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UniProtKB/Swiss-Prot entry P47791


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GSHR_MOUSE
Primary accession number P47791
Secondary accession numbers Q7TNC2 Q8BN97 Q8C9Z6
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on June 21, 2004 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 90)
Name and origin of the protein
Protein name Glutathione reductase, mitochondrial [Precursor]
Synonyms GRase
GR
EC 1.8.1.7
Gene name
Name: Gsr
Synonyms: Gr1
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE INITIATION.
DOI=10.1006/bbrc.1997.7153; PubMed=9268726 [NCBI, ExPASy, EBI, Israel, Japan]
Tamura T., McMicken H.W., Smith C.V., Hansen T.N.;
"Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal.";
Biochem. Biophys. Res. Commun. 237:419-422(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION.
Werner D.;
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[3]
PARTIAL NUCLEOTIDE SEQUENCE.
PubMed=2185014 [NCBI, ExPASy, EBI, Israel, Japan]
Tutic M., Lu X.A., Schirmer R.H., Werner D.;
"Cloning and sequencing of mammalian glutathione reductase cDNA.";
Eur. J. Biochem. 188:523-528(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Eye, and Thymus;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X76341; CAA53959.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK040136; BAC30518.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK084328; BAC39162.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056357; AAH56357.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC057325; AAH57325.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR PC4370; PC4370.
S39494; S39494.
RefSeq NP_034474.4; -.
UniGene Mm.283573
3D structure databases
HSSP P00390; 1ALG. [HSSP ENTRY / PDB]
SMR P47791; 41-500.
ModBase P47791.
PTM databases
PhosphoSite P47791; -.
Organism-specific databases
MGI MGI:95804; Gsr.
Gene expression databases
ArrayExpress P47791; -.
CleanEx MM_GSR; -.
GermOnline ENSMUSG00000031584; Mus musculus.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from MGI).
GO:0004362; Molecular function: glutathione-disulfide reductase activity (inferred from direct assay from MGI).
GO:0006749; Biological process: glutathione metabolic process (inferred by curator from MGI).
QuickGo view.
Family and domain databases
InterPro IPR013027; FAD_pyr_nucl-diS_OxRdtase.
IPR006322; Glut_reduct_1.
IPR000815; Hg_reductase.
IPR001100; Pyr_nuc-diS_OxRdtase.
IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
IPR012999; Pyr_OxRdtase_I_AS.
IPR001327; Pyr_OxRdtase_NAD_bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.390.30; Pyr_redox_dim; 1.
Pfam PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
PF02852; Pyr_redox_dim; 1.
Pfam graphical view of domain structure.
PRINTS PR00368; FADPNR.
PR00945; HGRDTASE.
PR00411; PNDRDTASEI.
ProDom PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01421; gluta_reduc_1; 1.
PROSITE PS00076; PYRIDINE_REDOX_1; 1.
BLOCKS P47791.
Genome annotation databases
Ensembl ENSMUSG00000031584; Mus musculus. [Contig view]
GeneID 14782; -.
KEGG mmu:14782; -.
NMPDR fig|10090.3.peg.18377; -.
Phylogenomic databases
HOGENOM P47791; -.
HOVERGEN P47791; -.
Other
SOURCE Gsr; Mus musculus.
ProtoNet P47791.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Alternative initiation; Cytoplasm; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    26  26     Mitochondrion (Potential). 
CHAIN   27   500  474     Glutathione reductase, mitochondrial. PRO_0000030278
NP_BIND   72    80  9     FAD (By similarity). 
ACT_SITE   489   489        Proton acceptor (By similarity). 
DISULFID   80    85        Redox-active (By similarity). 
DISULFID   112   112        Interchain (By similarity). 
VAR_SEQ   1    26        Missing (in isoform Cytoplasmic). VSP_018973
CONFLICT   26    26        A -> T (in Ref. 2; CAA53959). 
CONFLICT   255   255        N -> K (in Ref. 2; CAA53959). 
CONFLICT   300   300        M -> V (in Ref. 2; CAA53959). 
CONFLICT   312   312        G -> R (in Ref. 5; AAH56357/AAH57325). 
Sequence information
Length: 500 AA [This is the length of the unprocessed precursor] Molecular weight: 53663 Da [This is the MW of the unprocessed precursor] CRC64: A2E6F629B5CC0B7B [This is a checksum on the sequence]
        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 

P47791 in FASTA format

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