ID Q1PBM0_9TREM Unreviewed; 191 AA. AC Q1PBM0; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 2. DT 22-FEB-2023, entry version 64. DE SubName: Full=Phospholipid hydroperoxide glutathione peroxidase isoform 2 {ECO:0000313|EMBL:ABE68812.1}; GN Name=GPx2 {ECO:0000313|EMBL:ABE68812.1}; OS Paragonimus westermani. OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda; OC Digenea; Plagiorchiida; Troglotremata; Troglotrematidae; Paragonimus. OX NCBI_TaxID=34504 {ECO:0000313|EMBL:ABE68812.1}; RN [1] {ECO:0000313|EMBL:ABE68812.1} RP NUCLEOTIDE SEQUENCE. RA Bae Y.-A., Cai G.-B., Kong Y.; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ABE68812.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19344533; DOI=10.1186/1471-2148-9-72; RA Bae Y.A., Cai G.B., Kim S.H., Zo Y.G., Kong Y.; RT "Modular evolution of glutathione peroxidase genes in association with RT different biochemical properties of their encoded proteins in invertebrate RT animals."; RL BMC Evol. Biol. 9:72-72(2009). RN [3] {ECO:0000313|EMBL:ABE68812.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19265561; DOI=10.1017/S0031182009005654; RA Kim S.H., Cai G.B., Bae Y.A., Lee E.G., Lee Y.S., Kong Y.; RT "Two novel phospholipid hydroperoxide glutathione peroxidase genes of RT Paragonimus westermani induced by oxidative stress."; RL Parasitology 136:553-565(2009). CC -!- SIMILARITY: Belongs to the glutathione peroxidase family. CC {ECO:0000256|ARBA:ARBA00006926}. 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; DQ454160; ABE68812.1; -; Genomic_DNA. DR BRENDA; 1.11.1.9; 10163. 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; IPR029759; GPX_AS. DR InterPro; IPR029760; GPX_CS. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1. DR PANTHER; PTHR11592:SF78; PHOSPHOLIPID HYDROPEROXIDE GLUTATHIONE PEROXIDASE; 1. DR Pfam; PF00255; GSHPx; 1. DR PIRSF; PIRSF000303; Glutathion_perox; 1. 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. PE 3: Inferred from homology; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:ABE68812.1}; KW Selenium {ECO:0000313|EMBL:ABE68812.1}; KW Selenocysteine {ECO:0000313|EMBL:ABE68812.1}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..18 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 19..191 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004195433" FT REGION 170..191 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 65 FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1" FT NON_STD 65 FT /note="Selenocysteine" FT /evidence="ECO:0000313|EMBL:ABE68812.1" SQ SEQUENCE 191 AA; 21685 MW; 25A718558993E6C8 CRC64; MGSSFGLLIG LIALTVYSLP NRDADSIASK TSIYDFNATD IDGNLVNLSK YRNKVCIIVN VASNUGLADL NYRQLQALYI QHAADGLCIL AFPSNQFLNL EPGTDEEIKQ HVTDKYNITF HLFRKIDVNG DHTIPLYRYL KKKLPGYQPN GAIEYNYVKF LIDRKGIPRE RFPSSTPPMK MEKSIQRMLS Q //