ID   PRDX2_RAT               Reviewed;         198 AA.
AC   P35704; Q6PDV3;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   04-NOV-2008, entry version 75.
DE   RecName: Full=Peroxiredoxin-2;
DE            EC=1.11.1.15;
DE   AltName: Full=Thioredoxin peroxidase 1;
DE   AltName: Full=Thioredoxin-dependent peroxide reductase 1;
DE   AltName: Full=Thiol-specific antioxidant protein;
DE            Short=TSA;
GN   Name=Prdx2; Synonyms=Tdpx1;
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   TISSUE=Brain;
RX   MEDLINE=94316629; PubMed=8041738;
RA   Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.;
RT   "Cloning and sequencing of thiol-specific antioxidant from mammalian
RT   brain: alkyl hydroperoxide reductase and thiol-specific antioxidant
RT   define a large family of antioxidant enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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 93-135 AND 140-157, AND MASS SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA   Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Involved in redox regulation of the cell. Reduces
CC       peroxides with reducing equivalents provided through the
CC       thioredoxin system. It is not able to receive electrons from
CC       glutaredoxin. May play an important role in eliminating peroxides
CC       generated during metabolism. Might participate in the signaling
CC       cascades of growth factors and tumor necrosis factor-alpha by
CC       regulating the intracellular concentrations of H(2)O(2).
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. Interacts
CC       with TIPIN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-51 oxidized
CC       to Cys-SOH. Cys-SOH rapidly reacts with Cys-172-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: Inactivated upon oxidative stress by overoxidation
CC       of Cys-51 to Cys-SO(2)H and Cys-SO(3)H. Cys-SO(2)H is retroreduced
CC       to Cys-SOH after removal of H(2)O(2), while Cys-SO(3)H may be
CC       irreversibly oxidized (By similarity).
CC   -!- SIMILARITY: Belongs to the ahpC/TSA family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; U06099; AAA19959.1; -; mRNA.
DR   EMBL; BC058481; AAH58481.1; -; mRNA.
DR   PIR; A57716; A57716.
DR   RefSeq; NP_058865.1; -.
DR   UniGene; Rn.2511; -.
DR   HSSP; P32119; 1QMV.
DR   SMR; P35704; 2-197, 3-198.
DR   PeroxiBase; 4477; Rno2CysPrx02.
DR   PhosphoSite; P35704; -.
DR   Ensembl; ENSRNOG00000003520; Rattus norvegicus.
DR   GeneID; 29338; -.
DR   KEGG; rno:29338; -.
DR   RGD; 3838; Prdx2.
DR   HOVERGEN; P35704; -.
DR   NextBio; 608824; -.
DR   ArrayExpress; P35704; -.
DR   GermOnline; ENSRNOG00000003520; Rattus norvegicus.
DR   GO; GO:0005737; C:cytoplasm; 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   1: Evidence at protein level;
KW   Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing;
KW   Oxidoreductase; Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    198       Peroxiredoxin-2.
FT                                /FTId=PRO_0000135083.
FT   DOMAIN        6    164       Thioredoxin.
FT   ACT_SITE     51     51       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   DISULFID     51     51       Interchain (with C-172); in linked form
FT                                (By similarity).
FT   DISULFID    172    172       Interchain (with C-51); in linked form
FT                                (By similarity).
FT   CONFLICT     17     17       G -> A (in Ref. 2; AAH58481).
SQ   SEQUENCE   198 AA;  21784 MW;  FC6AD9B0E9C4447B CRC64;
     MASGNAHIGK PAPDFTGTAV VDGAFKEIKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSD
     HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTKS LSQNYGVLKN
     DEGIAYRGLF IIDAKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
     DTIKPNVDDS KEYFSKHN
//