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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)

 PRDX6_RAT               Reviewed;         224 AA.
O35244;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 148.
RecName: Full=Peroxiredoxin-6;
EC=1.11.1.15 {ECO:0000269|PubMed:15004285};
AltName: Full=1-Cys peroxiredoxin;
Short=1-Cys PRX;
AltName: Full=Acidic calcium-independent phospholipase A2;
Short=aiPLA2;
EC=3.1.1.4 {ECO:0000269|PubMed:8999971};
AltName: Full=Antioxidant protein 2;
AltName: Full=Non-selenium glutathione peroxidase;
Short=NSGPx;
AltName: Full=Thiol-specific antioxidant protein;
Name=Prdx6; Synonyms=Aipla2, Aop2, Tsa;
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].
STRAIN=Sprague-Dawley; TISSUE=Lung;
Kim T.-S., Feinstein S.I., Dodia C., Hennigan B.B., Fisher A.B.;
Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Wistar; TISSUE=Olfactory epithelium;
Andreeva S.;
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-41; 57-84; 98-118; 133-142; 156-162 AND 183-199,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q.;
Submitted (APR-2007) to UniProtKB.
[4]
PROTEIN SEQUENCE OF 26-42 AND 146-163, FUNCTION, CATALYTIC ACTIVITY,
AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8999971; DOI=10.1074/jbc.272.4.2542;
Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R.,
Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.;
"Identification of a human cDNA clone for lysosomal type Ca2+-
independent phospholipase A2 and properties of the expressed
protein.";
J. Biol. Chem. 272:2542-2550(1997).
[5]
ERRATUM.
Kim T.-S., Sundaresh C.S., Feinstein S.I., Dodia C., Skach W.R.,
Jain M.K., Nagase T., Seki N., Ishikawa K., Nomura N., Fisher A.B.;
J. Biol. Chem. 272:10981-10981(1997).
[6]
FUNCTION, AND ACTIVATION BY GLUTATHIONE.
PubMed=15004285; DOI=10.1073/pnas.0400181101;
Manevich Y., Feinstein S.I., Fisher A.B.;
"Activation of the antioxidant enzyme 1-CYS peroxiredoxin requires
glutathionylation mediated by heterodimerization with pi GST.";
Proc. Natl. Acad. Sci. U.S.A. 101:3780-3785(2004).
[7]
FUNCTION, ACTIVE SITE, AND MUTAGENESIS OF HIS-26; SER-32 AND ASP-140.
PubMed=17652308; DOI=10.1194/jlr.M700299-JLR200;
Manevich Y., Reddy K.S., Shuvaeva T., Feinstein S.I., Fisher A.B.;
"Structure and phospholipase function of peroxiredoxin 6:
identification of the catalytic triad and its role in phospholipid
substrate binding.";
J. Lipid Res. 48:2306-2318(2007).
[8]
SUBCELLULAR LOCATION.
PubMed=19700648; DOI=10.1152/ajplung.00052.2009;
Sorokina E.M., Feinstein S.I., Milovanova T.N., Fisher A.B.;
"Identification of the amino acid sequence that targets peroxiredoxin
6 to lysosome-like structures of lung epithelial cells.";
Am. J. Physiol. 297:L871-L880(2009).
[9]
PHOSPHORYLATION AT THR-177 BY MAPK.
PubMed=19140803; DOI=10.1042/BJ20082061;
Wu Y., Feinstein S.I., Manevich Y., Chowdhury I., Pak J.H., Kazi A.,
Dodia C., Speicher D.W., Fisher A.B.;
"Mitogen-activated protein kinase-mediated phosphorylation of
peroxiredoxin 6 regulates its phospholipase A(2) activity.";
Biochem. J. 419:669-679(2009).
-!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction
of hydrogen peroxide and organic hydroperoxides to water and
alcohols, respectively. Can reduce H(2)O(2) and short chain
organic, fatty acid, and phospholipid hydroperoxides. Also has
phospholipase activity, and can therefore either reduce the
oxidized sn-2 fatty acyl grup of phospholipids (peroxidase
activity) or hydrolyze the sn-2 ester bond of phospholipids
(phospholipase activity). These activities are dependent on
binding to phospholipids at acidic pH and to oxidized phospholipds
at cytosolic pH. Plays a role in cell protection against oxidative
stress by detoxifying peroxides and in phospholipid homeostasis.
{ECO:0000269|PubMed:15004285, ECO:0000269|PubMed:17652308,
ECO:0000269|PubMed:8999971}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000269|PubMed:15004285}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
{ECO:0000269|PubMed:8999971}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.25 mM for dipalmitoyl phosphatidylcholine
{ECO:0000269|PubMed:8999971};
Vmax=1.89 nmol/h/mg enzyme for dipalmitoyl phosphatidylcholine
{ECO:0000269|PubMed:8999971};
pH dependence:
Optimum pH is 4 (for phospholipase activity).
{ECO:0000269|PubMed:8999971};
-!- SUBUNIT: Homodimer (By similarity). Interacts with GSTP1; mediates
PRDX6 glutathionylation and regeneration (Probable). Interacts
with APEX1. Interacts with STH. May interact with FAM168B (By
similarity). May interact with HTR2A (By similarity).
{ECO:0000250|UniProtKB:O08709, ECO:0000250|UniProtKB:P30041,
ECO:0000305|PubMed:15004285}.
-!- INTERACTION:
P62258:YWHAE (xeno); NbExp=2; IntAct=EBI-915490, EBI-356498;
P62259:Ywhae (xeno); NbExp=2; IntAct=EBI-915490, EBI-356480;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19700648}.
Lysosome {ECO:0000269|PubMed:19700648}. Note=Also found in lung
secretory organelles (lamellar bodies).
{ECO:0000269|PubMed:19700648}.
-!- PTM: Phosphorylation at Thr-177 by MAP kinases increases the
phospholipase activity of the enzyme.
{ECO:0000269|PubMed:19140803}.
-!- PTM: Irreversibly inactivated by overoxidation of Cys-47 to
sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms
upon oxidative stress. {ECO:0000250|UniProtKB:P30041}.
-!- 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 1-Cys peroxiredoxin, no C(R) is present and C(P)
instead forms a disulfide with a cysteine from another protein or
with a small thiol molecule. C(P) is reactivated by
glutathionylation mediated by glutathione S-transferase Pi,
followed by spontaneous reduction of the enzyme with glutathione.
{ECO:0000305|PubMed:15004285}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF014009; AAB66341.1; -; mRNA.
EMBL; Y17295; CAA76732.1; -; mRNA.
RefSeq; NP_446028.1; NM_053576.2.
UniGene; Rn.42; -.
ProteinModelPortal; O35244; -.
SMR; O35244; -.
BioGrid; 250165; 2.
IntAct; O35244; 4.
STRING; 10116.ENSRNOP00000030323; -.
PeroxiBase; 4427; Rno1CysPrx.
iPTMnet; O35244; -.
PhosphoSitePlus; O35244; -.
SwissPalm; O35244; -.
World-2DPAGE; 0004:O35244; -.
PaxDb; O35244; -.
PRIDE; O35244; -.
Ensembl; ENSRNOT00000034583; ENSRNOP00000030323; ENSRNOG00000002896.
GeneID; 94167; -.
KEGG; rno:94167; -.
UCSC; RGD:71005; rat.
CTD; 9588; -.
RGD; 71005; Prdx6.
eggNOG; KOG0854; Eukaryota.
eggNOG; COG0450; LUCA.
GeneTree; ENSGT00550000074794; -.
HOGENOM; HOG000022346; -.
HOVERGEN; HBG105234; -.
InParanoid; O35244; -.
KO; K11188; -.
OMA; YPIIADD; -.
OrthoDB; EOG091G0IWK; -.
PhylomeDB; O35244; -.
TreeFam; TF105183; -.
BRENDA; 1.11.1.15; 5301.
Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:O35244; -.
Proteomes; UP000002494; Chromosome 13.
Bgee; ENSRNOG00000002896; -.
Genevisible; O35244; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IEA:Ensembl.
GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IEA:Ensembl.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:RGD.
GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-EC.
GO; GO:0102567; F:phospholipase A2 activity (consuming 1,2-dipalmitoylphosphatidylcholine); IEA:UniProtKB-EC.
GO; GO:0102568; F:phospholipase A2 activity consuming 1,2-dioleoylphosphatidylethanolamine); IEA:UniProtKB-EC.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0046475; P:glycerophospholipid catabolic process; IEA:Ensembl.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:RGD.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
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; Hydrolase; Lipid degradation;
Lipid metabolism; Lysosome; Multifunctional enzyme; Oxidoreductase;
Peroxidase; Phosphoprotein; Redox-active center; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P30041}.
CHAIN 2 224 Peroxiredoxin-6.
/FTId=PRO_0000135104.
DOMAIN 5 169 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 31 40 Required and sufficient for targeting to
lysosomes and lamellar bodies.
{ECO:0000269|PubMed:19700648}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate; for peroxidase activity.
{ECO:0000269|PubMed:17652308}.
ACT_SITE 140 140 For phospholipase activity.
{ECO:0000305|PubMed:17652308}.
SITE 32 32 Important for phospholipase activity.
{ECO:0000305|PubMed:17652308}.
MOD_RES 44 44 Phosphothreonine.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 63 63 N6-acetyllysine.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 89 89 Phosphotyrosine.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 177 177 Phosphothreonine; by MAPK.
{ECO:0000269|PubMed:19140803}.
MOD_RES 209 209 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 209 209 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:O08709}.
MUTAGEN 26 26 H->A: Abolishes lipid binding.
{ECO:0000269|PubMed:17652308}.
MUTAGEN 32 32 S->A: Abolishes lipid binding.
{ECO:0000269|PubMed:17652308}.
MUTAGEN 140 140 D->A: Abolishes phospholipase activity,
but does not impair lipid binding.
{ECO:0000269|PubMed:17652308}.
SEQUENCE 224 AA; 24819 MW; EE41D9079A708FD9 CRC64;
MPGGLLLGDE APNFEANTTI GHIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE
FAKRNVKLIA LSIDSVEDHF AWSKDINAYN GAAPTEKLPF PIIDDKDRDL AILLGMLDPA
EKDEKGMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT ASNPVATPVD
WKKGESVMVL PTLPEEEAKQ LFPKGVFTKE LPSGKKYLRY TPQP


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