Reviewed, UniProtKB/Swiss-Prot P47791 (GSHR_MOUSE)

Names and origin

Protein names

Recommended name:
    Glutathione reductase, mitochondrial
      Short name=GRase
      Short name=GR
    EC=1.8.1.7

Gene names

Name:	Gsr
Synonyms:	Gr1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript 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	Mitochondrion. 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.
Post-translational modification	The initiator Met-1 of isoform Cytoplasmic is removed. Isoform Cytoplasmic is acetylated at position 2 By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Alternative initiation
Domain	Redox-active center Transit peptide
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic process Inferred by curator. Source: MGI oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	external side of plasma membrane Inferred from direct assay. Source: MGI mitochondrion Inferred from direct assay. Source: MGI
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activity Inferred from direct assay. Source: MGI
Complete GO annotation...

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.

Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity).

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Potential
	Chain	27 – 500	474	Glutathione reductase, mitochondrial		PRO_0000030278
Regions
	Nucleotide binding	72 – 80	9	FAD By similarity
Sites
	Active site	489	1	Proton acceptor By similarity
Amino acid modifications
	Disulfide bond	80 ↔ 85		Redox-active By similarity
	Disulfide bond	112		Interchain By similarity
Natural variations
	Alternative sequence	1 – 26	26	Missing in isoform Cytoplasmic.		VSP_018973
Experimental info
	Sequence conflict	26	1	A → T in CAA53959. Ref.2
	Sequence conflict	255	1	N → K in CAA53959. Ref.2
	Sequence conflict	300	1	M → V in CAA53959. Ref.2
	Sequence conflict	312	1	G → R in AAH56357. Ref.5
	Sequence conflict	312	1	G → R in AAH57325. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform Mitochondrial [UniParc]. Last modified June 21, 2004. Version 3. Checksum: A2E6F629B5CC0B7B	FASTA	500	53,663
	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
	Isoform Cytoplasmic. Checksum: 8E4F19F62DE1AD74	FASTA	474	51,074
	10 20 30 40 50 60 MASPGEPQPP APDTSSFDYL VIGGGSGGLA SARRAAELGA RAAVVESHKL GGTCVNVGCV 70 80 90 100 110 120 PKKVMWNTAV HSEFMHDHVD YGFQSCEGKF SWHVIKQKRD AYVSRLNTIY QNNLTKSHIE 130 140 150 160 170 180 IIHGYATFAD GPRPTVEVNG KKFTAPHILI ATGGVPTVPH ESQIPGASLG ITSDGFFQLE 190 200 210 220 230 240 DLPSRSVIVG AGYIAVEIAG ILSALGSKTS LMIRHDKVLR NFDSLISSNC TEELENAGVE 250 260 270 280 290 300 VLKFTQVKEV KKTSSGLELQ VVTSVPGRKP TTTMIPDVDC LLWAIGRDPN SKGLNLNKVG 310 320 330 340 350 360 IQTDEKGHIL VDEFQNTNVK GVYAVGDVCG KALLTPVAIA AGRKLAHRLF ECKQDSKLDY 370 380 390 400 410 420 DNIPTVVFSH PPIGTVGLTE DEAVHKYGKD NVKIYSTAFT PMYHAVTTRK TKCVMKMVCA 430 440 450 460 470 NKEEKVVGIH MQGIGCDEML QGFAVAVKMG ATKADFDNTV AIHPTSSEEL VTLR

References

	« Hide 'large scale' referencesShow '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: 9268726] [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: 2185014] [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: 16141072] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
IPI	IPI00111359. IPI00760002.
PIR	PC4370. S39494.
RefSeq	NP_034474.4.
UniGene	Mm.283573
3D structure databases
HSSP	HSSP built from PDB template 1ALG based on UniProtKB P00390.
SMR	P47791. Positions 41-500.
ModBase	Search...
PTM databases
PhosphoSite	P47791.
Proteomic databases
PRIDE	P47791.
Genome annotation databases
Ensembl	ENSMUSG00000031584. Mus musculus. [Contig view]
GeneID	14782.
KEGG	mmu:14782.
NMPDR	fig|10090.3.peg.18377.
Organism-specific databases
MGI	MGI:95804. Gsr.
Phylogenomic databases
HOGENOM	P47791.
HOVERGEN	P47791.
OMA	P47791. EFQNTSR.
Enzyme and pathway databases
BRENDA	1.8.1.7. 244.
Gene expression databases
ArrayExpress	P47791.
Bgee	P47791.
CleanEx	MM_GSR.
GermOnline	ENSMUSG00000031584. Mus musculus.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glut_reduct_1. IPR000815. Hg_reductase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view]
Gene3D	G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00945. HGRDTASE.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01421. gluta_reduc_1. 1 hit.
PROSITE	PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	286899.
SOURCE	Search...

Entry information

Entry name

GSHR_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)