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Database: UniProt
Entry: G3TDW6_LOXAF
LinkDB: G3TDW6_LOXAF
Original site: G3TDW6_LOXAF 
ID   G3TDW6_LOXAF            Unreviewed;       124 AA.
AC   G3TDW6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Glutaredoxin-2, mitochondrial {ECO:0000256|ARBA:ARBA00039819};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000012401.3, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000012401.3, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012401.3,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000012401.3}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000012401.3};
RG   Ensembl;
RL   Submitted (JUL-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   AlphaFoldDB; G3TDW6; -.
DR   STRING; 9785.ENSLAFP00000012401; -.
DR   Ensembl; ENSLAFT00000014809.3; ENSLAFP00000012401.3; ENSLAFG00000014814.3.
DR   eggNOG; KOG1752; Eukaryota.
DR   GeneTree; ENSGT00940000164211; -.
DR   HOGENOM; CLU_026126_7_2_1; -.
DR   InParanoid; G3TDW6; -.
DR   OMA; INGNCVG; -.
DR   TreeFam; TF319627; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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   Glutathionylation {ECO:0000256|ARBA:ARBA00023206};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          30..92
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   124 AA;  14098 MW;  BBDCD807A34FDDA8 CRC64;
     RMGSNISSSW GKSAVAPMNQ IQETISDNCV VIFSKTSCSY CTMAKKLFHD ININYKVVEL
     DMLEYGNQFQ DALFKMTGER TVPRIFVNGT FIGGATDTHR LHKEGKLLPL VHQCYVKKSK
     RKEF
//
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