Reviewed, UniProtKB/Swiss-Prot Q9QUH0 (GLRX1_MOUSE)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-1
Alternative name(s):
    Thioltransferase-1
      Short name=TTase-1

Gene names

Name:	Glrx
Synonyms:	Glrx1, Grx, Grx1

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	107 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Acetylation Disulfide bond
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro protein-disulfide reductase (glutathione) activity Ref.2 Traceable author statement. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 107	106	Glutaredoxin-1		PRO_0000141601
Regions
	Domain	3 – 106	104	Glutaredoxin
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Disulfide bond	23 ↔ 26		Redox-active
	Disulfide bond	79 ↔ 83		By similarity
Experimental info
	Mutagenesis	23	1	C → S: Loss of activity.
	Mutagenesis	26	1	C → S: Loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	Q9QUH0-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DC0C7718DCD8805F	FASTA	107	11,871
	10 20 30 40 50 60 MAQEFVNCKI QSGKVVVFIK PTCPYCRKTQ EILSQLPFKQ GLLEFVDITA TNNTSAIQDY 70 80 90 100 LQQLTGARTV PRVFIGKDCI GGCSDLISMQ QTGELMTRLK QIGALQL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse glutaredoxin -- cDNA cloning, high level expression in E. coli and its possible implication in redox regulation of the DNA binding activity in transcription factor PEBP2." Nakamura T., Ohno T., Hirota K., Nishiyama A., Nakamura H., Wada H., Yodoi J. Free Radic. Res. 31:357-365(1999) [PubMed: 10517541] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS. Tissue: Spleen.
[2]	"Cloning and sequencing of mouse glutaredoxin (grx) cDNA." Miranda-Vizuete A., Pedrajas J.R., Damdimopoulos A.E., Spyrou G. DNA Seq. 10:179-182(1999) [PubMed: 10647820] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	Reddy P.G., Bhuyan D.K., Bhuyan K.C. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: CFW. Tissue: Lens.
[4]	"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: FVB/N. Tissue: Colon.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB013137 mRNA. Translation: BAA86926.1. AF109314 mRNA. Translation: AAF04780.1. AF276917 mRNA. Translation: AAF86464.1. BC012642 mRNA. Translation: AAH12642.1.
IPI	IPI00331528.
RefSeq	NP_444338.2.
UniGene	Mm.25844
3D structure databases
HSSP	HSSP built from PDB template 1JHB based on UniProtKB P35754.
SMR	Q9QUH0. Positions 2-106.
ModBase	Search...
Genome annotation databases
Ensembl	ENSMUSG00000021591. Mus musculus. [Contig view]
GeneID	93692.
KEGG	mmu:93692.
Organism-specific databases
MGI	MGI:2135625. Glrx.
Phylogenomic databases
HOGENOM	Q9QUH0.
HOVERGEN	Q9QUH0.
OMA	Q9QUH0. GGCSDLI.
Gene expression databases
ArrayExpress	Q9QUH0.
Bgee	Q9QUH0.
CleanEx	MM_GLRX.
GermOnline	ENSMUSG00000021591. Mus musculus.
Family and domain databases
InterPro	IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR014025. Glutaredoxin_sub. IPR011899. GRX_euk. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
PRINTS	PR00160. GLUTAREDOXIN.
TIGRFAMs	TIGR02180. GRX_euk. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	351441.
SOURCE	Search...

Entry information

Entry name

GLRX1_MOUSE

Accession

Primary (citable) accession number: Q9QUH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)