ID   A0A1R3IA58_COCAP        Unreviewed;       849 AA.
AC   A0A1R3IA58;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN   ORFNames=CCACVL1_13624 {ECO:0000313|EMBL:OMO79482.1};
OS   Corchorus capsularis (Jute).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX   NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO79482.1, ECO:0000313|Proteomes:UP000188268};
RN   [1] {ECO:0000313|EMBL:OMO79482.1, ECO:0000313|Proteomes:UP000188268}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC   TISSUE=Whole seedling {ECO:0000313|EMBL:OMO79482.1};
RA   Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA   Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA   Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT   "Corchorus capsularis genome sequencing.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protects cells and enzymes from oxidative damage, by
CC       catalyzing the reduction of hydrogen peroxide, lipid peroxides and
CC       organic hydroperoxide, by glutathione. {ECO:0000256|ARBA:ARBA00037287}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a hydroperoxy polyunsaturated fatty acid + 2 glutathione = a
CC         hydroxy polyunsaturated fatty acid + glutathione disulfide + H2O;
CC         Xref=Rhea:RHEA:19057, ChEBI:CHEBI:15377, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:58297, ChEBI:CHEBI:131871, ChEBI:CHEBI:134019;
CC         EC=1.11.1.12; Evidence={ECO:0000256|ARBA:ARBA00036974};
CC   -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC       {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC       {ECO:0000256|ARBA:ARBA00010271}.
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:OMO79482.1}.
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DR   EMBL; AWWV01010388; OMO79482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R3IA58; -.
DR   STRING; 210143.A0A1R3IA58; -.
DR   EnsemblPlants; OMO79482; OMO79482; CCACVL1_13624.
DR   Gramene; OMO79482; OMO79482; CCACVL1_13624.
DR   OrthoDB; 1428603at2759; -.
DR   Proteomes; UP000188268; Unassembled WGS sequence.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR040911; Exostosin_GT47.
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:SF118; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE 6, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF03016; Exostosin; 1.
DR   Pfam; PF00255; GSHPx; 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   Membrane {ECO:0000256|ARBA:ARBA00023136};
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:UP000188268};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          687..849
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   849 AA;  96726 MW;  3D1CB82DA8AD8391 CRC64;
     MSRGNFLEEK LQLPPTRKTR SRAMNRNTLH QKMAISMSKK KSKSSKKLEI QQQYHFSDSI
     LFKLLSRIPL AIFLLILVFI WSSSTTIISG KFVHVCVSSR KLNNLYCLSA GTQPNFDIPI
     PAFNHSSISP NISSSIKEAV NNVRVDPDPI FSNNVVNNNG SDGEIAIAVK VVEEQLQAQR
     SWISNKNHAA SCDGIGIYVY DLPSKFNKDL VGQCGDMIPW TNFCKYFSNE AMGEPIEKLG
     KGWYKTHQYA LELIFHTRIL KHPCRVYDEN AAKLFYVPYY GGLDILRWHF KNVSNDVKDT
     LALELVKWLE KKRPWIQNSG KDHVFVLGKI SWDFRRKSEE SWGTRLLELE QMQNSLKLLI
     ERQPWHINDI GIPHPTYFHP NSDNDIINWQ LKIMRSNRKS LVSFAGAARP EAPENIRSIL
     IDQCNSDEAK CRFLNCSSGK CDQPESVIEL FMESEFCLQP PGDSPTRKSV FDSLVSGCIP
     VLFDPFTAYY QYPWHLPEDH SKYSVFIDQE EVRKMKVNVV ERLMQVPVRE RDNMRSSHAQ
     NKKSPWAMTY SLMRRIVALF TSMTHQTCKH EKAPRGKTTF NTIVKARCEL HKQDLTKQSY
     KLKCKRFLVL TSNSMLCSPQ NLIRRNLSSV AISASLLFAK RFSPSSKPTL SSFPQISPVS
     LVSSSKETGF SRSFLGSLRF DHSMASQSAQ TSVHDFTVKD ARGKDVDLST YKGKVLLIVN
     VASQCGLTNS NYTELSQLYE KYKDQGFEIL AFPCNQFGGQ EPGNNEQILE FACTRFKAEY
     PIFDKVEVNG ANTAPIYKFL KSSKGGLFGD SIKWNFSKFL VDKDGNVVDR YAPTTSPLSI
     EKDIKKLLA
//