ID   A0A2G8KJV3_STIJA        Unreviewed;       234 AA.
AC   A0A2G8KJV3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=BSL78_14859 {ECO:0000313|EMBL:PIK48283.1};
OS   Stichopus japonicus (Sea cucumber).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC   Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX   NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK48283.1, ECO:0000313|Proteomes:UP000230750};
RN   [1] {ECO:0000313|EMBL:PIK48283.1, ECO:0000313|Proteomes:UP000230750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Shaxun {ECO:0000313|EMBL:PIK48283.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PIK48283.1};
RX   PubMed=29023486;
RA   Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA   Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA   Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA   Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT   "The sea cucumber genome provides insights into morphological evolution and
RT   visceral regeneration.";
RL   PLoS Biol. 15:E2003790-E2003790(2017).
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PIK48283.1}.
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DR   EMBL; MRZV01000531; PIK48283.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8KJV3; -.
DR   SMR; A0A2G8KJV3; -.
DR   STRING; 307972.A0A2G8KJV3; -.
DR   Proteomes; UP000230750; Unassembled WGS sequence.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd00340; GSH_Peroxidase; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR000889; Glutathione_peroxidase.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR   PANTHER; PTHR11592:SF88; GLUTATHIONE PEROXIDASE; 1.
DR   Pfam; PF00255; GSHPx; 1.
DR   PRINTS; PR01011; GLUTPROXDASE.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 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:UP000230750};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..234
FT                   /note="Glutathione peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013721858"
SQ   SEQUENCE   234 AA;  26537 MW;  73F08AB6DD055968 CRC64;
     MVTKLFFITL WWLPVGSGHP AEMSSYCHTG ANSIHGYTLV PLDGGEETPL SLYEGKVLII
     VNVASFCQYT SQYLDFNELK NIAELEGKIE VIGVPSNQFG LQEPGANGEE IRNSLKYVRP
     GNSFEPDFDL FEKCDVNGAN EIALFTALKR ACPAVKEEIG DPAIRFWSPF KNNDITWNFN
     KFLIGPDGTP LKRYDSEVEP FDLLDDIHDV LIETKKIEKR KNYNEEEFED LLFI
//