ID G1S8U0_NOMLE Unreviewed; 164 AA.
AC G1S8U0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glutaredoxin-2, mitochondrial {ECO:0000256|ARBA:ARBA00039819};
GN Name=GLRX2 {ECO:0000313|Ensembl:ENSNLEP00000021929.2};
OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Nomascus.
OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000021929.2, ECO:0000313|Proteomes:UP000001073};
RN [1] {ECO:0000313|Ensembl:ENSNLEP00000021929.2, ECO:0000313|Proteomes:UP000001073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Gibbon Genome Sequencing Consortium;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSNLEP00000021929.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00037470}.
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The homodimer
CC is probably linked by 1 2Fe-2S cluster.
CC {ECO:0000256|ARBA:ARBA00038558}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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DR EMBL; ADFV01022863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003264542.1; XM_003264494.3.
DR AlphaFoldDB; G1S8U0; -.
DR STRING; 61853.ENSNLEP00000021929; -.
DR Ensembl; ENSNLET00000023037.3; ENSNLEP00000021929.2; ENSNLEG00000018049.3.
DR GeneID; 100597542; -.
DR KEGG; nle:100597542; -.
DR CTD; 51022; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000162420; -.
DR HOGENOM; CLU_026126_7_0_1; -.
DR InParanoid; G1S8U0; -.
DR OrthoDB; 203654at2759; -.
DR TreeFam; TF319627; -.
DR Proteomes; UP000001073; Chromosome 9.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02180; GRX_euk; 1.
DR PANTHER; PTHR46679; -; 1.
DR PANTHER; PTHR46679:SF1; GLUTAREDOXIN-2, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Glutathionylation {ECO:0000256|ARBA:ARBA00023206};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 69..131
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 164 AA; 18200 MW; 516116C43CAABD31 CRC64;
MLWRRAALAG TRLVWSRSGS AGWLDWAAGA AGAAAAAASR MESNTSSSLE NLATAPVNQI
QETISDNCVV IFSKTSCSYC TMAKKLFRDM NVNYKVVELD LLEYGNQFQD ALYKMTGERT
VPRIFVNGTF IGGATDTHRL HKEGKLLPLV HQCYLKKSKR KEFQ
//
