ID A0A3S1BCX5_ELYCH Unreviewed; 140 AA.
AC A0A3S1BCX5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Glutaredoxin-2, mitochondrial {ECO:0000256|ARBA:ARBA00039819};
GN ORFNames=EGW08_011610 {ECO:0000313|EMBL:RUS80630.1};
OS Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC Plakobranchidae; Elysia.
OX NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS80630.1, ECO:0000313|Proteomes:UP000271974};
RN [1] {ECO:0000313|EMBL:RUS80630.1, ECO:0000313|Proteomes:UP000271974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC2010 {ECO:0000313|EMBL:RUS80630.1};
RC TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS80630.1};
RA Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL Submitted (JAN-2019) 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 {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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RUS80630.1}.
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DR EMBL; RQTK01000381; RUS80630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S1BCX5; -.
DR STRING; 188477.A0A3S1BCX5; -.
DR Proteomes; UP000271974; 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 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:UP000271974};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 54..116
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 140 AA; 15162 MW; DBF8697BC67C7E1B CRC64;
MDSSVDISSE LNSRAKGDYG EGEAAAINLS PKIKELVPSD EHSYVQEMVN RNRVVVFSKT
HCPHCTDSKT LLTGRGVEYK TVELDQINNG SQVQNVLGSI TDARTVPRIF INGQCVGGNS
DLKSLDQEGK LGELLKKAGL
//
