Q32L67 (GLRX2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutaredoxin-2, mitochondrial

Gene names

Name:

GLRX2

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	157 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
Technical term	Complete proteome Reference proteome
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 metal 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 – 18	18	Mitochondrion Potential
	Chain	19 – 157	139	Glutaredoxin-2, mitochondrial		PRO_0000326628
Regions
	Domain	51 – 151	101	Glutaredoxin
Sites
	Metal binding	62	1	Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
	Metal binding	147	1	Iron-sulfur (2Fe-2S); shared with dimeric partner; in inactive form By similarity
	Binding site	68	1	Glutathione By similarity
	Binding site	103	1	Glutathione By similarity
	Binding site	115	1	Glutathione; via amide nitrogen and carbonyl oxygen By similarity
Amino acid modifications
	Modified residue	71	1	S-glutathionyl cysteine; alternate By similarity
	Disulfide bond	71 ↔ 74		Redox-active; alternate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q32L67 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 3106F9214733EFD1	FASTA	157	17,202
	10 20 30 40 50 60 MYWRRAALVG TRLIPVRSSS AGRLEGPAGI SGSGMGNSTS SSLGNAATAP VNQIQETISN 70 80 90 100 110 120 NCVVIFSKTS CSYCTMAKNL FHDMNVNYKV VELDMLEYGS QFQDALHKMT GERTVPRIFV 130 140 150 NGTFIGGATD THRLHKEGKL LPLVHQCHLK NSKREEL

References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC109742 mRNA. Translation: AAI09743.1.
IPI	IPI00705575.
RefSeq	NP_001035613.1. NM_001040523.1.
UniGene	Bt.27603.
3D structure databases
HSSP	HSSP built from PDB template 2FLS based on UniProtKB Q9NS18.
ProteinModelPortal	Q32L67.
SMR	Q32L67. Positions 43-157.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000021249; ENSBTAP00000021249; ENSBTAG00000015972.
GeneID	513762.
KEGG	bta:513762.
Organism-specific databases
CTD	51022.
Phylogenomic databases
eggNOG	maNOG20253.
GeneTree	ENSGT00390000003677.
HOVERGEN	HBG096801.
InParanoid	Q32L67.
OMA	KLFHDIN.
OrthoDB	EOG498V20.
PhylomeDB	Q32L67.
Family and domain databases
InterPro	IPR002109. Glutaredoxin. IPR011899. Glutaredoxin_euk/vir. IPR014025. Glutaredoxin_subgr. IPR015450. Grx-2. IPR012336. Thioredoxin-like_fold. [Graphical view]
Gene3D	G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KO	K03676.
PANTHER	PTHR10168:SF17. Grx-2. 1 hit.
Pfam	PF00462. Glutaredoxin. 1 hit. [Graphical view]
PRINTS	PR00160. GLUTAREDOXIN.
SUPFAM	SSF52833. Thiordxn-like_fd. 1 hit.
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_BOVIN

Accession

Primary (citable) accession number: Q32L67

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	December 6, 2005
Last modified:	November 16, 2011
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program