GLRX2_PONAB
ID GLRX2_PONAB Reviewed; 161 AA.
AC Q5RC53;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Glutaredoxin-2, mitochondrial;
DE Flags: Precursor;
GN Name=GLRX2; Synonyms=GRX2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glutathione-dependent oxidoreductase that facilitates the
CC maintenance of mitochondrial redox homeostasis upon induction of
CC apoptosis by oxidative stress. Involved in response to hydrogen
CC peroxide and regulation of apoptosis caused by oxidative stress. Acts
CC as a very efficient catalyst of monothiol reactions because of its high
CC affinity for protein glutathione-mixed disulfides. Can receive
CC electrons not only from glutathione (GSH), but also from thioredoxin
CC reductase supporting both monothiol and dithiol reactions. Efficiently
CC catalyzes both glutathionylation and deglutathionylation of
CC mitochondrial complex I, which in turn regulates the superoxide
CC production by the complex. Overexpression decreases the susceptibility
CC to apoptosis and prevents loss of cardiolipin and cytochrome c release
CC (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: The 2Fe-2S present in the homodimer leads to
CC inactivation of the enzyme. The 2Fe-2S may serve as a redox sensor: the
CC presence of one-electron oxidants or reductants leading to the loss of
CC the 2Fe-2S cluster, subsequent monomerization and activation of the
CC enzyme (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The homodimer
CC is probably linked by 1 2Fe-2S cluster (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; CR858428; CAH90657.1; -; mRNA.
DR RefSeq; NP_001125356.1; NM_001131884.1.
DR AlphaFoldDB; Q5RC53; -.
DR SMR; Q5RC53; -.
DR STRING; 9601.ENSPPYP00000000449; -.
DR Ensembl; ENSPPYT00000000468; ENSPPYP00000000449; ENSPPYG00000000396.
DR GeneID; 100172258; -.
DR KEGG; pon:100172258; -.
DR CTD; 51022; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000162420; -.
DR InParanoid; Q5RC53; -.
DR OrthoDB; 1535999at2759; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Disulfide bond; Electron transport; Glutathionylation; Iron;
KW Iron-sulfur; Metal-binding; Mitochondrion; Phosphoprotein;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..19
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 20..161
FT /note="Glutaredoxin-2, mitochondrial"
FT /id="PRO_0000011630"
FT DOMAIN 54..154
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in inactive form"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in inactive form"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS18"
FT MOD_RES 74
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 74..77
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 161 AA; 17888 MW; 1FE3E25772979DFA CRC64;
MLWRRAALAG TRLVWSRSGS AGWLDRAAGA AATAASGMES NTSSSLENLE TAPVNQIQET
ISDNCVVIFS KTSCSYCTMA KKLFRDMNVN YKVVELDLLE YGNQFQDALY KMTGGRTVPR
IFVNGTFIGG ATDTHRLHKE GKLLPLVHQC YLKKSKRKEF Q
