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Peroxiredoxin-2 (EC 1.11.1.15) (Thiol-specific antioxidant protein) (TSA) (Thioredoxin peroxidase 1) (Thioredoxin-dependent peroxide reductase 1)

 PRDX2_RAT               Reviewed;         198 AA.
P35704; Q6PDV3;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 149.
RecName: Full=Peroxiredoxin-2;
EC=1.11.1.15;
AltName: Full=Thiol-specific antioxidant protein;
Short=TSA;
AltName: Full=Thioredoxin peroxidase 1;
AltName: Full=Thioredoxin-dependent peroxide reductase 1;
Name=Prdx2; Synonyms=Tdpx1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8041738; DOI=10.1073/pnas.91.15.7017;
Chae H.Z., Robison K., Poole L.B., Church G., Storz G., Rhee S.G.;
"Cloning and sequencing of thiol-specific antioxidant from mammalian
brain: alkyl hydroperoxide reductase and thiol-specific antioxidant
define a large family of antioxidant enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 91:7017-7021(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pituitary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 93-135 AND 140-157, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Plays a role in cell protection against
oxidative stress by detoxifying peroxides and as sensor of
hydrogen peroxide-mediated signaling events. Might participate in
the signaling cascades of growth factors and tumor necrosis
factor-alpha by regulating the intracellular concentrations of
H(2)O(2). {ECO:0000250|UniProtKB:P32119}.
-!- CATALYTIC ACTIVITY:
Reaction=[protein]-dithiol + an hydroperoxide = [protein]-
disulfide + an alcohol + H2O; Xref=Rhea:RHEA:10008, Rhea:RHEA-
COMP:10593, Rhea:RHEA-COMP:10594, ChEBI:CHEBI:15377,
ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924,
ChEBI:CHEBI:50058; EC=1.11.1.15;
Evidence={ECO:0000250|UniProtKB:P32119};
-!- SUBUNIT: Homodimer; disulfide-linked, upon oxidation. 5 homodimers
assemble to form a ring-like decamer. Interacts with TIPIN.
{ECO:0000250|UniProtKB:P32119}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32119}.
-!- PTM: The enzyme can be inactivated by further oxidation of the
cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H)
instead of its condensation to a disulfide bond. It can be
reactivated by forming a transient disulfide bond with
sulfiredoxin SRXN1, which reduces the cysteine sulfinic acid in an
ATP- and Mg-dependent manner. {ECO:0000250|UniProtKB:P32119,
ECO:0000250|UniProtKB:Q06830}.
-!- MISCELLANEOUS: The active site is a conserved redox-active
cysteine residue, the peroxidatic cysteine (C(P)), which makes the
nucleophilic attack on the peroxide substrate. The peroxide
oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which
then reacts with another cysteine residue, the resolving cysteine
(C(R)), to form a disulfide bridge. The disulfide is subsequently
reduced by an appropriate electron donor to complete the catalytic
cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by
the other dimeric subunit to form an intersubunit disulfide. The
disulfide is subsequently reduced by thioredoxin.
{ECO:0000250|UniProtKB:P32119}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1
subfamily. {ECO:0000305}.
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EMBL; U06099; AAA19959.1; -; mRNA.
EMBL; BC058481; AAH58481.1; -; mRNA.
PIR; A57716; A57716.
RefSeq; NP_058865.1; NM_017169.1.
RefSeq; XP_006255306.1; XM_006255244.1.
UniGene; Rn.2511; -.
ProteinModelPortal; P35704; -.
SMR; P35704; -.
BioGrid; 247997; 3.
IntAct; P35704; 3.
STRING; 10116.ENSRNOP00000004799; -.
PeroxiBase; 4477; Rno2CysPrx02.
iPTMnet; P35704; -.
PhosphoSitePlus; P35704; -.
SwissPalm; P35704; -.
World-2DPAGE; 0004:P35704; -.
PaxDb; P35704; -.
PRIDE; P35704; -.
GeneID; 29338; -.
KEGG; rno:29338; -.
CTD; 7001; -.
RGD; 3838; Prdx2.
eggNOG; KOG0852; Eukaryota.
eggNOG; COG0450; LUCA.
HOGENOM; HOG000022343; -.
HOVERGEN; HBG000286; -.
InParanoid; P35704; -.
KO; K03386; -.
PhylomeDB; P35704; -.
TreeFam; TF105181; -.
BRENDA; 1.11.1.15; 5301.
PRO; PR:P35704; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0008379; F:thioredoxin peroxidase activity; IBA:GO_Central.
GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
InterPro; IPR000866; AhpC/TSA.
InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
InterPro; IPR019479; Peroxiredoxin_C.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
Pfam; PF10417; 1-cysPrx_C; 1.
Pfam; PF00578; AhpC-TSA; 1.
PIRSF; PIRSF000239; AHPC; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
Acetylation; Antioxidant; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Oxidoreductase; Peroxidase;
Phosphoprotein; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P32119}.
CHAIN 2 198 Peroxiredoxin-2.
/FTId=PRO_0000135083.
DOMAIN 6 164 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
ACT_SITE 51 51 Cysteine sulfenic acid (-SOH)
intermediate.
{ECO:0000250|UniProtKB:P32119}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P32119}.
MOD_RES 112 112 Phosphoserine.
{ECO:0000250|UniProtKB:P32119}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000250|UniProtKB:P32119}.
DISULFID 51 51 Interchain (with C-172); in linked form.
{ECO:0000250|UniProtKB:P32119}.
DISULFID 172 172 Interchain (with C-51); in linked form.
{ECO:0000250|UniProtKB:P32119}.
CONFLICT 17 17 G -> A (in Ref. 2; AAH58481).
{ECO:0000305}.
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


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