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Database: UniProt
Entry: E3MAZ2_CAERE
LinkDB: E3MAZ2_CAERE
Original site: E3MAZ2_CAERE 
ID   E3MAZ2_CAERE            Unreviewed;       223 AA.
AC   E3MAZ2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|ARBA:ARBA00012310, ECO:0000256|RuleBase:RU000499};
GN   ORFNames=CRE_16659 {ECO:0000313|EMBL:EFO97434.1}, FL81_01324
GN   {ECO:0000313|EMBL:POM50555.1}, GCK72_023325
GN   {ECO:0000313|EMBL:KAF1746867.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFO97434.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|EMBL:EFO97434.1};
RG   The Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:POM50555.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM50555.1};
RX   PubMed=26114425; DOI=10.1371/journal.pgen.1005323;
RA   Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA   Ahearne T.E., Cutter A.D., Phillips P.C.;
RT   "Reproductive Mode and the Evolution of Genome Size and Structure in
RT   Caenorhabditis Nematodes.";
RL   PLoS Genet. 11:e1005323-e1005323(2015).
RN   [4] {ECO:0000313|EMBL:POM50555.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM50555.1};
RX   PubMed=26394399; DOI=10.1371/journal.pgen.1005497;
RA   Fierst J.L., Willis J.H., Thomas C.G., Wang W., Reynolds R.M.,
RA   Ahearne T.E., Cutter A.D., Phillips P.C.;
RT   "Correction: Reproductive Mode and the Evolution of Genome Size and
RT   Structure in Caenorhabditis Nematodes.";
RL   PLoS Genet. 11:e1005497-e1005497(2015).
RN   [5] {ECO:0000313|EMBL:POM50555.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PX356 {ECO:0000313|EMBL:POM50555.1};
RA   Banno H., Chua N.-H.;
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:KAF1746867.1, ECO:0000313|Proteomes:UP000483820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX506 {ECO:0000313|EMBL:KAF1746867.1,
RC   ECO:0000313|Proteomes:UP000483820};
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KAF1746867.1};
RA   Teterina A.A., Willis J.H., Phillips P.C.;
RT   "Chromosome-level assembly of the Caenorhabditis remanei genome.";
RL   Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O;
CC         Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC         ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00000217};
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR   EMBL; DS268432; EFO97434.1; -; Genomic_DNA.
DR   EMBL; WUAV01000006; KAF1746867.1; -; Genomic_DNA.
DR   EMBL; LFJK02000005; POM50555.1; -; Genomic_DNA.
DR   RefSeq; XP_003106828.1; XM_003106780.1.
DR   AlphaFoldDB; E3MAZ2; -.
DR   STRING; 31234.E3MAZ2; -.
DR   EnsemblMetazoa; CRE16659.1; CRE16659.1; WBGene00081886.
DR   GeneID; 9809194; -.
DR   KEGG; crq:GCK72_023325; -.
DR   CTD; 9809194; -.
DR   eggNOG; KOG1651; Eukaryota.
DR   HOGENOM; CLU_029507_2_1_1; -.
DR   OMA; HELMNGI; -.
DR   OrthoDB; 67394at2759; -.
DR   Proteomes; UP000008281; Unassembled WGS sequence.
DR   Proteomes; UP000483820; Chromosome x.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000302; P:response to reactive oxygen species; IEA:EnsemblMetazoa.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR029759; GPX_AS.
DR   InterPro; IPR029760; GPX_CS.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF88; GLUTATHIONE PEROXIDASE-RELATED; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PIRSF; PIRSF000303; Glutathion_perox; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR   PROSITE; PS00763; GLUTATHIONE_PEROXID_2; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000499};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008281};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..223
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015089682"
FT   DOMAIN          34..219
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ   SEQUENCE   223 AA;  25838 MW;  23CEDD1F08DC34DC CRC64;
     MALWQLTLAA LFALAAAQPG PKMVDETTRW SQCRDTNQSI YDFQVETLQG EYTDLSQYRG
     QVLLMVNVAT FCAYTQQYTD FNPLIEKYQS QGFTLIAFPC NQFYLQEPAE NHELMNGIMY
     VRPGNGWKPH QNLHIYGKLE TNGENHHPIY EFVKESCPQT VDKIGKTDEL MYNPIRASDI
     TWNFEKFLID RNGQPRFRFH PTAWSHGDVV TPFIEQLLAE QAN
//
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