ID   PRDX2_CRIGR             Reviewed;         198 AA.
AC   Q8K3U7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   16-JUN-2009, entry version 39.
DE   RecName: Full=Peroxiredoxin-2;
DE            EC=1.11.1.15;
GN   Name=PRDX2;
OS   Cricetulus griseus (Chinese hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Keightley J.A., Shang L., Kinter M.;
RT   "2D Gel analysis of the proteomic adaptation of a mammalian cell line
RT   to oxidative stress reveals changes in the expression of metabolically
RT   relevant enzymes.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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) (By
CC       similarity).
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-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; AF532110; AAM95673.1; -; mRNA.
DR   HSSP; P32119; 1QMV.
DR   SMR; Q8K3U7; 2-197, 3-198.
DR   HOVERGEN; Q8K3U7; -.
DR   BRENDA; 1.11.1.15; 18.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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   Acetylation; Antioxidant; Cytoplasm; Disulfide bond; Oxidoreductase;
KW   Peroxidase; Redox-active center.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    198       Peroxiredoxin-2.
FT                                /FTId=PRO_0000256855.
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).
SQ   SEQUENCE   198 AA;  21813 MW;  5A11BF0B70F27B4C CRC64;
     MASGNAHIGK PAPDFTATAV VDGAFKEVKL SDYRGKYVVL FFYPLDFTFV CPTEIIAFSN
     HAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRS LSENYGVLKT
     DEGIAYRGLF IIDAKGILRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS
     DTIKPNVDDS KEYFSKHN
//