Reviewed, UniProtKB/Swiss-Prot Q5RC53 (GLRX2_PONAB)

Names and origin

Protein names

Recommended name:
    Glutaredoxin-2, mitochondrial

Gene names

Name:	GLRX2
Synonyms:	GRX2

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	161 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	Glutathione-dependent oxidoreductase that facilitates the maintenance of mitochondrial redox homeostasis upon induction of apoptosis by oxidative stress. Involved in response to hydrogen peroxide and regulation of apoptosis caused by oxidative stress. Acts as a very efficient catalyst of monothiol reactions because of its high affinity for protein glutathione-mixed disulfides. Can receive electrons not only from glutathione (GSH), but also from thioredoxin reductase supporting both monothiol and dithiol reactions. Efficiently catalyzes both glutathionylation and deglutathionylation of mitochondrial complex I, which in turn regulates the superoxide production by the complex. Overexpression decreases the susceptibility to apoptosis and prevents loss of cardiolipin and cytochrome c release By similarity.
Enzyme regulation	The 2Fe-2S present in the homodimer leads to inactivation of the enzyme. The 2Fe-2S may serve as a redox sensor: the presence of one-electron oxidants or reductants leading to the loss of the 2Fe-2S cluster, subsequent monomerization and activation of the enzyme By similarity.
Subunit structure	Monomer; active form. Homodimer; inactive form. The homodimer is probably linked by 1 2Fe-2S cluster By similarity.
Subcellular location	Mitochondrion By similarity.
Sequence similarities	Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Mitochondrion
Domain	Redox-active center Transit peptide
Ligand	2Fe-2S Iron Iron-sulfur Metal-binding
PTM	Disulfide bond Glutathionylation
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	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 19	19	Mitochondrion Potential
	Chain	20 – 161	142	Glutaredoxin-2, mitochondrial		PRO_0000011630
Regions
	Domain	54 – 154	101	Glutaredoxin
Sites
	Metal binding	65	1	Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
	Metal binding	150	1	Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
	Binding site	71	1	Glutathione By similarity
	Binding site	106	1	Glutathione By similarity
	Binding site	118	1	Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	74	1	S-glutathionyl cysteine; alternate By similarity
	Disulfide bond	74 ↔ 77		Redox-active; alternate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RC53-1 [UniParc]. Last modified December 21, 2004. Version 1. Checksum: 1FE3E25772979DFA	FASTA	161	17,888
	10 20 30 40 50 60 MLWRRAALAG TRLVWSRSGS AGWLDRAAGA AATAASGMES NTSSSLENLE TAPVNQIQET 70 80 90 100 110 120 ISDNCVVIFS KTSCSYCTMA KKLFRDMNVN YKVVELDLLE YGNQFQDALY KMTGGRTVPR 130 140 150 160 IFVNGTFIGG ATDTHRLHKE GKLLPLVHQC YLKKSKRKEF Q

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR858428 mRNA. Translation: CAH90657.1.
RefSeq	NP_001125356.1.
UniGene	Pab.10987
3D structure databases
SMR	Q5RC53. Positions 51-161.
ModBase	Search...
Genome annotation databases
GeneID	100172258.
Phylogenomic databases
HOVERGEN	Q5RC53.
Family and domain databases
InterPro	IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR014025. Glutaredoxin_sub. IPR015450. Grx-2. IPR011899. GRX_euk. IPR012335. Thioredoxin_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
PANTHER	PTHR10168:SF17. Grx-2. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
PRINTS	PR00160. GLUTAREDOXIN.
TIGRFAMs	TIGR02180. GRX_euk. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. False negative. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLRX2_PONAB

Accession

Primary (citable) accession number: Q5RC53

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	December 21, 2004
Last modified:	June 16, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)