ID   PRDX6_CHICK             Reviewed;         224 AA.
AC   Q5ZJF4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 41.
DE   RecName: Full=Peroxiredoxin-6;
DE            EC=1.11.1.15;
GN   Name=PRDX6; ORFNames=RCJMB04_18k11;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005).
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 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By
CC       similarity). Cytoplasmic vesicle (By similarity).
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-46 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-46
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; AJ720480; CAG32139.1; -; mRNA.
DR   IPI; IPI00577013; -.
DR   RefSeq; NP_001034418.1; -.
DR   UniGene; Gga.34325; -.
DR   SMR; Q5ZJF4; 3-222, 4-223.
DR   PeroxiBase; 4421; Gga1CysPrx.
DR   Ensembl; ENSGALG00000003053; Gallus gallus.
DR   GeneID; 429062; -.
DR   KEGG; gga:429062; -.
DR   HOVERGEN; Q5ZJF4; -.
DR   BRENDA; 1.11.1.15; 4.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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: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   2: Evidence at transcript level;
KW   Antioxidant; Cytoplasm; Cytoplasmic vesicle; 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_0000256863.
FT   DOMAIN        4    168       Thioredoxin.
FT   ACT_SITE     31     31       For phospholipase activity (By
FT                                similarity).
FT   ACT_SITE     46     46       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   MOD_RES      88     88       Phosphotyrosine (By similarity).
FT   DISULFID     46     46       Interchain; in linked form (By
FT                                similarity).
SQ   SEQUENCE   224 AA;  24977 MW;  4F2759FB44EC9493 CRC64;
     MPGLLLGDEA PNFEADTTQG GIRFHDFLGD SWGILFSHPR DFTPVCTTEL GRAAKLAPEF
     SKRNVKMIAL SIDSVPDHLA WSKDINAYNG DQPVEKLPFP IIADKDRELA VKLGMLDPDE
     RDKDGMPLTA RVVFIFGPDK KLKLSILYPA TTGRNFDEIL RVVDSLQLTA YKKVATPVDW
     KCGDSVMVVP TLPDEEAKKL FPKGVFTKDL PSGKKYLRYT PQPE
//