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P47791 (GSHR_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutathione reductase, mitochondrial

Short name=GR
Short name=GRase
EC=1.8.1.7
Gene names
Name:Gsr
Synonyms:Gr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Maintains high levels of reduced glutathione in the cytosol.

Catalytic activity

2 glutathione + NADP+ = glutathione disulfide + NADPH.

Cofactor

Binds 1 FAD per subunit By similarity.

Subunit structure

Homodimer; disulfide-linked.

Subcellular location

Isoform Mitochondrial: Mitochondrion.

Isoform Cytoplasmic: Cytoplasm.

Domain

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.

Miscellaneous

The active site is a redox-active disulfide bond.

Sequence similarities

Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: P47791-1)

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.
Isoform Cytoplasmic (identifier: P47791-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 500474Glutathione reductase, mitochondrial
PRO_0000030278

Regions

Nucleotide binding72 – 809FAD By similarity

Sites

Active site4891Proton acceptor By similarity

Amino acid modifications

Modified residue751N6-acetyllysine Ref.6
Disulfide bond80 ↔ 85Redox-active By similarity
Disulfide bond112Interchain By similarity

Natural variations

Alternative sequence1 – 2626Missing in isoform Cytoplasmic.
VSP_018973

Experimental info

Sequence conflict261A → T in CAA53959. Ref.2
Sequence conflict2551N → K in CAA53959. Ref.2
Sequence conflict3001M → V in CAA53959. Ref.2
Sequence conflict3121G → R in AAH56357. Ref.5
Sequence conflict3121G → R in AAH57325. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform Mitochondrial [UniParc].

Last modified June 21, 2004. Version 3.
Checksum: A2E6F629B5CC0B7B

FASTA50053,663
        10         20         30         40         50         60 
MALLPRALGV GAAPSLRRAA RALTCAMASP GEPQPPAPDT SSFDYLVIGG GSGGLASARR 

        70         80         90        100        110        120 
AAELGARAAV VESHKLGGTC VNVGCVPKKV MWNTAVHSEF MHDHVDYGFQ SCEGKFSWHV 

       130        140        150        160        170        180 
IKQKRDAYVS RLNTIYQNNL TKSHIEIIHG YATFADGPRP TVEVNGKKFT APHILIATGG 

       190        200        210        220        230        240 
VPTVPHESQI PGASLGITSD GFFQLEDLPS RSVIVGAGYI AVEIAGILSA LGSKTSLMIR 

       250        260        270        280        290        300 
HDKVLRNFDS LISSNCTEEL ENAGVEVLKF TQVKEVKKTS SGLELQVVTS VPGRKPTTTM 

       310        320        330        340        350        360 
IPDVDCLLWA IGRDPNSKGL NLNKVGIQTD EKGHILVDEF QNTNVKGVYA VGDVCGKALL 

       370        380        390        400        410        420 
TPVAIAAGRK LAHRLFECKQ DSKLDYDNIP TVVFSHPPIG TVGLTEDEAV HKYGKDNVKI 

       430        440        450        460        470        480 
YSTAFTPMYH AVTTRKTKCV MKMVCANKEE KVVGIHMQGI GCDEMLQGFA VAVKMGATKA 

       490        500 
DFDNTVAIHP TSSEELVTLR 

« Hide

Isoform Cytoplasmic [UniParc].

Checksum: 8E4F19F62DE1AD74
Show »

FASTA47451,074

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22235.1. [P47791-1]
PIRPC4370.
S39494.
RefSeqNP_034474.4. NM_010344.4. [P47791-1]
UniGeneMm.283573.

3D structure databases

ProteinModelPortalP47791.
SMRP47791. Positions 41-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP47791. 3 interactions.
MINTMINT-1869660.

PTM databases

PhosphoSiteP47791.

Proteomic databases

MaxQBP47791.
PaxDbP47791.
PRIDEP47791.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033992; ENSMUSP00000033992; ENSMUSG00000031584. [P47791-1]
GeneID14782.
KEGGmmu:14782.
UCSCuc009lkf.1. mouse. [P47791-1]

Organism-specific databases

CTD2936.
MGIMGI:95804. Gsr.

Phylogenomic databases

eggNOGCOG1249.
GeneTreeENSGT00390000007578.
HOGENOMHOG000276712.
HOVERGENHBG004959.
InParanoidP47791.
KOK00383.
OMAHRQPCKM.
OrthoDBEOG7HHWS0.
PhylomeDBP47791.
TreeFamTF105353.

Gene expression databases

ArrayExpressP47791.
BgeeP47791.
CleanExMM_GSR.
GenevestigatorP47791.

Family and domain databases

Gene3D3.30.390.30. 1 hit.
InterProIPR016156. 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]
PfamPF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]
PRINTSPR00368. FADPNR.
SUPFAMSSF55424. SSF55424. 1 hit.
TIGRFAMsTIGR01421. gluta_reduc_1. 1 hit.
PROSITEPS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGSR. mouse.
NextBio286899.
PROP47791.
SOURCESearch...

Entry information

Entry nameGSHR_MOUSE
AccessionPrimary (citable) accession number: P47791
Secondary accession number(s): Q7TNC2, Q8BN97, Q8C9Z6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: June 21, 2004
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot