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P47791

- GSHR_MOUSE

UniProt

P47791 - GSHR_MOUSE

Protein

Glutathione reductase, mitochondrial

Gene

Gsr

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 3 (21 Jun 2004)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei489 – 4891Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi72 – 809FADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glutathione metabolic process Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_189141. Detoxification of Reactive Oxygen Species.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase, mitochondrial (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:Gsr
    Synonyms:Gr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:95804. Gsr.

    Subcellular locationi

    GO - Cellular componenti

    1. external side of plasma membrane Source: MGI
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
    BLAST
    Chaini27 – 500474Glutathione reductase, mitochondrialPRO_0000030278Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei75 – 751N6-acetyllysine1 Publication
    Disulfide bondi80 ↔ 85Redox-activeBy similarity
    Disulfide bondi112 – 112InterchainBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP47791.
    PaxDbiP47791.
    PRIDEiP47791.

    PTM databases

    PhosphoSiteiP47791.

    Expressioni

    Gene expression databases

    ArrayExpressiP47791.
    BgeeiP47791.
    CleanExiMM_GSR.
    GenevestigatoriP47791.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.

    Protein-protein interaction databases

    IntActiP47791. 3 interactions.
    MINTiMINT-1869660.

    Structurei

    3D structure databases

    ProteinModelPortaliP47791.
    SMRiP47791. Positions 41-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Each subunit can be divided into 4 domains that are consecutive along the polypeptide chain. Domains 1 and 2 bind FAD and NADPH, respectively. Domain 4 forms the interface.

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    Phylogenomic databases

    eggNOGiCOG1249.
    GeneTreeiENSGT00390000007578.
    HOGENOMiHOG000276712.
    HOVERGENiHBG004959.
    InParanoidiP47791.
    KOiK00383.
    OMAiHRQPCKM.
    OrthoDBiEOG7HHWS0.
    PhylomeDBiP47791.
    TreeFamiTF105353.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [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.
    TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative initiation. Align

    Isoform Mitochondrial (identifier: P47791-1) [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

    MALLPRALGV GAAPSLRRAA RALTCAMASP GEPQPPAPDT SSFDYLVIGG    50
    GSGGLASARR AAELGARAAV VESHKLGGTC VNVGCVPKKV MWNTAVHSEF 100
    MHDHVDYGFQ SCEGKFSWHV IKQKRDAYVS RLNTIYQNNL TKSHIEIIHG 150
    YATFADGPRP TVEVNGKKFT APHILIATGG VPTVPHESQI PGASLGITSD 200
    GFFQLEDLPS RSVIVGAGYI AVEIAGILSA LGSKTSLMIR HDKVLRNFDS 250
    LISSNCTEEL ENAGVEVLKF TQVKEVKKTS SGLELQVVTS VPGRKPTTTM 300
    IPDVDCLLWA IGRDPNSKGL NLNKVGIQTD EKGHILVDEF QNTNVKGVYA 350
    VGDVCGKALL TPVAIAAGRK LAHRLFECKQ DSKLDYDNIP TVVFSHPPIG 400
    TVGLTEDEAV HKYGKDNVKI YSTAFTPMYH AVTTRKTKCV MKMVCANKEE 450
    KVVGIHMQGI GCDEMLQGFA VAVKMGATKA DFDNTVAIHP TSSEELVTLR 500
    Length:500
    Mass (Da):53,663
    Last modified:June 21, 2004 - v3
    Checksum:iA2E6F629B5CC0B7B
    GO
    Isoform Cytoplasmic (identifier: P47791-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.

    Show »
    Length:474
    Mass (Da):51,074
    Checksum:i8E4F19F62DE1AD74
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261A → T in CAA53959. 1 PublicationCurated
    Sequence conflicti255 – 2551N → K in CAA53959. 1 PublicationCurated
    Sequence conflicti300 – 3001M → V in CAA53959. 1 PublicationCurated
    Sequence conflicti312 – 3121G → R in AAH56357. (PubMed:15489334)Curated
    Sequence conflicti312 – 3121G → R in AAH57325. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626Missing in isoform Cytoplasmic. CuratedVSP_018973Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76341 mRNA. Translation: CAA53959.3.
    AK040136 mRNA. Translation: BAC30518.1.
    AK084328 mRNA. Translation: BAC39162.1.
    BC056357 mRNA. Translation: AAH56357.1.
    BC057325 mRNA. Translation: AAH57325.1.
    CCDSiCCDS22235.1. [P47791-1]
    PIRiPC4370.
    S39494.
    RefSeqiNP_034474.4. NM_010344.4. [P47791-1]
    UniGeneiMm.283573.

    Genome annotation databases

    EnsembliENSMUST00000033992; ENSMUSP00000033992; ENSMUSG00000031584. [P47791-1]
    GeneIDi14782.
    KEGGimmu:14782.
    UCSCiuc009lkf.1. mouse. [P47791-1]

    Keywords - Coding sequence diversityi

    Alternative initiation

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76341 mRNA. Translation: CAA53959.3 .
    AK040136 mRNA. Translation: BAC30518.1 .
    AK084328 mRNA. Translation: BAC39162.1 .
    BC056357 mRNA. Translation: AAH56357.1 .
    BC057325 mRNA. Translation: AAH57325.1 .
    CCDSi CCDS22235.1. [P47791-1 ]
    PIRi PC4370.
    S39494.
    RefSeqi NP_034474.4. NM_010344.4. [P47791-1 ]
    UniGenei Mm.283573.

    3D structure databases

    ProteinModelPortali P47791.
    SMRi P47791. Positions 41-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P47791. 3 interactions.
    MINTi MINT-1869660.

    PTM databases

    PhosphoSitei P47791.

    Proteomic databases

    MaxQBi P47791.
    PaxDbi P47791.
    PRIDEi P47791.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033992 ; ENSMUSP00000033992 ; ENSMUSG00000031584 . [P47791-1 ]
    GeneIDi 14782.
    KEGGi mmu:14782.
    UCSCi uc009lkf.1. mouse. [P47791-1 ]

    Organism-specific databases

    CTDi 2936.
    MGIi MGI:95804. Gsr.

    Phylogenomic databases

    eggNOGi COG1249.
    GeneTreei ENSGT00390000007578.
    HOGENOMi HOG000276712.
    HOVERGENi HBG004959.
    InParanoidi P47791.
    KOi K00383.
    OMAi HRQPCKM.
    OrthoDBi EOG7HHWS0.
    PhylomeDBi P47791.
    TreeFami TF105353.

    Enzyme and pathway databases

    Reactomei REACT_189141. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi GSR. mouse.
    NextBioi 286899.
    PROi P47791.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47791.
    Bgeei P47791.
    CleanExi MM_GSR.
    Genevestigatori P47791.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [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 TIGR01421. gluta_reduc_1. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal."
      Tamura T., McMicken H.W., Smith C.V., Hansen T.N.
      Biochem. Biophys. Res. Commun. 237:419-422(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE INITIATION.
    2. Werner D.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
    3. "Cloning and sequencing of mammalian glutathione reductase cDNA."
      Tutic M., Lu X.A., Schirmer R.H., Werner D.
      Eur. J. Biochem. 188:523-528(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE.
    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: Eye and Thymus.
    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/6.
      Tissue: Brain.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-75, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiGSHR_MOUSE
    AccessioniPrimary (citable) accession number: P47791
    Secondary accession number(s): Q7TNC2, Q8BN97, Q8C9Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: June 21, 2004
    Last modified: October 1, 2014
    This is version 147 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.

    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