GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

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.
13-FEB-2019, entry version 151.
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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
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; 4.
IntAct; P35704; 3.
STRING; 10116.ENSRNOP00000004799; -.
PeroxiBase; 4477; Rno2CysPrx02.
iPTMnet; P35704; -.
PhosphoSitePlus; P35704; -.
SwissPalm; P35704; -.
World-2DPAGE; 0004:P35704; -.
jPOST; 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; -.
OrthoDB; 1326484at2759; -.
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:0045321; P:leukocyte activation; IBA:GO_Central.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0019430; P:removal of superoxide radicals; IBA:GO_Central.
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


Related products :

Catalog number Product name Quantity
E1123p ELISA kit Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123p ELISA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
U1123p CLIA Peroxiredoxin-2,Pig,PRDX2,Sus scrofa,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123m ELISA kit Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
E1123r ELISA kit Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123r ELISA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
U1123m CLIA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
U1123r CLIA Peroxiredoxin-2,Prdx2,Rat,Rattus norvegicus,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,TSA 96T
E1123m ELISA Mouse,Mus musculus,Peroxiredoxin-2,Prdx2,Tdpx1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide reductase 1,Tpx,TSA 96T
15-288-21018 Peroxiredoxin-2 - EC 1.11.1.15; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1; Thiol-specific antioxidant protein; TSA; PRP; Natural killer cell-enhancing factor B; NKEF-B Polyc 0.1 mg
15-288-21018 Peroxiredoxin-2 - EC 1.11.1.15; Thioredoxin peroxidase 1; Thioredoxin-dependent peroxide reductase 1; Thiol-specific antioxidant protein; TSA; PRP; Natural killer cell-enhancing factor B; NKEF-B Polyc 0.05 mg
E1123h ELISA Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide 96T
U1123h CLIA Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent peroxide r 96T
EIAAB32327 Antioxidant enzyme AOE372,Mouse,Mus musculus,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
EIAAB32326 Antioxidant enzyme AOE372,Peroxiredoxin IV,Peroxiredoxin-4,Prdx4,Prx-IV,Rat,Rattus norvegicus,Rno2CysPrx04,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
EIAAB32329 Antioxidant enzyme AOE372,AOE37-2,Homo sapiens,Human,Peroxiredoxin IV,Peroxiredoxin-4,PRDX4,Prx-IV,Thioredoxin peroxidase AO372,Thioredoxin-dependent peroxide reductase A0372
E1123h ELISA kit Homo sapiens,Human,Natural killer cell-enhancing factor B,NKEFB,NKEF-B,Peroxiredoxin-2,PRDX2,PRP,TDPX1,Thiol-specific antioxidant protein,Thioredoxin peroxidase 1,Thioredoxin-dependent pero 96T
E2222m Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
E2222m ELISA Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
U2222m CLIA Macrophage 23 kDa stress protein,Mouse,Msp23,Mus musculus,OSF-3,Osteoblast-specific factor 3,Paga,Peroxiredoxin-1,Prdx1,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E2222r HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2
U2222r CLIA HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E2222r ELISA HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
E2222r ELISA kit HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T
U2222r CLIA kit HBP23,Heme-binding 23 kDa protein,Peroxiredoxin-1,Prdx1,Rat,Rattus norvegicus,Tdpx2,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2 96T

Kits Elisa; taq POLYMERASE

Search in Google:

google

Share this page:
share on twitter rss feedsfacebookgoogle gentaur



Quick order!
Enter catalog number :


Gentaur; yes we can

Pathways :
WP2199: Seed Development
WP1493: Carbon assimilation C4 pathway
WP1566: Citrate cycle (TCA cycle)
WP1625: Base excision repair
WP1672: Mismatch repair
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair
WP1006: metapathway biotransformation
WP1049: G Protein Signaling Pathways
WP1090: Eicosanoid Synthesis
WP1124: metapathway biotransformation
WP1165: G Protein Signaling Pathways
WP1212: metapathway biotransformation
WP1251: metapathway biotransformation
WP1286: metapathway biotransformation
WP1318: Eicosanoid Synthesis
WP1371: G Protein Signaling Pathways
WP1403: AMPK signaling
WP1438: Influenza A virus infection
WP1461: Photosynthetic Carbon Reduction
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1619: Amino sugar and nucleotide sugar metabolism

Related Genes :
[Prdx6 Aipla2 Aop2 Tsa] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Thiol-specific antioxidant protein)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (HBC189) (Peroxiredoxin III) (Prx-III) (Peroxiredoxin-3) (Protein MER5 homolog)
[PRDX3 AOP1] Thioredoxin-dependent peroxide reductase, mitochondrial (EC 1.11.1.15) (Antioxidant protein 1) (AOP-1) (Peroxiredoxin-3) (Protein SP-22)
[PRX1 YBL064C YBL0503 YBL0524] Peroxiredoxin PRX1, mitochondrial (Prx) (EC 1.11.1.15) (1-Cys PRX) (Mitochondrial thiol peroxidase) (mTPx) (Thioredoxin peroxidase)
[PRXIIB TPX1 At1g65980 F12P19.14] Peroxiredoxin-2B (EC 1.11.1.15) (Peroxiredoxin IIB) (Peroxiredoxin TPx1) (Thioredoxin peroxidase 2B) (Thioredoxin-dependent peroxidase 1)
[Prdx6 Aop2 Ltw4 Prdx5] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx)
[PRDX6 AOP2 GPX PHGPX] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Ciliary body glutathione peroxidase) (Non-selenium glutathione peroxidase) (NSGPx) (PHGPx)
[ahpC b0605 JW0598] Alkyl hydroperoxide reductase C (EC 1.11.1.15) (Alkyl hydroperoxide reductase protein C22) (Peroxiredoxin) (SCRP-23) (Sulfate starvation-induced protein 8) (SSI8) (Thioredoxin peroxidase)
[PRDX6 AOP2 KIAA0106] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Liver 2D page spot 40) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12)
[ahpC Rv2428] Alkyl hydroperoxide reductase C (MtAhpC) (EC 1.11.1.15) (Peroxiredoxin) (Thioredoxin peroxidase)
[PRXIIF At3g06050 F24F17.3] Peroxiredoxin-2F, mitochondrial (EC 1.11.1.15) (Peroxiredoxin IIF) (Thioredoxin peroxidase 2F)
[tpx Rv1932 MTCY09F9.32c] Thiol peroxidase (Tpx) (EC 1.11.1.15) (Peroxiredoxin tpx) (Prx) (Thioredoxin peroxidase)
[HYR1 GPX3 ORP1 YIR037W] Glutathione peroxidase-like peroxiredoxin HYR1 (EC 1.11.1.15) (Glutathione peroxidase homolog 3) (GPx 3) (Hydrogen peroxide resistance protein 1) (Oxidant receptor peroxidase 1) (Phospholipid hydroperoxide glutathione peroxidase 3) (PHGPx3)
[PRXIIE At3g52960 F8J2_130] Peroxiredoxin-2E, chloroplastic (EC 1.11.1.15) (Peroxiredoxin IIE) (Thioredoxin peroxidase 2E)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[ahpE Rv2238c MTCY427.19c] Alkyl hydroperoxide reductase E (EC 1.11.1.15) (Peroxiredoxin AhpE) (Prx) (Thioredoxin peroxidase) (TPx)
[PRDX6 RCJMB04_18k11] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PER1 At1g48130 F21D18.15] 1-Cys peroxiredoxin PER1 (EC 1.11.1.15) (Rehydrin homolog) (Thioredoxin peroxidase)
[GPX2 YBR244W YBR1632] Glutathione peroxidase-like peroxiredoxin 2 (EC 1.11.1.15) (Glutathione peroxidase homolog 2) (GPx 2)
[] Peroxiredoxin-2 (Prx) (EC 1.11.1.15) (1-Cys D-peroxiredoxin) (Peroxiredoxin II) (Thioredoxin peroxidase)
[] Thioredoxin peroxidase (EC 1.11.1.15) (Peroxiredoxin) (Thiol-specific antioxidant protein) (Thioredoxin-dependent peroxide reductase)
[PRXIIC TPX2 At1g65970 F12P19.13] Peroxiredoxin-2C (EC 1.11.1.15) (Peroxiredoxin IIC) (Peroxiredoxin TPx2) (Thioredoxin peroxidase 2C) (Thioredoxin-dependent peroxidase 2)
[GPX1 YKL026C] Glutathione peroxidase-like peroxiredoxin 1 (EC 1.11.1.15) (Glutathione peroxidase homolog 1) (GPx 1)
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[PRDX6 QtsA-11939] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Non-selenium glutathione peroxidase) (NSGPx)
[] Genome polyprotein [Cleaved into: P3; Protein 3AB; P2; P1; Capsid protein VP0 (VP4-VP2); Capsid protein VP4 (P1A) (Virion protein 4); Capsid protein VP2 (P1B) (Virion protein 2); Capsid protein VP3 (P1C) (Virion protein 3); Capsid protein VP1 (P1D) (Virion protein 1); Protease 2A (P2A) (EC 3.4.22.29) (Picornain 2A) (Protein 2A); Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3A (P3A); Viral protein genome-linked (VPg) (Protein 3B) (P3B); Protein 3CD (EC 3.4.22.28); Protease 3C (P3C) (EC 3.4.22.28); RNA-directed RNA polymerase (RdRp) (EC 2.7.7.48) (3D polymerase) (3Dpol) (Protein 3D) (3D)]
[PRDX6] Peroxiredoxin-6 (EC 1.11.1.15) (1-Cys peroxiredoxin) (1-Cys PRX) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Non-selenium glutathione peroxidase) (NSGPx) (Fragments)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 1 (nsp1); Non-structural protein 2 (nsp2); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL1-PRO/PL2-PRO) (PLP1/PLP2) (Papain-like proteinases 1/2) (p195); Non-structural protein 4 (nsp4) (Peptide HD2); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10); Non-structural protein 11 (nsp11); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (p28); Non-structural protein 2 (nsp2) (p65); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL1-PRO/PL2-PRO) (PL1/PL2) (Papain-like proteinases 1/2) (p210); Non-structural protein 4 (nsp4) (Peptide HD2) (p44); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p27); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7) (p10); Non-structural protein 8 (nsp8) (p22); Non-structural protein 9 (nsp9) (p12); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p15); Non-structural protein 11 (nsp11)]
[DUOX2 LNOX2 THOX2] Dual oxidase 2 (EC 1.11.1.-) (EC 1.6.3.1) (Large NOX 2) (Long NOX 2) (NADH/NADPH thyroid oxidase p138-tox) (NADPH oxidase/peroxidase DUOX2) (NADPH thyroid oxidase 2) (Thyroid oxidase 2) (p138 thyroid oxidase)

Bibliography :
[29279589] DNA vaccination with a plasmid encoding LACK-TSA fusion against Leishmania major infection in BALB/c mice.
[28233451] Immunogenicity and efficacy of a bivalent DNA vaccine containing LeIF and TSA genes against murine cutaneous leishmaniasis.
[27283449] Cloning and characterization of thioredoxin peroxidases from Trichinella spiralis.
[25118246] Proteome-wide light/dark modulation of thiol oxidation in cyanobacteria revealed by quantitative site-specific redox proteomics.
[24056278] Characterization of a 2-Cys peroxiredoxin IV in Marsupenaeus japonicus (kuruma shrimp) and its role in the anti-viral immunity.
[23030526] Enhancement of immune response induced by DNA vaccine cocktail expressing complete LACK and TSA genes against Leishmania major.
[22102027] Expression, purification, crystallization and preliminary X-ray crystallographic studies of alkyl hydroperoxide reductase (AhpC) from the cyanobacterium Anabaena sp. PCC 7120.
[21822800] Antioxidant proteins TSA and PAG interact synergistically with Presenilin to modulate Notch signaling in Drosophila.
[19633316] Trichostatin A enhances proliferation and migration of vascular smooth muscle cells by downregulating thioredoxin 1.
[18191469] Trichostatin A regulates peroxiredoxin expression and virulence of the parasite Entamoeba histolytica.
?>