ID A0A9Y1YSP0_CHISP Unreviewed; 223 AA. AC A0A9Y1YSP0; DT 08-NOV-2023, integrated into UniProtKB/TrEMBL. DT 08-NOV-2023, sequence version 1. DT 29-MAY-2024, entry version 4. DE SubName: Full=Peroxiredoxin 6 {ECO:0000313|EMBL:WIR74294.1}; DE EC=1.11.1.24 {ECO:0000313|EMBL:WIR74294.1}; GN Name=Prx6 {ECO:0000313|EMBL:WIR74294.1}; OS Chilo suppressalis (Asiatic rice borer moth). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Pyraloidea; OC Crambidae; Crambinae; Chilo. OX NCBI_TaxID=168631 {ECO:0000313|EMBL:WIR74294.1}; RN [1] {ECO:0000313|EMBL:WIR74294.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=37282754; RA Mo W., Li Q., He X., Lu Z., Xu H., Zheng X., Guo J., Lu Y., Wang S.; RT "Identification and characterization of Prx5 and Prx6 in Chilo suppressalis RT in response to environmental stress."; RL Insect Biochem. 0:0-0(2023). RN [2] {ECO:0000313|EMBL:WIR74294.1} RP NUCLEOTIDE SEQUENCE. RA Lu Y.; RL Submitted (JAN-2023) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of CC hydrogen peroxide and organic hydroperoxides to water and alcohols, CC respectively. {ECO:0000256|PIRNR:PIRNR000239}. CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily. CC {ECO:0000256|ARBA:ARBA00025719}. 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; OQ230772; WIR74294.1; -; mRNA. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro. DR GO; GO:0045454; P:cell redox homeostasis; IEA:TreeGrafter. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:TreeGrafter. DR CDD; cd03016; PRX_1cys; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR045020; PRX_1cys. DR InterPro; IPR036249; Thioredoxin-like_sf. DR InterPro; IPR013766; Thioredoxin_domain. DR PANTHER; PTHR43503; MCG48959-RELATED; 1. DR PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 2: Evidence at transcript level; KW Antioxidant {ECO:0000256|ARBA:ARBA00022862, ECO:0000256|PIRNR:PIRNR000239}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000256|PIRNR:PIRNR000239}; KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR000239}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, KW ECO:0000256|PIRNR:PIRNR000239}. FT DOMAIN 2..166 FT /note="Thioredoxin" FT /evidence="ECO:0000259|PROSITE:PS51352" FT ACT_SITE 44 FT /note="Cysteine sulfenic acid (-SOH) intermediate; for FT peroxidase activity" FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1" SQ SEQUENCE 223 AA; 25145 MW; 864B42042214CB63 CRC64; MPLLGEEFPD FTANTTEGEI NFHEWVGKSW AILFSHPSDF TPVCTTELAR ILNLLPEFNK RNVKVIGLSC DTVSSHKEWC KDIKHYAGFN EDEKFPYPII EDKDRKVATL LGMVDKDELD TSGMPLTARA VFIIDANKKF RLSFLYPATT GRNFDEILRV IDSLQLTDKA KVATPVDWKM GDDCMVLPTL PEDQLSKVFP QGVTTVPVPS GKNYLKKTTC PKV //