ID   PRDX2_PIG               Reviewed;         127 AA.
AC   P52552;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-NOV-2008, entry version 51.
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;
DE   Flags: Fragment;
GN   Name=PRDX2; Synonyms=TDPX1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
RX   MEDLINE=96327607; PubMed=8672129; DOI=10.1007/s003359900153;
RA   Winteroe A.K., Fredholm M., Davies W.;
RT   "Evaluation and characterization of a porcine small intestine cDNA
RT   library: analysis of 839 clones.";
RL   Mamm. Genome 7:509-517(1996).
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 (By similarity).
CC   -!- MISCELLANEOUS: The active site is the redox-active Cys-12 oxidized
CC       to Cys-SOH. Cys-SOH rapidly reacts with 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: Inactivated upon oxidative stress by overoxidation
CC       of Cys-12 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; F14561; CAA23125.1; -; mRNA.
DR   HSSP; P32119; 1QMV.
DR   SMR; P52552; 1-127.
DR   HOVERGEN; P52552; -.
DR   GO; GO:0005737; C:cytoplasm; 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   2: Evidence at transcript level;
KW   Antioxidant; Cytoplasm; Oxidoreductase; Peroxidase;
KW   Redox-active center.
FT   CHAIN        <1   >127       Peroxiredoxin-2.
FT                                /FTId=PRO_0000135082.
FT   DOMAIN       <1    125       Thioredoxin.
FT   ACT_SITE     12     12       Cysteine sulfenic acid (-SOH)
FT                                intermediate (By similarity).
FT   DISULFID     12     12       Interchain (with C-?); in linked form (By
FT                                similarity).
FT   NON_TER       1      1
FT   NON_TER     127    127
SQ   SEQUENCE   127 AA;  14168 MW;  1C05A9765EB69E84 CRC64;
     LFFYPLDFTF VCPTEIIAFS DRAEEFHQLG CEVLGVSVDX QXTHLAWINT PRKEGGLGPL
     KIPLLADVTR NLSLDYGVLK EDEGIAYRGL FIIDGKGVLR QITVNDLPVG RXVDEALRLV
     QGXQYTD
//