ID   PRDX3_PONAB             Reviewed;         256 AA.
AC   Q5REY3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   04-NOV-2008, entry version 29.
DE   RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
DE            EC=1.11.1.15;
DE   AltName: Full=Peroxiredoxin-3;
DE   Flags: Precursor;
GN   Name=PRDX3;
OS   Pongo abelii (Sumatran orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in redox regulation of the cell. Protects
CC       radical-sensitive enzymes from oxidative damage by a radical-
CC       generating system (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation (By
CC       similarity). Binds MAP3K13 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-108
CC       oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-229-SH of the
CC       other subunit to form an intermolecular disulfide with a
CC       concomitant homodimer formation. The enzyme may be subsequently
CC       regenerated by reduction of the disulfide by thioredoxin (By
CC       similarity).
CC   -!- MISCELLANEOUS: Irreversibly inactivated by overoxidation of Cys-
CC       108 (to Cys-SO(3)H) upon oxidative stress (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; CR857380; CAH89674.1; -; mRNA.
DR   RefSeq; NP_001127184.1; -.
DR   SMR; Q5REY3; 63-223.
DR   PeroxiBase; 4500; Ppy2CysPrx03.
DR   GeneID; 100174238; -.
DR   HOVERGEN; Q5REY3; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000866; AhpC-TSA.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Antioxidant; Mitochondrion; Oxidoreductase; Peroxidase;
KW   Redox-active center; Transit peptide.
FT   TRANSIT       1     62       Mitochondrion (By similarity).
FT   CHAIN        63    256       Thioredoxin-dependent peroxide reductase,
FT                                mitochondrial (By similarity).
FT                                /FTId=PRO_0000256858.
FT   DOMAIN       63    221       Thioredoxin.
FT   ACT_SITE    108    108       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   DISULFID    108    108       Interchain (with C-229); in linked form
FT                                (By similarity).
FT   DISULFID    229    229       Interchain (with C-108); in linked form
FT                                (By similarity).
SQ   SEQUENCE   256 AA;  27700 MW;  BF425B99C7794406 CRC64;
     MAAAVGRLLR ASVARGVSAI PWGISATAAL RPAACGRTSL TNLLCSGSSQ AKLFSTSSSY
     HAPAVTQHAP YFKGTAVVNG EFKDLSLDDF KGKYLVLFFY PLDFTFVCPT EIVAFSDKAN
     EFHDVNCEVV AVSVDSHFSH LAWINTPRKN GGLGHMNIAL LSDLTKQISR DYGVLLEGSG
     LALRGLFIID PNGVIKHLSV NDLPVGRSVE ETLRLVKAFQ YVETHGEVCP ANWTPDSPTI
     KPNPAASKEY FQKVNQ
//