ID A0A1E7FJC7_9STRA Unreviewed; 109 AA.
AC A0A1E7FJC7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Glutaredoxin-2, mitochondrial {ECO:0000256|ARBA:ARBA00039819};
DE Flags: Fragment;
GN ORFNames=FRACYDRAFT_164287 {ECO:0000313|EMBL:OEU18281.1};
OS Fragilariopsis cylindrus CCMP1102.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Bacillariophyceae; Bacillariophycidae; Bacillariales; Bacillariaceae;
OC Fragilariopsis.
OX NCBI_TaxID=635003 {ECO:0000313|EMBL:OEU18281.1, ECO:0000313|Proteomes:UP000095751};
RN [1] {ECO:0000313|EMBL:OEU18281.1, ECO:0000313|Proteomes:UP000095751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1102 {ECO:0000313|EMBL:OEU18281.1,
RC ECO:0000313|Proteomes:UP000095751};
RG DOE Joint Genome Institute;
RA Mock T., Otillar R.P., Strauss J., Dupont C., Frickenhaus S., Maumus F.,
RA Mcmullan M., Sanges R., Schmutz J., Toseland A., Valas R., Veluchamy A.,
RA Ward B.J., Allen A., Barry K., Falciatore A., Ferrante M., Fortunato A.E.,
RA Gloeckner G., Gruber A., Hipkin R., Janech M., Kroth P., Leese F.,
RA Lindquist E., Lyon B.R., Martin J., Mayer C., Parker M., Quesneville H.,
RA Raymond J., Uhlig C., Valentin K.U., Worden A.Z., Armbrust E.V., Bowler C.,
RA Green B., Moulton V., Van Oosterhout C., Grigoriev I.;
RT "Extensive genetic diversity and differential bi-allelic expression allows
RT diatom success in the polar Southern Ocean.";
RL Submitted (SEP-2016) 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}.
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DR EMBL; KV784356; OEU18281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E7FJC7; -.
DR EnsemblProtists; OEU18281; OEU18281; FRACYDRAFT_164287.
DR KEGG; fcy:FRACYDRAFT_164287; -.
DR InParanoid; A0A1E7FJC7; -.
DR OrthoDB; 203654at2759; -.
DR Proteomes; UP000095751; Unassembled WGS sequence.
DR CDD; cd03419; GRX_GRXh_1_2_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
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 SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Glutathionylation {ECO:0000256|ARBA:ARBA00023206};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000095751};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 12..85
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OEU18281.1"
FT NON_TER 109
FT /evidence="ECO:0000313|EMBL:OEU18281.1"
SQ SEQUENCE 109 AA; 11934 MW; 963B9AF60EE34249 CRC64;
DCINRIIHKY PVVVFSKPSC PYCRKALEAL SLAGISQNEK SEHNDSVLHV IDLSQHSNTQ
EIQRTLQTMT GRRTVPNVFV GGTSIGGGDE TSKFQRNGQL VPLLEKAGA
//