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P10639

- THIO_MOUSE

UniProt

P10639 - THIO_MOUSE

Protein

Thioredoxin

Gene

Txn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions By similarity. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity By similarity.By similarity
    ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei26 – 261Deprotonates C-terminal active site CysBy similarity
    Active sitei32 – 321NucleophileBy similarity
    Sitei33 – 331Contributes to redox potential valueBy similarity
    Sitei34 – 341Contributes to redox potential valueBy similarity
    Active sitei35 – 351NucleophileBy similarity

    GO - Molecular functioni

    1. peptide disulfide oxidoreductase activity Source: MGI
    2. protein binding Source: MGI
    3. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: MGI
    2. glycerol ether metabolic process Source: InterPro
    3. negative regulation of protein export from nucleus Source: MGI
    4. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    5. oxidation-reduction process Source: UniProtKB
    6. positive regulation of DNA binding Source: UniProtKB
    7. regulation of protein import into nucleus, translocation Source: UniProtKB
    8. response to radiation Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Electron transport, Transcription, Transcription regulation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_188970. Oxidative Stress Induced Senescence.
    REACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_198644. The NLRP3 inflammasome.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin
    Short name:
    Trx
    Alternative name(s):
    ATL-derived factor
    Short name:
    ADF
    Gene namesi
    Name:Txn
    Synonyms:Txn1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:98874. Txn1.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity. Secreted By similarity
    Note: Secreted by a leaderless secretory pathway. Predominantly in the cytoplasm in non irradiated cells. Radiation induces translocation of TRX from the cytoplasm to the nucleus By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. extracellular region Source: UniProtKB-SubCell
    4. mitochondrion Source: MGI
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 105104ThioredoxinPRO_0000120007Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6-acetyllysineBy similarity
    Modified residuei8 – 81N6-succinyllysine1 Publication
    Disulfide bondi32 ↔ 35Redox-activePROSITE-ProRule annotation
    Modified residuei39 – 391N6-acetyllysine1 Publication
    Modified residuei62 – 621S-nitrosocysteineBy similarity
    Modified residuei69 – 691S-nitrosocysteineBy similarity
    Modified residuei73 – 731S-nitrosocysteine; alternateBy similarity
    Disulfide bondi73 – 73Interchain; alternateBy similarity
    Modified residuei94 – 941N6-acetyllysine; alternate1 Publication
    Modified residuei94 – 941N6-succinyllysine; alternate1 Publication

    Post-translational modificationi

    In the fully reduced protein, both Cys-69 and Cys-73 are nitrosylated in response to nitric oxide (NO). When two disulfide bonds are present in the protein, only Cys-73 is nitrosylated. Cys-73 can serve as donor for nitrosylation of target proteins By similarity.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, S-nitrosylation

    Proteomic databases

    MaxQBiP10639.
    PaxDbiP10639.
    PRIDEiP10639.

    2D gel databases

    SWISS-2DPAGEP10639.
    UCD-2DPAGEP10639.

    PTM databases

    PhosphoSiteiP10639.

    Expressioni

    Gene expression databases

    BgeeiP10639.
    CleanExiMM_TXN1.
    GenevestigatoriP10639.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with TXNIP through the redox-active site. Interacts with MAP3K5 and CASP3. Interacts with APEX1; the interaction stimulates the FOS/JUN AP-1 DNA-binding activity in a redox-dependent manner By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204389. 3 interactions.
    IntActiP10639. 3 interactions.
    MINTiMINT-1868937.

    Structurei

    3D structure databases

    ProteinModelPortaliP10639.
    SMRiP10639. Positions 1-103.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 105104ThioredoxinPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the thioredoxin family.Curated
    Contains 1 thioredoxin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0526.
    GeneTreeiENSGT00530000063008.
    HOGENOMiHOG000292977.
    HOVERGENiHBG009243.
    InParanoidiP10639.
    KOiK03671.
    OMAiCKMISPH.
    OrthoDBiEOG7H4DX9.
    PhylomeDBiP10639.
    TreeFamiTF318932.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view]
    PANTHERiPTHR10438. PTHR10438. 1 hit.
    PfamiPF00085. Thioredoxin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000077. Thioredoxin. 1 hit.
    SUPFAMiSSF52833. SSF52833. 1 hit.
    PROSITEiPS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P10639-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS    50
    NVVFLEVDVD DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAS 100
    ITEYA 105
    Length:105
    Mass (Da):11,675
    Last modified:January 23, 2007 - v3
    Checksum:i3A2B925935F952DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001S → C in BAB25256. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77585 mRNA. Translation: CAA54688.1.
    D21859 Genomic DNA. Translation: BAA04881.1.
    AK007537 mRNA. Translation: BAB25096.1.
    AK007790 mRNA. Translation: BAB25256.1.
    BC010756 mRNA. Translation: AAH10756.1.
    BC094415 mRNA. Translation: AAH94415.1.
    CCDSiCCDS18207.1.
    PIRiJC4068. S04107.
    RefSeqiNP_035790.1. NM_011660.3.
    UniGeneiMm.260618.

    Genome annotation databases

    EnsembliENSMUST00000030051; ENSMUSP00000030051; ENSMUSG00000028367.
    GeneIDi22166.
    KEGGimmu:22166.
    UCSCiuc008syp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X77585 mRNA. Translation: CAA54688.1 .
    D21859 Genomic DNA. Translation: BAA04881.1 .
    AK007537 mRNA. Translation: BAB25096.1 .
    AK007790 mRNA. Translation: BAB25256.1 .
    BC010756 mRNA. Translation: AAH10756.1 .
    BC094415 mRNA. Translation: AAH94415.1 .
    CCDSi CCDS18207.1.
    PIRi JC4068. S04107.
    RefSeqi NP_035790.1. NM_011660.3.
    UniGenei Mm.260618.

    3D structure databases

    ProteinModelPortali P10639.
    SMRi P10639. Positions 1-103.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204389. 3 interactions.
    IntActi P10639. 3 interactions.
    MINTi MINT-1868937.

    PTM databases

    PhosphoSitei P10639.

    2D gel databases

    SWISS-2DPAGE P10639.
    UCD-2DPAGE P10639.

    Proteomic databases

    MaxQBi P10639.
    PaxDbi P10639.
    PRIDEi P10639.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030051 ; ENSMUSP00000030051 ; ENSMUSG00000028367 .
    GeneIDi 22166.
    KEGGi mmu:22166.
    UCSCi uc008syp.1. mouse.

    Organism-specific databases

    CTDi 22166.
    MGIi MGI:98874. Txn1.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00530000063008.
    HOGENOMi HOG000292977.
    HOVERGENi HBG009243.
    InParanoidi P10639.
    KOi K03671.
    OMAi CKMISPH.
    OrthoDBi EOG7H4DX9.
    PhylomeDBi P10639.
    TreeFami TF318932.

    Enzyme and pathway databases

    Reactomei REACT_188970. Oxidative Stress Induced Senescence.
    REACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_198644. The NLRP3 inflammasome.

    Miscellaneous databases

    NextBioi 302106.
    PROi P10639.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10639.
    CleanExi MM_TXN1.
    Genevestigatori P10639.

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR005746. Thioredoxin.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    PANTHERi PTHR10438. PTHR10438. 1 hit.
    Pfami PF00085. Thioredoxin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000077. Thioredoxin. 1 hit.
    SUPFAMi SSF52833. SSF52833. 1 hit.
    PROSITEi PS00194. THIOREDOXIN_1. 1 hit.
    PS51352. THIOREDOXIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ATL-derived factor (ADF), an IL-2 receptor/Tac inducer homologous to thioredoxin; possible involvement of dithiol-reduction in the IL-2 receptor induction."
      Tagaya Y., Maeda Y., Mitsui A., Kndo N., Matsui H., Hamuro J., Brown N., Arai K., Yokota T., Wakasugi H., Yodoi J.
      EMBO J. 8:757-764(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: SEQUENCE REVISION.
    3. "Structure of the mouse thioredoxin-encoding gene and its processed pseudogene."
      Matsui M., Taniguchi Y., Hirota K., Taketo M., Yodoi J.
      Gene 152:165-171(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
      Tissue: Liver.
    4. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pancreas.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Colon and Thymus.
    6. "Vitamin D3 up-regulated protein 1 mediates oxidative stress via suppressing the thioredoxin function."
      Junn E., Han S.H., Im J.Y., Yang Y., Cho E.W., Um H.D., Kim D.K., Lee K.W., Han P.L., Rhee S.G., Choi I.
      J. Immunol. 164:6287-6295(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXNIP.
    7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-39 AND LYS-94, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-8 AND LYS-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiTHIO_MOUSE
    AccessioniPrimary (citable) accession number: P10639
    Secondary accession number(s): Q52KC4, Q9D8R0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3