ID PRDX6_RAT Reviewed; 224 AA. AC O35244; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 77. DE RecName: Full=Peroxiredoxin-6; DE EC=1.11.1.15; DE AltName: Full=Antioxidant protein 2; DE AltName: Full=1-Cys peroxiredoxin; DE Short=1-Cys PRX; DE AltName: Full=Acidic calcium-independent phospholipase A2; DE Short=aiPLA2; DE EC=3.1.1.-; DE AltName: Full=Non-selenium glutathione peroxidase; DE Short=NSGPx; DE EC=1.11.1.7; DE AltName: Full=Thiol-specific antioxidant protein; GN Name=Prdx6; Synonyms=Aipla2, Aop2, Tsa; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Lung; RA Kim T.-S., Feinstein S.I., Dodia C., Hennigan B.B., Fisher A.B.; RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Wistar; TISSUE=Olfactory epithelium; RA Andreeva S.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 2-41; 57-84; 98-118; 133-142; 156-162 AND 183-199, RP AND MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord; RA Lubec G., Afjehi-Sadat L., Chen W.-Q.; RL Submitted (APR-2007) to UniProtKB. RN [4] RP PROTEIN SEQUENCE OF 26-42 AND 146-163. RX MEDLINE=97153037; PubMed=8999971; DOI=10.1074/jbc.272.4.2542; RA Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., RA Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.; RT "Identification of a human cDNA clone for lysosomal type Ca2+- RT independent phospholipase A2 and properties of the expressed RT protein."; RL J. Biol. Chem. 272:2542-2550(1997). RN [5] RP ERRATUM. RA Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R., RA Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.; RL J. Biol. Chem. 272:10981-10981(1997). CC -!- FUNCTION: Involved in redox regulation of the cell. Can reduce CC H(2)O(2) and short chain organic, fatty acid, and phospholipid CC hydroperoxides. May play a role in the regulation of phospholipid CC turnover as well as in protection against oxidative injury. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC -!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O. CC -!- SUBUNIT: Homotetramer. May interact with HTR2A. Interacts with STH CC (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome. Note=Also found in lung CC secretory organelles. CC -!- MISCELLANEOUS: The active site is the redox-active Cys-47 oxidized CC to Cys-SOH. Cys-SOH may rapidly react with a Cys-SH of the other CC subunit to form an intermolecular disulfide with a concomitant CC homodimer formation. The enzyme may be subsequently regenerated by CC reduction of the disulfide by thioredoxin (By similarity). CC -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-47 CC (to Cys-SO(3)H) upon oxidative stress (By similarity). CC -!- SIMILARITY: Belongs to the ahpC/TSA family. Rehydrin subfamily. CC -!- SIMILARITY: Contains 1 thioredoxin domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF014009; AAB66341.1; -; mRNA. DR EMBL; Y17295; CAA76732.1; -; mRNA. DR IPI; IPI00231260; -. DR RefSeq; NP_446028.1; -. DR UniGene; Rn.42; -. DR HSSP; P30041; 1PRX. DR SMR; O35244; 5-224. DR PeroxiBase; 4427; Rno1CysPrx. DR PhosphoSite; O35244; -. DR PRIDE; O35244; -. DR Ensembl; ENSRNOG00000002896; Rattus norvegicus. DR GeneID; 94167; -. DR KEGG; rno:94167; -. DR RGD; 71005; Prdx6. DR HOVERGEN; O35244; -. DR OMA; O35244; TARVVFI. DR BRENDA; 1.11.1.15; 248. DR BRENDA; 1.11.1.7; 248. DR NextBio; 617808; -. DR ArrayExpress; O35244; -. DR GermOnline; ENSRNOG00000002896; Rattus norvegicus. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD. DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR000866; Alkyl_hydroperoxide_Rdtase. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR017936; Thioredoxin-like. DR InterPro; IPR012335; Thioredoxin_fold. DR Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 1: Evidence at protein level; KW Antioxidant; Cytoplasm; Direct protein sequencing; Disulfide bond; KW Hydrolase; Lipid degradation; Lysosome; Multifunctional enzyme; KW Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 224 Peroxiredoxin-6. FT /FTId=PRO_0000135104. FT DOMAIN 5 169 Thioredoxin. FT ACT_SITE 32 32 For phospholipase activity (By FT similarity). FT ACT_SITE 47 47 Cysteine sulfenic acid (-SOH) FT intermediate (By similarity). FT MOD_RES 44 44 Phosphothreonine (By similarity). FT MOD_RES 89 89 Phosphotyrosine (By similarity). FT DISULFID 47 47 Interchain; in linked form (By FT similarity). SQ SEQUENCE 224 AA; 24819 MW; EE41D9079A708FD9 CRC64; MPGGLLLGDE APNFEANTTI GHIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHF AWSKDINAYN GAAPTEKLPF PIIDDKDRDL AILLGMLDPA EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT ASNPVATPVD WKKGESVMVL PTLPEEEAKQ LFPKGVFTKE LPSGKKYLRY TPQP //