ID   PRDX3_RAT               Reviewed;         257 AA.
AC   Q9Z0V6; Q6P9W3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Thioredoxin-dependent peroxide reductase, mitochondrial;
DE            EC=1.11.1.15;
DE   AltName: Full=Peroxiredoxin-3;
DE            Short=PRX-3;
DE   AltName: Full=PRx III;
DE   Flags: Precursor;
GN   Name=Prdx3;
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   MEDLINE=99148808; PubMed=10025941; DOI=10.1016/S0014-5793(98)01736-0;
RA   Matsumoto A., Okado A., Fujii T., Fujii J., Egashira M., Niikawa N.,
RA   Taniguchi N.;
RT   "Cloning of the peroxiredoxin gene family in rats and characterization
RT   of the fourth member.";
RL   FEBS Lett. 443:246-250(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 171-208; 172-197 AND 209-239, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA   Lubec G., Afjehi-Sadat L.;
RL   Submitted (NOV-2006) to UniProtKB.
CC   -!- FUNCTION: Involved in redox regulation of the cell. Protects
CC       radical-sensitive enzymes from oxidative damage by a radical-
CC       generating system. Acts synergistically with MAP3K13 to regulate
CC       the activation of NF-kappa-B in the cytosol (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   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-109
CC       oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-230-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       109 (to Cys-SO(3)H) upon oxidative stress (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
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; AF106944; AAD17992.1; -; mRNA.
DR   EMBL; BC060567; AAH60567.1; -; mRNA.
DR   RefSeq; NP_071985.1; -.
DR   UniGene; Rn.2011; -.
DR   HSSP; P32119; 1QMV.
DR   SMR; Q9Z0V6; 64-224.
DR   PeroxiBase; 4507; Rno2CysPrx03.
DR   Ensembl; ENSRNOG00000010958; Rattus norvegicus.
DR   GeneID; 64371; -.
DR   KEGG; rno:64371; -.
DR   RGD; 620040; Prdx3.
DR   HOVERGEN; Q9Z0V6; -.
DR   NextBio; 613116; -.
DR   ArrayExpress; Q9Z0V6; -.
DR   GermOnline; ENSRNOG00000010958; Rattus norvegicus.
DR   GO; GO:0005739; C:mitochondrion; 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: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   1: Evidence at protein level;
KW   Antioxidant; Direct protein sequencing; Mitochondrion; Oxidoreductase;
KW   Peroxidase; Redox-active center; Transit peptide.
FT   TRANSIT       1     62       Mitochondrion (By similarity).
FT   CHAIN        63    257       Thioredoxin-dependent peroxide reductase,
FT                                mitochondrial (By similarity).
FT                                /FTId=PRO_0000256859.
FT   DOMAIN       64    222       Thioredoxin.
FT   ACT_SITE    109    109       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   DISULFID    109    109       Interchain (with C-229); in linked form
FT                                (By similarity).
FT   DISULFID    230    230       Interchain (with C-108); in linked form
FT                                (By similarity).
FT   CONFLICT    207    216       Missing (in Ref. 2; AAH60567).
FT   CONFLICT    232    232       A -> P (in Ref. 1; AAD17992).
SQ   SEQUENCE   257 AA;  28295 MW;  752198F5918206AE CRC64;
     MAAAAGRLLW SSVARPASTI FRSISASTVL RPVASRRTCL TDMLWSACPQ AKFAFSTSSS
     FHTPAVTQHA PHFKGTAVVN GEFKELSLDD FKGKYLVLFF YPLDFTFVCP TEIVAFSDKA
     NEFHDVNCEV VAVSVDSHFS HLAWINTPRK NGGLGHMNIT LLSDLTKQIS RDYGVLLESA
     GIALRGLFII DPNGVIKHLS VNDLPVGRSV EEPLRLVKAF QFVETHGEVC PANWTPESPT
     IKPSPTASKE YFEKVHQ
//