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   24-JAN-2024, entry version 124.
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; 9913-ENSBTAP00000021249; -.
DR   Ensembl; ENSBTAT00000021249.4; ENSBTAP00000021249.3; ENSBTAG00000015972.4.
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; INGNCVG; -.
DR   OrthoDB; 203654at2759; -.
DR   TreeFam; TF319627; -.
DR   Proteomes; UP000009136; Chromosome 16.
DR   Bgee; ENSBTAG00000015972; Expressed in rumen papilla and 108 other cell types or 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IBA:GO_Central.
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   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
//