GLRX2_BOVIN
ID GLRX2_BOVIN Reviewed; 157 AA.
AC Q32L67;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Glutaredoxin-2, mitochondrial;
DE Flags: Precursor;
GN Name=GLRX2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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 (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: The 2Fe-2S present in the homodimer leads to
CC inactivation of the enzyme. The 2Fe-2S may serve as a redox sensor: the
CC presence of one-electron oxidants or reductants leading to the loss of
CC the 2Fe-2S cluster, subsequent monomerization and activation of the
CC enzyme (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer; active form. Homodimer; inactive form. The homodimer
CC is probably linked by 1 2Fe-2S cluster (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}.
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DR EMBL; BC109742; AAI09743.1; -; mRNA.
DR RefSeq; NP_001035613.1; NM_001040523.2.
DR RefSeq; XP_005216824.1; XM_005216767.3.
DR RefSeq; XP_010811391.1; XM_010813089.2.
DR AlphaFoldDB; Q32L67; -.
DR SMR; Q32L67; -.
DR STRING; 9913.ENSBTAP00000021249; -.
DR PaxDb; Q32L67; -.
DR PRIDE; Q32L67; -.
DR Ensembl; ENSBTAT00000021249; ENSBTAP00000021249; ENSBTAG00000015972.
DR GeneID; 513762; -.
DR KEGG; bta:513762; -.
DR CTD; 51022; -.
DR VEuPathDB; HostDB:ENSBTAG00000015972; -.
DR VGNC; VGNC:29416; GLRX2.
DR eggNOG; KOG1752; Eukaryota.
DR GeneTree; ENSGT00940000164211; -.
DR HOGENOM; CLU_026126_7_0_1; -.
DR InParanoid; Q32L67; -.
DR OMA; DSTHAQF; -.
DR OrthoDB; 1535999at2759; -.
DR TreeFam; TF319627; -.
DR Proteomes; UP000009136; Chromosome 16.
DR Bgee; ENSBTAG00000015972; Expressed in rumen papilla and 108 other tissues.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0097573; F:glutathione oxidoreductase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Disulfide bond; Electron transport; Glutathionylation; Iron;
KW Iron-sulfur; Metal-binding; Mitochondrion; Phosphoprotein;
KW Redox-active center; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..18
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 19..157
FT /note="Glutaredoxin-2, mitochondrial"
FT /id="PRO_0000326628"
FT DOMAIN 51..151
FT /note="Glutaredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT BINDING 62
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in inactive form"
FT /evidence="ECO:0000250"
FT BINDING 68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in inactive form"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NS18"
FT MOD_RES 71
FT /note="S-glutathionyl cysteine; alternate"
FT /evidence="ECO:0000250"
FT DISULFID 71..74
FT /note="Redox-active; alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 157 AA; 17202 MW; 3106F9214733EFD1 CRC64;
MYWRRAALVG TRLIPVRSSS AGRLEGPAGI SGSGMGNSTS SSLGNAATAP VNQIQETISN
NCVVIFSKTS CSYCTMAKNL FHDMNVNYKV VELDMLEYGS QFQDALHKMT GERTVPRIFV
NGTFIGGATD THRLHKEGKL LPLVHQCHLK NSKREEL
