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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)

 PRDX6_MOUSE             Reviewed;         224 AA.
O08709; Q91WT2; Q9QWP4; Q9QWW0;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-JUN-2018, entry version 167.
RecName: Full=Peroxiredoxin-6;
EC=1.11.1.15;
AltName: Full=1-Cys peroxiredoxin;
Short=1-Cys PRX;
AltName: Full=Acidic calcium-independent phospholipase A2;
Short=aiPLA2;
EC=3.1.1.4;
AltName: Full=Antioxidant protein 2;
AltName: Full=Non-selenium glutathione peroxidase;
Short=NSGPx;
Name=Prdx6; Synonyms=Aop2, Ltw4, Prdx5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-26.
STRAIN=C3H/FEJ, C57BL/6J, and DBA/2J; TISSUE=Kidney, and Liver;
PubMed=9205120; DOI=10.1006/geno.1997.4762;
Iakoubova O.A., Pacella L.A., Her H., Beier D.R.;
"LTW4 protein on mouse chromosome 1 is a member of a family of
antioxidant proteins.";
Genomics 42:474-478(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Skin;
PubMed=9291135; DOI=10.1042/bj3260579;
Munz B., Frank S., Huebner G., Olsen E., Werner S.;
"A novel type of glutathione peroxidase: expression and regulation
during wound repair.";
Biochem. J. 326:579-585(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/SvJ, and C57BL/6J; TISSUE=Brain;
PubMed=10395907; DOI=10.1016/S0378-1119(99)00190-0;
Lee T.-H., Yu S.-L., Kim S.-U., Kim Y.-M., Choi I., Kang S.W.,
Rhee S.G., Yu D.-Y.;
"Characterization of the murine gene encoding 1-Cys peroxiredoxin and
identification of highly homologous genes.";
Gene 234:337-344(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Pituitary;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon;
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).
[6]
PROTEIN SEQUENCE OF 2-22; 25-53; 98-106; 109-122; 145-155 AND 163-182,
AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
Submitted (APR-2007) to UniProtKB.
[7]
INTERACTION WITH HTR2A.
PubMed=14988405; DOI=10.1074/jbc.M312106200;
Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
Dumuis A., Bockaert J., Marin P.;
"The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
of PDZ proteins.";
J. Biol. Chem. 279:20257-20266(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, VARIANT [LARGE SCALE
ANALYSIS] ALA-124, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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:0000250|UniProtKB:P30041}.
-!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
{ECO:0000250|UniProtKB:P30041}.
-!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
acylglycerophosphocholine + a carboxylate.
{ECO:0000250|UniProtKB:P30041}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with GSTP1; mediates
PRDX6 glutathionylation and regeneration (By similarity).
Interacts with APEX1. Interacts with STH. May interact with
FAM168B (By similarity). May interact with HTR2A
(PubMed:14988405). {ECO:0000250|UniProtKB:O77834,
ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:14988405}.
-!- INTERACTION:
P19157:Gstp1; NbExp=2; IntAct=EBI-444895, EBI-2309446;
O70145:Ncf2; NbExp=3; IntAct=EBI-444895, EBI-9550667;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35244}.
Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung
secretory organelles (lamellar bodies).
{ECO:0000250|UniProtKB:O35244}.
-!- TISSUE SPECIFICITY: Highly expressed in heart, kidney and liver.
Moderate expression in brain and stomach. Very low levels in
intestine.
-!- 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}.
-!- PTM: Phosphorylation at Thr-177 by MAP kinases increases the
phospholipase activity of the enzyme.
{ECO:0000250|UniProtKB:O35244}.
-!- 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:0000250|UniProtKB:O35244}.
-!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
{ECO:0000305}.
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EMBL; AF004670; AAC53277.1; -; mRNA.
EMBL; Y12883; CAA73383.1; -; mRNA.
EMBL; AF093852; AAC63376.1; -; mRNA.
EMBL; AF093853; AAC67553.1; -; Genomic_DNA.
EMBL; AF093857; AAD03716.1; -; Genomic_DNA.
EMBL; AF093854; AAD03716.1; JOINED; Genomic_DNA.
EMBL; AF093855; AAD03716.1; JOINED; Genomic_DNA.
EMBL; AF093856; AAD03716.1; JOINED; Genomic_DNA.
EMBL; AK030413; BAC26952.1; -; mRNA.
EMBL; BC013489; AAH13489.1; -; mRNA.
CCDS; CCDS15415.1; -.
RefSeq; NP_031479.1; NM_007453.4.
UniGene; Mm.186185; -.
ProteinModelPortal; O08709; -.
SMR; O08709; -.
BioGrid; 198118; 4.
IntAct; O08709; 9.
MINT; O08709; -.
STRING; 10090.ENSMUSP00000071636; -.
iPTMnet; O08709; -.
PhosphoSitePlus; O08709; -.
SwissPalm; O08709; -.
COMPLUYEAST-2DPAGE; O08709; -.
REPRODUCTION-2DPAGE; O08709; -.
SWISS-2DPAGE; O08709; -.
UCD-2DPAGE; O08709; -.
EPD; O08709; -.
MaxQB; O08709; -.
PaxDb; O08709; -.
PeptideAtlas; O08709; -.
PRIDE; O08709; -.
TopDownProteomics; O08709; -.
GeneID; 11758; -.
KEGG; mmu:11758; -.
CTD; 9588; -.
MGI; MGI:894320; Prdx6.
eggNOG; KOG0854; Eukaryota.
eggNOG; COG0450; LUCA.
HOVERGEN; HBG105234; -.
InParanoid; O08709; -.
KO; K11188; -.
BRENDA; 1.11.1.15; 3474.
ChiTaRS; Prdx6; mouse.
PRO; PR:O08709; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_PRDX5; -.
CleanEx; MM_PRDX6; -.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISO:MGI.
GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
GO; GO:0004601; F:peroxidase activity; IMP:MGI.
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; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0032060; P:bleb assembly; IMP:MGI.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0098869; P:cellular oxidant detoxification; ISO:MGI.
GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:MGI.
GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISO:MGI.
GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
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:0000269|PubMed:9205120,
ECO:0000269|Ref.6}.
CHAIN 2 224 Peroxiredoxin-6.
/FTId=PRO_0000135103.
DOMAIN 5 169 Thioredoxin. {ECO:0000255|PROSITE-
ProRule:PRU00691}.
REGION 31 40 Required and sufficient for targeting to
lysosomes and lamellar bodies.
{ECO:0000250|UniProtKB:O35244}.
ACT_SITE 47 47 Cysteine sulfenic acid (-SOH)
intermediate; for peroxidase activity.
{ECO:0000250|UniProtKB:P30041}.
ACT_SITE 140 140 For phospholipase activity.
{ECO:0000250|UniProtKB:O35244}.
SITE 32 32 Important for phospholipase activity.
{ECO:0000250|UniProtKB:O35244}.
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:0000244|PubMed:18034455}.
MOD_RES 93 93 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 177 177 Phosphothreonine; by MAPK.
{ECO:0000250|UniProtKB:O35244}.
MOD_RES 209 209 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P30041}.
MOD_RES 209 209 N6-succinyllysine; alternate.
{ECO:0000244|PubMed:23806337}.
VARIANT 124 124 D -> A (in strain: C57BL/6, C57BL/6J and
FVB/N). {ECO:0000244|PubMed:21183079}.
CONFLICT 154 154 G -> S (in Ref. 3; AAC67553).
{ECO:0000305}.
CONFLICT 181 181 W -> R (in Ref. 3; AAD03716).
{ECO:0000305}.
SEQUENCE 224 AA; 24871 MW; AECDEDD332858B8F CRC64;
MPGGLLLGDE APNFEANTTI GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE
FAKRNVKLIA LSIDSVEDHL AWSKDINAYN GETPTEKLPF PIIDDKGRDL AILLGMLDPV
EKDDNNMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT GTKPVATPVD
WKKGESVMVV PTLSEEEAKQ CFPKGVFTKE LPSGKKYLRY TPQP


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