Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione reductase, mitochondrial

Gene

Gsr

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

Functioni

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activityi

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactori

FADBy similarityNote: 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

GO - Biological processi

  • cell redox homeostasis Source: InterPro
  • glutathione metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_308972. Detoxification of Reactive Oxygen Species.
REACT_360191. TP53 Regulates Metabolic Genes.

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 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:95804. Gsr.

Subcellular locationi

GO - Cellular componenti

  • external side of plasma membrane Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

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

BgeeiP47791.
CleanExiMM_GSR.
ExpressionAtlasiP47791. baseline and differential.
GenevisibleiP47791. MM.

Interactioni

Subunit structurei

Homodimer; disulfide-linked.

Protein-protein interaction databases

IntActiP47791. 3 interactions.
MINTiMINT-1869660.
STRINGi10090.ENSMUSP00000033992.

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.
OMAiYAEDYGF.
OrthoDBiEOG7HHWS0.
PhylomeDBiP47791.
TreeFamiTF105353.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
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. AlignAdd to basket

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

        10         20         30         40         50
MALLPRALGV GAAPSLRRAA RALTCAMASP GEPQPPAPDT SSFDYLVIGG
60 70 80 90 100
GSGGLASARR AAELGARAAV VESHKLGGTC VNVGCVPKKV MWNTAVHSEF
110 120 130 140 150
MHDHVDYGFQ SCEGKFSWHV IKQKRDAYVS RLNTIYQNNL TKSHIEIIHG
160 170 180 190 200
YATFADGPRP TVEVNGKKFT APHILIATGG VPTVPHESQI PGASLGITSD
210 220 230 240 250
GFFQLEDLPS RSVIVGAGYI AVEIAGILSA LGSKTSLMIR HDKVLRNFDS
260 270 280 290 300
LISSNCTEEL ENAGVEVLKF TQVKEVKKTS SGLELQVVTS VPGRKPTTTM
310 320 330 340 350
IPDVDCLLWA IGRDPNSKGL NLNKVGIQTD EKGHILVDEF QNTNVKGVYA
360 370 380 390 400
VGDVCGKALL TPVAIAAGRK LAHRLFECKQ DSKLDYDNIP TVVFSHPPIG
410 420 430 440 450
TVGLTEDEAV HKYGKDNVKI YSTAFTPMYH AVTTRKTKCV MKMVCANKEE
460 470 480 490 500
KVVGIHMQGI GCDEMLQGFA VAVKMGATKA DFDNTVAIHP TSSEELVTLR
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 (Ref. 2) Curated
Sequence conflicti255 – 2551N → K in CAA53959 (Ref. 2) Curated
Sequence conflicti300 – 3001M → V in CAA53959 (Ref. 2) Curated
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP47791. 3 interactions.
MINTiMINT-1869660.
STRINGi10090.ENSMUSP00000033992.

Chemistry

ChEMBLiCHEMBL2366476.

PTM databases

PhosphoSiteiP47791.

Proteomic databases

MaxQBiP47791.
PaxDbiP47791.
PRIDEiP47791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2936.
MGIiMGI:95804. Gsr.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_274011. Synthesis and interconversion of nucleotide di- and triphosphates.
REACT_308972. Detoxification of Reactive Oxygen Species.
REACT_360191. TP53 Regulates Metabolic Genes.

Miscellaneous databases

ChiTaRSiGsr. mouse.
NextBioi286899.
PROiP47791.
SOURCEiSearch...

Gene expression databases

BgeeiP47791.
CleanExiMM_GSR.
ExpressionAtlasiP47791. baseline and differential.
GenevisibleiP47791. MM.

Family and domain databases

Gene3Di3.30.390.30. 1 hit.
InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
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]
SUPFAMiSSF55424. SSF55424. 1 hit.
TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 157 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.