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-NOV-2011, entry version 101.
DE   RecName: Full=Peroxiredoxin-6;
DE            EC=1.11.1.15;
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=Antioxidant protein 2;
DE   AltName: Full=Non-selenium glutathione peroxidase;
DE            Short=NSGPx;
DE            EC=1.11.1.9;
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).
RN   [6]
RP   ACTIVATION BY GLUTATHIONE.
RX   PubMed=15004285; DOI=10.1073/pnas.0400181101;
RA   Manevich Y., Feinstein S.I., Fisher A.B.;
RT   "Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires
RT   glutathionylation mediated by heterodimerization with pi GST.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004).
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: 2 glutathione + H(2)O(2) = glutathione
CC       disulfide + 2 H(2)O.
CC   -!- SUBUNIT: Homotetramer. Interacts with GSTP1; mediates PRDX6
CC       glutathionylation and regeneration. May interact with HTR2A.
CC       Interacts with APEX1 and STH (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Lysosome. Cytoplasmic vesicle (By
CC       similarity). Note=Also found in lung secretory organelles.
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-47 oxidized
CC       to Cys-SOH. Unlike 2-Cys peroxiredoxins, PRDX6 conserves only this
CC       peroxidatic cysteine. To regenerate and activate the enzyme, the
CC       oxidized form is directly reduced to cysteine by glutathione and
CC       not thioredoxin.
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.
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DR   EMBL; AF014009; AAB66341.1; -; mRNA.
DR   EMBL; Y17295; CAA76732.1; -; mRNA.
DR   IPI; IPI00231260; -.
DR   RefSeq; NP_446028.1; NM_053576.2.
DR   UniGene; Rn.42; -.
DR   ProteinModelPortal; O35244; -.
DR   SMR; O35244; 5-224.
DR   IntAct; O35244; 1.
DR   STRING; O35244; -.
DR   PeroxiBase; 4427; Rno1CysPrx.
DR   PhosphoSite; O35244; -.
DR   World-2DPAGE; 0004:O35244; -.
DR   PRIDE; O35244; -.
DR   Ensembl; ENSRNOT00000034583; ENSRNOP00000030323; ENSRNOG00000002896.
DR   GeneID; 94167; -.
DR   KEGG; rno:94167; -.
DR   UCSC; NM_053576; rat.
DR   CTD; 9588; -.
DR   RGD; 71005; Prdx6.
DR   eggNOG; roNOG13330; -.
DR   GeneTree; ENSGT00550000074794; -.
DR   HOVERGEN; HBG105234; -.
DR   InParanoid; O35244; -.
DR   OMA; NYPILAD; -.
DR   OrthoDB; EOG4M399H; -.
DR   PhylomeDB; O35244; -.
DR   BRENDA; 1.11.1.15; 5301.
DR   NextBio; 617808; -.
DR   ArrayExpress; O35244; -.
DR   Genevestigator; O35244; -.
DR   GermOnline; ENSRNOG00000002896; Rattus norvegicus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:RGD.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   KO; K11188; -.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PIRSF; PIRSF000239; AHPC; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Antioxidant; Complete proteome; Cytoplasm;
KW   Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW   Hydrolase; Lipid degradation; Lysosome; Multifunctional enzyme;
KW   Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
KW   Reference proteome.
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      63     63       N6-acetyllysine (By similarity).
FT   MOD_RES      89     89       Phosphotyrosine (By similarity).
FT   MOD_RES     209    209       N6-acetyllysine (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
//