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P11232

- THIO_RAT

UniProt

P11232 - THIO_RAT

Protein

Thioredoxin

Gene

Txn

Organism
Rattus norvegicus (Rat)
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

    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. enzyme binding Source: RGD
    2. protein disulfide oxidoreductase activity Source: InterPro
    3. thioredoxin-disulfide reductase activity Source: RGD

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. cellular response to antibiotic Source: RGD
    3. cellular response to drug Source: RGD
    4. cellular response to glucose stimulus Source: RGD
    5. cellular response to hyperoxia Source: RGD
    6. glycerol ether metabolic process Source: InterPro
    7. oxidation-reduction process Source: UniProtKB
    8. positive regulation of DNA binding Source: UniProtKB
    9. regulation of protein import into nucleus, translocation Source: UniProtKB
    10. regulation of transcription, DNA-templated Source: UniProtKB-KW
    11. response to activity Source: RGD
    12. response to axon injury Source: RGD
    13. response to dexamethasone Source: RGD
    14. response to drug Source: RGD
    15. response to radiation Source: UniProtKB
    16. response to selenium ion Source: RGD
    17. response to thyroxine Source: RGD
    18. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Electron transport, Transcription, Transcription regulation, Transport

    Enzyme and pathway databases

    ReactomeiREACT_196450. The NLRP3 inflammasome.
    REACT_203770. Oxidative Stress Induced Senescence.
    REACT_213899. Detoxification of Reactive Oxygen Species.
    REACT_215006. Synthesis and interconversion of nucleotide di- and triphosphates.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin
    Short name:
    Trx
    Gene namesi
    Name:Txn
    Synonyms:Txn1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi621157. 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. axon Source: RGD
    2. cytoplasm Source: RGD
    3. cytosol Source: RGD
    4. dendrite Source: RGD
    5. extracellular region Source: UniProtKB-SubCell
    6. neuronal cell body Source: RGD
    7. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 105104ThioredoxinPRO_0000120011Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3 – 31N6-acetyllysineBy similarity
    Modified residuei8 – 81N6-succinyllysineBy similarity
    Disulfide bondi32 ↔ 35Redox-activePROSITE-ProRule annotation
    Modified residuei39 – 391N6-acetyllysineBy similarity
    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; alternateBy similarity
    Modified residuei94 – 941N6-succinyllysine; alternateBy similarity

    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

    PaxDbiP11232.
    PRIDEiP11232.

    Expressioni

    Gene expression databases

    GenevestigatoriP11232.

    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

    BioGridi250461. 1 interaction.
    IntActiP11232. 2 interactions.
    MINTiMINT-4571509.
    STRINGi10116.ENSRNOP00000016447.

    Structurei

    3D structure databases

    ProteinModelPortaliP11232.
    SMRiP11232. Positions 1-104.
    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.
    HOGENOMiHOG000292977.
    HOVERGENiHBG009243.
    InParanoidiP11232.
    KOiK03671.
    OrthoDBiEOG7H4DX9.
    PhylomeDBiP11232.
    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.

    P11232-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKLIESKEA FQEALAAAGD KLVVVDFSAT WCGPCKMIKP FFHSLCDKYS    50
    NVVFLEVDVD DCQDVAADCE VKCMPTFQFY KKGQKVGEFS GANKEKLEAT 100
    ITEFA 105
    Length:105
    Mass (Da):11,673
    Last modified:January 23, 2007 - v2
    Checksum:i3A39025935FD42DA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14878 mRNA. Translation: CAA33019.1.
    AF311055 mRNA. Translation: AAG49923.1.
    BC058454 mRNA. Translation: AAH58454.1.
    PIRiS04352.
    RefSeqiNP_446252.1. NM_053800.3.
    UniGeneiRn.29777.

    Genome annotation databases

    GeneIDi116484.
    KEGGirno:116484.
    UCSCiRGD:621157. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14878 mRNA. Translation: CAA33019.1 .
    AF311055 mRNA. Translation: AAG49923.1 .
    BC058454 mRNA. Translation: AAH58454.1 .
    PIRi S04352.
    RefSeqi NP_446252.1. NM_053800.3.
    UniGenei Rn.29777.

    3D structure databases

    ProteinModelPortali P11232.
    SMRi P11232. Positions 1-104.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 250461. 1 interaction.
    IntActi P11232. 2 interactions.
    MINTi MINT-4571509.
    STRINGi 10116.ENSRNOP00000016447.

    Proteomic databases

    PaxDbi P11232.
    PRIDEi P11232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 116484.
    KEGGi rno:116484.
    UCSCi RGD:621157. rat.

    Organism-specific databases

    CTDi 22166.
    RGDi 621157. Txn1.

    Phylogenomic databases

    eggNOGi COG0526.
    HOGENOMi HOG000292977.
    HOVERGENi HBG009243.
    InParanoidi P11232.
    KOi K03671.
    OrthoDBi EOG7H4DX9.
    PhylomeDBi P11232.
    TreeFami TF318932.

    Enzyme and pathway databases

    Reactomei REACT_196450. The NLRP3 inflammasome.
    REACT_203770. Oxidative Stress Induced Senescence.
    REACT_213899. Detoxification of Reactive Oxygen Species.
    REACT_215006. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    NextBioi 619063.
    PROi P11232.

    Gene expression databases

    Genevestigatori P11232.

    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. "Nucleotide sequence of a cDNA encoding rat thioredoxin."
      Tonissen K.F., Robins A.J., Wells J.R.E.
      Nucleic Acids Res. 17:3973-3973(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. Xie Z.H., Liu C.Z., He Y.H., Wang A.M., Ma C.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "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].
      Tissue: Pituitary.
    4. "Characterization of a thioredoxin-related surface protein."
      Dean M.F., Martin H., Sansom P.A.
      Biochem. J. 304:861-867(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21.
      Tissue: Glial cell.
    5. Lubec G., Diao W., Kang S.U., Lubec S.
      Submitted (SEP-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 9-21; 73-81 AND 86-94, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Hippocampus.

    Entry informationi

    Entry nameiTHIO_RAT
    AccessioniPrimary (citable) accession number: P11232
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3