ID   PRDX6_MACFA             Reviewed;         224 AA.
AC   Q2PFL9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Peroxiredoxin-6;
DE            EC=1.11.1.15;
GN   Name=PRDX6; ORFNames=QtsA-11939;
OS   Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RA   Kobayashi M., Tanuma R., Hirata M., Osada N., Kusuda J., Sugano S.,
RA   Hashimoto K.;
RT   "Analysis of gene expression in cynomolgus monkey tissues by macaque
RT   cDNA oligo-chips.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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. May interact with HTR2A. Interacts with STH
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By
CC       similarity). Cytoplasmic vesicle (By similarity). Note=And also
CC       found in lung secretory organelles (By similarity).
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.
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DR   EMBL; AB220568; BAE73101.1; -; mRNA.
DR   SMR; Q2PFL9; 4-223, 5-224.
DR   PeroxiBase; 4430; Mfa1CysPrx.
DR   HOVERGEN; Q2PFL9; -.
DR   BRENDA; 1.11.1.15; 3438.
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_0000256860.
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;  25011 MW;  21304B97BD3B5F3E CRC64;
     MPGGLLLGDE APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE
     FAKRNVKLIA LSIDSVEDHL AWSKDTNAYN CEEPTEKLPF PIIDDKNRDL AILLGMLDPA
     EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD
     WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP
//