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Database: UniProt
Entry: B5X3J5_SALSA
LinkDB: B5X3J5_SALSA
Original site: B5X3J5_SALSA 
ID   B5X3J5_SALSA            Unreviewed;       489 AA.
AC   B5X3J5;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=Glutaredoxin {ECO:0000313|EMBL:ACI33876.1, ECO:0000313|RefSeq:NP_001133773.1};
DE            EC=1.8.4.1 {ECO:0000313|RefSeq:NP_001133773.1};
DE   SubName: Full=Glutaredoxin-1 isoform X2 {ECO:0000313|RefSeq:XP_014029439.1, ECO:0000313|RefSeq:XP_014029440.1};
GN   Name=GLRX {ECO:0000313|EMBL:ACI33876.1};
GN   Synonyms=glrx {ECO:0000313|RefSeq:NP_001133773.1,
GN   ECO:0000313|RefSeq:XP_014029439.1, ECO:0000313|RefSeq:XP_014029440.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|EMBL:ACI33876.1};
RN   [1] {ECO:0000313|EMBL:ACI33876.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33876.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RA   Leong J., von Schalburg K., Cooper G., Moore R., Holt R., Davidson W.S.,
RA   Koop B.F.;
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACI33876.1, ECO:0000313|RefSeq:NP_001133773.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33876.1};
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
RN   [3] {ECO:0000313|EMBL:ACI33876.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:ACI33876.1};
RG   cGRASP (B.F. Koop & W.S. Davidson);
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|RefSeq:NP_001133773.1, ECO:0000313|RefSeq:XP_014029439.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_014029439.1,
RC   ECO:0000313|RefSeq:XP_014029440.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC       presence of NADPH and glutathione reductase. Reduces low molecular
CC       weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549}.
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DR   EMBL; BT045614; ACI33876.1; -; mRNA.
DR   RefSeq; NP_001133773.1; NM_001140301.1.
DR   RefSeq; XP_014029439.1; XM_014173964.1.
DR   RefSeq; XP_014029440.1; XM_014173965.1.
DR   STRING; 8030.ENSSSAP00000066466; -.
DR   PaxDb; 8030-ENSSSAP00000066466; -.
DR   GeneID; 100195272; -.
DR   KEGG; sasa:100195272; -.
DR   OMA; IVVSQCH; -.
DR   OrthoDB; 1216362at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa25.
DR   Bgee; ENSSSAG00000059573; Expressed in head kidney and 15 other cell types or tissues.
DR   GO; GO:0047139; F:glutathione-homocystine transhydrogenase activity; IEA:UniProtKB-EC.
DR   CDD; cd04371; DEP; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR006869; DUF547.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR34386; GLUTAREDOXIN; 1.
DR   PANTHER; PTHR34386:SF1; GLUTAREDOXIN-LIKE PROTEIN NRDH; 1.
DR   Pfam; PF04784; DUF547; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087266}.
FT   DOMAIN          12..71
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   DOMAIN          287..413
FT                   /note="DUF547"
FT                   /evidence="ECO:0000259|Pfam:PF04784"
FT   REGION          99..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  54475 MW;  6E3DCB63042AE638 CRC64;
     MGETEGRVLG RVTVYSVLGC PHCVQAKTSL GRLGLPVWDV DMGKHPELRG SVKELTGRST
     VPQIFFNSVH IGGNDDLQEL LPEELERLVR LVREEPVLPE ALPLPEENQS DGSDTAEEAD
     GEFKCERDAL ANVVEDLKRS DVIGFQWRGL SMCRNSFTGA QLVGWLQKDR GMEMTKACET
     GQVLLDRKYM VGVAGAGKGE GFGVSDRLYR LMEHNPHSAL NAGQTAACSP LQTAELSAIL
     RDMILKLFSE YLSSDGKCVD YKAMSLSPVF ERYCELAVQL QRVELLSLTR EEKLAFFINT
     YNALVIHGNV RMGAPTNMWQ RYKFFNYVSY LIGGEVFTLQ DIENGVLRGN RKGVAQLLRP
     FSKTDPRLQV ALPDAEPLIH FALNCGAMGC PPIKTYTPQD IDSQLRTAAE SFLENDDGCV
     VDSEKGEVRL SQIFKWYKAD FGGTDEKLLN WILEHMGESP KRSSLQSVLS SGKIKVSYLP
     YDWSTNSSH
//
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