GSHR_CALJA
ID GSHR_CALJA Reviewed; 522 AA.
AC A2TIL1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Glutathione reductase, mitochondrial;
DE Short=GR;
DE Short=GRase;
DE EC=1.8.1.7;
DE Flags: Precursor;
GN Name=GSR;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Atanasova S., von Ahsen N., Schlumbohm C., Wieland E., Oellerich M.,
RA Armstrong V.;
RT "Free radical scavenging enzymes in Callithrix jacchus.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Maintains high levels of reduced glutathione in the cytosol.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + NADP(+) = glutathione disulfide + H(+) +
CC NADPH; Xref=Rhea:RHEA:11740, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58349; EC=1.8.1.7;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Mitochondrial;
CC IsoId=A2TIL1-1; Sequence=Displayed;
CC Name=Cytoplasmic;
CC IsoId=A2TIL1-2; Sequence=VSP_030441;
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EF203010; ABN05297.1; -; mRNA.
DR RefSeq; NP_001171974.1; NM_001185045.1. [A2TIL1-1]
DR AlphaFoldDB; A2TIL1; -.
DR SMR; A2TIL1; -.
DR STRING; 9483.ENSCJAP00000006959; -.
DR GeneID; 100393824; -.
DR KEGG; cjc:100393824; -.
DR CTD; 2936; -.
DR eggNOG; KOG0405; Eukaryota.
DR InParanoid; A2TIL1; -.
DR OrthoDB; 581771at2759; -.
DR Proteomes; UP000008225; Unplaced.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004362; F:glutathione-disulfide reductase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR006322; Glutathione_Rdtase_euk/bac.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR42737; PTHR42737; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR SUPFAM; SSF55424; SSF55424; 1.
DR TIGRFAMs; TIGR01421; gluta_reduc_1; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative initiation; Cytoplasm; Disulfide bond; FAD;
KW Flavoprotein; Mitochondrion; NADP; Oxidoreductase; Redox-active center;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..522
FT /note="Glutathione reductase, mitochondrial"
FT /id="PRO_0000314948"
FT ACT_SITE 511
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 94..102
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 97
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P47791"
FT DISULFID 102..107
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 134
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform Cytoplasmic)"
FT /evidence="ECO:0000305"
FT /id="VSP_030441"
SQ SEQUENCE 522 AA; 56193 MW; A952357C8E8E0E86 CRC64;
MALLPRALSS GGRPSWRRAA RASRGFPLPL PFPAAATHAL SRAMACRQEP QPQGPPPSAG
AVVSYDYLVI GGGSGGLASA RRAAELGARA AVVESHKLGG TCVNVGCVPK KVMWNTAVHS
EFLHDHGDYG FSSCEGKFNW RVIKEKRDTY VSRLNTIYQN NLTKAHIEII HGHAVFTSDT
KPTIEVSGRK YTAPHILIAT GGMPSSPHES QIPGASLGIT SDGFFELEEL PSRSVIVGAG
YIAVEIAGIL SALGSKTSLM IRHDKVLRSF DSMISTNCTE ELENAGVEVL KFSQVKEVKK
TSSGLEVSLV TAVPGRLPVM TTISDVDCLL WAIGRDPNSK GLSLNKLGIK TDDKGHIIVD
EFQNTNVKGI YAVGDVCGKA LLTPVAIAAG RKLAHRLFEN KEDSKLDYNN IPTVVFSHPP
IGTVGLTEDE AIHKYGKENV KIYSTSFTPM YHAVTKRKTK CVMKMVCAYE EEKVVGIHMQ
GLGCDEMLQG FAVAVKMGAT KADFDNTVAI HPTSSEELVP LR
