NameGlutaredoxin-2, mitochondrial
Synonyms
  • GRX2
Gene NameGLRX2
OrganismHuman
Amino acid sequence
>lcl|BSEQ0004500|Glutaredoxin-2, mitochondrial
MIWRRAALAGTRLVWSRSGSAGWLDRAAGAAGAAAAAASGMESNTSSSLENLATAPVNQI
QETISDNCVVIFSKTSCSYCTMAKKLFHDMNVNYKVVELDLLEYGNQFQDALYKMTGERT
VPRIFVNGTFIGGATDTHRLHKEGKLLPLVHQCYLKKSKRKEFQ
Number of residues164
Molecular Weight18051.515
Theoretical pI9.49
GO Classification
Functions
  • protein disulfide oxidoreductase activity
  • metal ion binding
  • 2 iron, 2 sulfur cluster binding
  • arsenate reductase (glutaredoxin) activity
  • protein disulfide isomerase activity
  • electron carrier activity
  • glutathione disulfide oxidoreductase activity
Processes
  • aging
  • protein folding
  • DNA protection
  • response to redox state
  • regulation of signal transduction
  • glutathione metabolic process
  • response to organic substance
  • cell redox homeostasis
  • cellular response to superoxide
  • cell differentiation
  • response to temperature stimulus
  • regulation of transcription, DNA-templated
  • response to hydrogen peroxide
  • apoptotic process
Components
  • mitochondrial matrix
  • nucleoplasm
  • intracellular membrane-bounded organelle
  • dendrite
  • mitochondrion
  • neuronal cell body
  • nucleus
General FunctionProtein disulfide oxidoreductase activity
Specific FunctionGlutathione-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.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID9507250
UniProtKB IDQ9NS18
UniProtKB Entry NameGLRX2_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0011651|Glutaredoxin-2, mitochondrial (GLRX2)
ATGGAGAGCAATACATCATCATCTTTGGAGAATTTAGCGACGGCGCCTGTGAACCAGATC
CAAGAAACAATTTCTGATAATTGTGTGGTGATTTTCTCAAAAACATCCTGTTCTTACTGT
ACAATGGCAAAAAAGCTTTTCCATGACATGAATGTTAACTATAAAGTGGTGGAACTGGAC
CTGCTTGAATATGGAAACCAGTTCCAAGATGCTCTTTACAAAATGACTGGTGAAAGAACT
GTTCCAAGAATATTTGTCAATGGTACTTTTATTGGAGGTGCAACTGACACTCATAGGCTT
CACAAAGAAGGAAAATTGCTCCCACTAGTTCATCAGTGTTATTTAAAAAAAAGTAAGAGG
AAAGAATTTCAGTGA
GenBank Gene IDAF132495
GeneCard IDNot Available
GenAtlas IDGLRX2
HGNC IDHGNC:16065
Chromosome Location1
Locus1q31.2-q31.3
References
  1. Lundberg M, Johansson C, Chandra J, Enoksson M, Jacobsson G, Ljung J, Johansson M, Holmgren A: Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. J Biol Chem. 2001 Jul 13;276(28):26269-75. Epub 2001 Apr 10. 11297543
  2. Gladyshev VN, Liu A, Novoselov SV, Krysan K, Sun QA, Kryukov VM, Kryukov GV, Lou MF: Identification and characterization of a new mammalian glutaredoxin (thioltransferase), Grx2. J Biol Chem. 2001 Aug 10;276(32):30374-80. Epub 2001 Jun 7. 11397793
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