ID K7FWZ7_PELSI Unreviewed; 127 AA.
AC K7FWZ7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Glutaredoxin-2, mitochondrial {ECO:0000256|ARBA:ARBA00039819};
GN Name=GLRX2 {ECO:0000313|Ensembl:ENSPSIP00000012557.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000012557.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000012557.1}
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; AGCU01128080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006129206.2; XM_006129144.2.
DR RefSeq; XP_006129207.1; XM_006129145.2.
DR RefSeq; XP_006129208.1; XM_006129146.2.
DR AlphaFoldDB; K7FWZ7; -.
DR STRING; 13735.ENSPSIP00000012557; -.
DR Ensembl; ENSPSIT00000012618.1; ENSPSIP00000012557.1; ENSPSIG00000011320.1.
DR GeneID; 102458298; -.
DR KEGG; pss:102458298; -.
DR CTD; 51022; -.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000162420; -.
DR HOGENOM; CLU_026126_7_2_1; -.
DR OMA; EYACYEL; -.
DR OrthoDB; 203654at2759; -.
DR TreeFam; TF319627; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
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:UP000007267};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 28..90
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 127 AA; 14115 MW; 1FA29F45A98975CB CRC64;
MGNNPSTVGL SNSATVNKIQ ETISDNCVVI FSKTTCAYCK MAKKLFQDMN VNYTAIELDM
YENGSQFQDI LHQMTGGRTV PRVFINGAFI GGATDTQRLH QEGKLLPLVH QCQMRRAKHS
DFPCSLP
//
