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Q9JMH6

- TRXR1_MOUSE

UniProt

Q9JMH6 - TRXR1_MOUSE

Protein

Thioredoxin reductase 1, cytoplasmic

Gene

Txnrd1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 3 (26 Feb 2008)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei586 – 5861Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi156 – 17318FADBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. NADP binding Source: InterPro
    3. thioredoxin-disulfide reductase activity Source: MGI

    GO - Biological processi

    1. cell proliferation Source: MGI
    2. cell redox homeostasis Source: InterPro
    3. gastrulation Source: MGI
    4. mesoderm formation Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BRENDAi1.8.1.9. 3474.
    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_198602. PPARA activates gene expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thioredoxin reductase 1, cytoplasmic (EC:1.8.1.9)
    Short name:
    TR
    Alternative name(s):
    Thioredoxin reductase TR1
    Gene namesi
    Name:Txnrd1
    Synonyms:Trxr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:1354175. Txnrd1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytosol Source: MGI
    3. mitochondrion Source: MGI
    4. nucleolus Source: Ensembl
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 613613Thioredoxin reductase 1, cytoplasmicPRO_0000067982Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi173 ↔ 178Redox-activeBy similarity
    Modified residuei182 – 1821N6-succinyllysine1 Publication
    Modified residuei245 – 2451Phosphotyrosine1 Publication
    Cross-linki611 ↔ 612Cysteinyl-selenocysteine (Cys-Sec)By similarity

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ9JMH6.
    PaxDbiQ9JMH6.
    PRIDEiQ9JMH6.

    2D gel databases

    REPRODUCTION-2DPAGEQ9JMH6.

    PTM databases

    PhosphoSiteiQ9JMH6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9JMH6.
    BgeeiQ9JMH6.
    CleanExiMM_TXNRD1.
    GenevestigatoriQ9JMH6.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiQ9JMH6. 3 interactions.
    MINTiMINT-1869051.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JMH6.
    SMRiQ9JMH6. Positions 124-611.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi26 – 9065Pro-richAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    GeneTreeiENSGT00390000007578.
    HOGENOMiHOG000276712.
    HOVERGENiHBG004959.
    InParanoidiQ9JMH6.
    KOiK00384.
    OMAiVCAEIFT.
    OrthoDBiEOG779NXG.
    PhylomeDBiQ9JMH6.
    TreeFamiTF314782.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01438. TGR. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9JMH6-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPVDDCWLYF PASRGRTFVQ TVWVAPTCPN CCWFPGFLPP VPRPPHVPRV    50
    LLRGPRGAVL PASRPSKTLP SSSQTPCPTD PCICPPPSTP DSRQEKNTQS 100
    ELPNKKGQLQ KLPTMNGSKD PPGSYDFDLI IIGGGSGGLA AAKEAAKFDK 150
    KVLVLDFVTP TPLGTRWGLG GTCVNVGCIP KKLMHQAALL GQALKDSRNY 200
    GWKVEDTVKH DWEKMTESVQ SHIGSLNWGY RVALREKKVV YENAYGRFIG 250
    PHRIVATNNK GKEKIYSAER FLIATGERPR YLGIPGDKEY CISSDDLFSL 300
    PYCPGKTLVV GASYVALECA GFLAGIGLDV TVMVRSILLR GFDQDMANKI 350
    GEHMEEHGIK FIRQFVPTKI EQIEAGTPGR LRVTAQSTNS EETIEGEFNT 400
    VLLAVGRDSC TRTIGLETVG VKINEKTGKI PVTDEEQTNV PYIYAIGDIL 450
    EGKLELTPVA IQAGRLLAQR LYGGSNVKCD YDNVPTTVFT PLEYGCCGLS 500
    EEKAVEKFGE ENIEVYHSFF WPLEWTVPSR DNNKCYAKII CNLKDDERVV 550
    GFHVLGPNAG EVTQGFAAAL KCGLTKQQLD STIGIHPVCA EIFTTLSVTK 600
    RSGGDILQSG CUG 613
    Length:613
    Mass (Da):67,084
    Last modified:February 26, 2008 - v3
    Checksum:iC9FD2E2E8C55118C
    GO
    Isoform 2 (identifier: Q9JMH6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-114: Missing.

    Show »
    Length:499
    Mass (Da):54,544
    Checksum:iFEBB478D8B22429E
    GO

    Sequence cautioni

    The sequence AAH37643.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.
    The sequence BAE26918.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.
    The sequence BAE40292.1 differs from that shown. Reason: Erroneous termination at position 612. Translated as Sec.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti238 – 2381K → E in BAE28994. (PubMed:16141072)Curated
    Sequence conflicti372 – 3721Q → R in BAE26918. (PubMed:16141072)Curated
    Sequence conflicti607 – 6071L → V in BAE26918. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 114114Missing in isoform 2. 3 PublicationsVSP_031566Add
    BLAST

    Non-standard residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-standard residuei612 – 6121SelenocysteineBy similarity

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB027565 mRNA. Translation: BAA86985.2.
    AF333036 mRNA. Translation: AAK01140.1.
    AK011902 mRNA. Translation: BAB27905.1.
    AK146125 mRNA. Translation: BAE26918.1. Sequence problems.
    AK149625 mRNA. Translation: BAE28994.1.
    AK168356 mRNA. Translation: BAE40292.1. Sequence problems.
    BC037643 mRNA. Translation: AAH37643.1. Sequence problems.
    CCDSiCCDS24072.1. [Q9JMH6-2]
    RefSeqiNP_001035978.1. NM_001042513.1. [Q9JMH6-2]
    NP_001035979.1. NM_001042514.1. [Q9JMH6-2]
    NP_001035988.1. NM_001042523.1. [Q9JMH6-1]
    NP_056577.2. NM_015762.2. [Q9JMH6-2]
    UniGeneiMm.210155.
    Mm.471159.

    Genome annotation databases

    EnsembliENSMUST00000020484; ENSMUSP00000020484; ENSMUSG00000020250. [Q9JMH6-2]
    GeneIDi50493.
    KEGGimmu:50493.
    UCSCiuc007gjy.1. mouse. [Q9JMH6-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Selenocysteine

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB027565 mRNA. Translation: BAA86985.2 .
    AF333036 mRNA. Translation: AAK01140.1 .
    AK011902 mRNA. Translation: BAB27905.1 .
    AK146125 mRNA. Translation: BAE26918.1 . Sequence problems.
    AK149625 mRNA. Translation: BAE28994.1 .
    AK168356 mRNA. Translation: BAE40292.1 . Sequence problems.
    BC037643 mRNA. Translation: AAH37643.1 . Sequence problems.
    CCDSi CCDS24072.1. [Q9JMH6-2 ]
    RefSeqi NP_001035978.1. NM_001042513.1. [Q9JMH6-2 ]
    NP_001035979.1. NM_001042514.1. [Q9JMH6-2 ]
    NP_001035988.1. NM_001042523.1. [Q9JMH6-1 ]
    NP_056577.2. NM_015762.2. [Q9JMH6-2 ]
    UniGenei Mm.210155.
    Mm.471159.

    3D structure databases

    ProteinModelPortali Q9JMH6.
    SMRi Q9JMH6. Positions 124-611.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JMH6. 3 interactions.
    MINTi MINT-1869051.

    PTM databases

    PhosphoSitei Q9JMH6.

    2D gel databases

    REPRODUCTION-2DPAGE Q9JMH6.

    Proteomic databases

    MaxQBi Q9JMH6.
    PaxDbi Q9JMH6.
    PRIDEi Q9JMH6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020484 ; ENSMUSP00000020484 ; ENSMUSG00000020250 . [Q9JMH6-2 ]
    GeneIDi 50493.
    KEGGi mmu:50493.
    UCSCi uc007gjy.1. mouse. [Q9JMH6-1 ]

    Organism-specific databases

    CTDi 7296.
    MGIi MGI:1354175. Txnrd1.

    Phylogenomic databases

    eggNOGi COG1249.
    GeneTreei ENSGT00390000007578.
    HOGENOMi HOG000276712.
    HOVERGENi HBG004959.
    InParanoidi Q9JMH6.
    KOi K00384.
    OMAi VCAEIFT.
    OrthoDBi EOG779NXG.
    PhylomeDBi Q9JMH6.
    TreeFami TF314782.

    Enzyme and pathway databases

    BRENDAi 1.8.1.9. 3474.
    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.
    REACT_198602. PPARA activates gene expression.

    Miscellaneous databases

    ChiTaRSi TXNRD1. mouse.
    NextBioi 307476.
    PROi Q9JMH6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JMH6.
    Bgeei Q9JMH6.
    CleanExi MM_TXNRD1.
    Genevestigatori Q9JMH6.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    IPR006338. Thioredoxin/glutathione_Rdtase.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01438. TGR. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of mouse thioredoxin reductases."
      Kawai H., Ota T., Suzuki F., Tatsuka M.
      Gene 242:321-330(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
      Tissue: Thymus.
    2. "Heterogeneity within animal thioredoxin reductases: evidence for alternative first exon splicing."
      Sun Q.-A., Zappacosta F., Factor V.M., Wirth P.J., Hatfield D.L., Gladyshev V.N.
      J. Biol. Chem. 276:3106-3114(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY.
    3. "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] (ISOFORM 2).
      Strain: C57BL/6J and DBA/2.
      Tissue: Embryo.
    4. "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] (ISOFORM 2).
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    5. "Genomic organisation and alternative splicing of mouse and human thioredoxin reductase 1 genes."
      Osborne S.A., Tonissen K.F.
      BMC Genomics 2:10-10(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2).
    6. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTRXR1_MOUSE
    AccessioniPrimary (citable) accession number: Q9JMH6
    Secondary accession number(s): Q3UEB7
    , Q3UK84, Q8CI31, Q99P49, Q9CSV5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2002
    Last sequence update: February 26, 2008
    Last modified: October 1, 2014
    This is version 133 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond. The selenocysteine residue is also essential for catalytic activity By similarity.By similarity

    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