; 105 AA.
AC P10639; Q52KC4; Q9D8R0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Thioredoxin;
DE Short=Trx;
DE AltName: Full=ATL-derived factor;
DE Short=ADF;
GN Name=Txn; Synonyms=Txn1;
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].
RX PubMed=2785919; DOI=10.1002/j.1460-2075.1989.tb03436.x;
RA Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N.,
RA Arai K., Yokota T., Wakasugi H., Yodoi J.;
RT "ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to
RT thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor
RT induction.";
RL EMBO J. 8:757-764(1989).
RN [2]
RP ERRATUM OF PUBMED:2785919, AND SEQUENCE REVISION.
RX PubMed=8187776; DOI=10.1002/j.1460-2075.1994.tb06502.x;
RA Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N.,
RA Arai K., Yokota T., Wakasugi H., Yodoi J.;
RL EMBO J. 13:2244-2244(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=7835695; DOI=10.1016/0378-1119(94)00707-y;
RA Matsui M., Taniguchi Y., Hirota K., Taketo M., Yodoi J.;
RT "Structure of the mouse thioredoxin-encoding gene and its processed
RT pseudogene.";
RL Gene 152:165-171(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Colon, and Thymus;
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 [6]
RP INTERACTION WITH TXNIP.
RX PubMed=10843682; DOI=10.4049/jimmunol.164.12.6287;
RA Junn E., Han S.H., Im J.Y., Yang Y., Cho E.W., Um H.D., Kim D.K., Lee K.W.,
RA Han P.L., Rhee S.G., Choi I.;
RT "Vitamin D3 up-regulated protein 1 mediates oxidative stress via
RT suppressing the thioredoxin function.";
RL J. Immunol. 164:6287-6295(2000).
RN [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39 AND LYS-94, SUCCINYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-94, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and 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: Participates in various redox reactions through the
CC reversible oxidation of its active center dithiol to a disulfide and
CC catalyzes dithiol-disulfide exchange reactions (By similarity). Plays a
CC role in the reversible S-nitrosylation of cysteine residues in target
CC proteins, and thereby contributes to the response to intracellular
CC nitric oxide. Nitrosylates the active site Cys of CASP3 in response to
CC nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the
CC FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells
CC through its oxidation/reduction status and stimulates AP-1
CC transcriptional activity (By similarity). {ECO:0000250}.
CC -!- FUNCTION: ADF augments the expression of the interleukin-2 receptor TAC
CC (IL2R/P55).
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with TXNIP through the
CC redox-active site. Interacts with MAP3K5 and CASP3. Interacts with
CC APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity
CC in a redox-dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10599}. Cytoplasm
CC {ECO:0000250|UniProtKB:P10599}. Secreted
CC {ECO:0000250|UniProtKB:P10599}. Note=Translocates from the cytoplasm
CC into the nucleus after phorbol 12-myristate 13-acetate induction (PMA).
CC Predominantly in the cytoplasm in non irradiated cells. Radiation
CC induces translocation of TRX from the cytoplasm to the nucleus.
CC Secreted by a leaderless secretory pathway.
CC {ECO:0000250|UniProtKB:P10599}.
CC -!- PTM: In the fully reduced protein, both Cys-69 and Cys-73 are
CC nitrosylated in response to nitric oxide (NO). When two disulfide bonds
CC are present in the protein, only Cys-73 is nitrosylated. Cys-73 can
CC serve as donor for nitrosylation of target proteins (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the thioredoxin family. {ECO:0000305}.
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DR EMBL; X77585; CAA54688.1; -; mRNA.
DR EMBL; D21859; BAA04881.1; -; Genomic_DNA.
DR EMBL; AK007537; BAB25096.1; -; mRNA.
DR EMBL; AK007790; BAB25256.1; -; mRNA.
DR EMBL; BC010756; AAH10756.1; -; mRNA.
DR EMBL; BC094415; AAH94415.1; -; mRNA.
DR CCDS; CCDS18207.1; -.
DR PIR; JC4068; S04107.
DR RefSeq; NP_035790.1; NM_011660.3.
DR AlphaFoldDB; P10639; -.
DR SMR; P10639; -.
DR BioGRID; 204389; 33.
DR IntAct; P10639; 3.
DR MINT; P10639; -.
DR STRING; 10090.ENSMUSP00000030051; -.
DR iPTMnet; P10639; -.
DR PhosphoSitePlus; P10639; -.
DR SwissPalm; P10639; -.
DR SWISS-2DPAGE; P10639; -.
DR UCD-2DPAGE; P10639; -.
DR CPTAC; non-CPTAC-3884; -.
DR EPD; P10639; -.
DR jPOST; P10639; -.
DR MaxQB; P10639; -.
DR PaxDb; P10639; -.
DR PeptideAtlas; P10639; -.
DR PRIDE; P10639; -.
DR ProteomicsDB; 262978; -.
DR TopDownProteomics; P10639; -.
DR Antibodypedia; 3281; 846 antibodies from 39 providers.
DR DNASU; 22166; -.
DR Ensembl; ENSMUST00000030051; ENSMUSP00000030051; ENSMUSG00000028367.
DR GeneID; 22166; -.
DR KEGG; mmu:22166; -.
DR UCSC; uc008syp.1; mouse.
DR CTD; 22166; -.
DR MGI; MGI:98874; Txn1.
DR VEuPathDB; HostDB:ENSMUSG00000028367; -.
DR eggNOG; KOG0907; Eukaryota.
DR GeneTree; ENSGT00940000154259; -.
DR HOGENOM; CLU_090389_14_6_1; -.
DR InParanoid; P10639; -.
DR OMA; QVGVAPK; -.
DR OrthoDB; 1482186at2759; -.
DR PhylomeDB; P10639; -.
DR TreeFam; TF318932; -.
DR Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-499943; Interconversion of nucleotide di- and triphosphates.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-5676934; Protein repair.
DR Reactome; R-MMU-844456; The NLRP3 inflammasome.
DR BioGRID-ORCS; 22166; 27 hits in 74 CRISPR screens.
DR ChiTaRS; Txn1; mouse.
DR PRO; PR:P10639; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P10639; protein.
DR Bgee; ENSMUSG00000028367; Expressed in jejunum and 68 other tissues.
DR Genevisible; P10639; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0047134; F:protein-disulfide reductase (NAD(P)) activity; ISO:MGI.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IDA:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IDA:MGI.
DR GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; ISO:MGI.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:2000170; P:positive regulation of peptidyl-cysteine S-nitrosylation; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0071731; P:response to nitric oxide; ISO:MGI.
DR GO; GO:0009314; P:response to radiation; ISS:UniProtKB.
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 PIRSF; PIRSF000077; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Disulfide bond; Electron transport;
KW Nucleus; Redox-active center; Reference proteome; S-nitrosylation;
KW Secreted; Transcription; Transcription regulation; Transport.
FT CHAIN 1..105
FT /note="Thioredoxin"
FT /id="PRO_0000120007"
FT DOMAIN 2..105
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 32
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 35
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT SITE 26
FT /note="Deprotonates C-terminal active site Cys"
FT /evidence="ECO:0000250"
FT SITE 33
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT SITE 34
FT /note="Contributes to redox potential value"
FT /evidence="ECO:0000250"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 8
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 39
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 62
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 69
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 73
FT /note="S-nitrosocysteine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P10599"
FT MOD_RES 94
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 94
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT DISULFID 32..35
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT DISULFID 73
FT /note="Interchain; alternate"
FT /evidence="ECO:0000250"
FT CONFLICT 100
FT /note="S -> C (in Ref. 4; BAB25256)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 105 AA; 11675 MW; 3A2B925935F952DA CRC64;
MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS NVVFLEVDVD
DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAS ITEYA
