PRDX6_MOUSE
ID PRDX6_MOUSE Reviewed; 224 AA.
AC O08709; Q91WT2; Q9QWP4; Q9QWW0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Peroxiredoxin-6;
DE EC=1.11.1.27 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=1-Cys peroxiredoxin;
DE Short=1-Cys PRX;
DE AltName: Full=Acidic calcium-independent phospholipase A2;
DE Short=aiPLA2;
DE EC=3.1.1.4 {ECO:0000269|PubMed:26830860};
DE AltName: Full=Antioxidant protein 2;
DE AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Lysophosphatidylcholine acyltransferase 5 {ECO:0000303|PubMed:26830860};
DE Short=LPC acyltransferase 5;
DE Short=LPCAT-5;
DE Short=Lyso-PC acyltransferase 5;
DE EC=2.3.1.23 {ECO:0000269|PubMed:26830860};
DE AltName: Full=Non-selenium glutathione peroxidase;
DE Short=NSGPx;
GN Name=Prdx6; Synonyms=Aop2, Ltw4, Prdx5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-26.
RC STRAIN=C3H/FEJ, C57BL/6J, and DBA/2J; TISSUE=Kidney, and Liver;
RX PubMed=9205120; DOI=10.1006/geno.1997.4762;
RA Iakoubova O.A., Pacella L.A., Her H., Beier D.R.;
RT "LTW4 protein on mouse chromosome 1 is a member of a family of antioxidant
RT proteins.";
RL Genomics 42:474-478(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Skin;
RX PubMed=9291135; DOI=10.1042/bj3260579;
RA Munz B., Frank S., Huebner G., Olsen E., Werner S.;
RT "A novel type of glutathione peroxidase: expression and regulation during
RT wound repair.";
RL Biochem. J. 326:579-585(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ, and C57BL/6J; TISSUE=Brain;
RX PubMed=10395907; DOI=10.1016/s0378-1119(99)00190-0;
RA Lee T.-H., Yu S.-L., Kim S.-U., Kim Y.-M., Choi I., Kang S.W., Rhee S.G.,
RA Yu D.-Y.;
RT "Characterization of the murine gene encoding 1-Cys peroxiredoxin and
RT identification of highly homologous genes.";
RL Gene 234:337-344(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-22; 25-53; 98-106; 109-122; 145-155 AND 163-182, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (APR-2007) to UniProtKB.
RN [7]
RP INTERACTION WITH HTR2A.
RX PubMed=14988405; DOI=10.1074/jbc.m312106200;
RA Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N., Dumuis A.,
RA Bockaert J., Marin P.;
RT "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets of
RT PDZ proteins.";
RL J. Biol. Chem. 279:20257-20266(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, VARIANT [LARGE SCALE
RP ANALYSIS] ALA-124, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP HIS-26; ASP-31; SER-32; CYS-47 AND ASP-140.
RX PubMed=26830860; DOI=10.1194/jlr.m064758;
RA Fisher A.B., Dodia C., Sorokina E.M., Li H., Zhou S., Raabe T.,
RA Feinstein S.I.;
RT "A novel lysophosphatidylcholine acyl transferase activity is expressed by
RT peroxiredoxin 6.";
RL J. Lipid Res. 57:587-596(2016).
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively (By similarity). Can reduce H(2)O(2) and short chain
CC organic, fatty acid, and phospholipid hydroperoxides (By similarity).
CC Has phospholipase activity (PubMed:26830860). Can either reduce the
CC oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity)
CC or hydrolyze the sn-2 ester bond of phospholipids (phospholipase
CC activity) (By similarity). These activities are dependent on binding to
CC phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH
CC (By similarity). Plays a role in cell protection against oxidative
CC stress by detoxifying peroxides and in phospholipid homeostasis (By
CC similarity). Exhibits acyl-CoA-dependent lysophospholipid
CC acyltransferase which mediates the conversion of
CC lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC)
CC into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC)
CC (PubMed:26830860). Shows a clear preference for LPC as the
CC lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By
CC similarity). {ECO:0000250|UniProtKB:P30041,
CC ECO:0000269|PubMed:26830860}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + 2 glutathione = an alcohol + glutathione
CC disulfide + H2O; Xref=Rhea:RHEA:62632, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58297; EC=1.11.1.27;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:26830860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000269|PubMed:26830860};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + hexadecanoyl-CoA
CC = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + CoA;
CC Xref=Rhea:RHEA:35983, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35984;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:P30041};
CC -!- ACTIVITY REGULATION: MJ33 or lithium;[(2R)-1-hexadecoxy-3-(2,2,2-
CC trifluoroethoxy)propan-2-yl] methyl phosphate inhibits its
CC phospholipase A2 activity (PubMed:26830860). CI-976 or 2,2-Dimethyl-N-
CC (2,4,6-trimethoxyphenyl)dodecanamide inhibits its
CC lysophosphatidylcholine acyltransferase activity (PubMed:26830860).
CC {ECO:0000269|PubMed:26830860}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with GSTP1; mediates
CC PRDX6 glutathionylation and regeneration (By similarity). Interacts
CC with APEX1. Interacts with STH. May interact with FAM168B (By
CC similarity). May interact with HTR2A (PubMed:14988405).
CC {ECO:0000250|UniProtKB:O77834, ECO:0000250|UniProtKB:P30041,
CC ECO:0000269|PubMed:14988405}.
CC -!- INTERACTION:
CC O08709; O70145: Ncf2; NbExp=3; IntAct=EBI-444895, EBI-9550667;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O35244}.
CC Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung
CC secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, kidney and liver.
CC Moderate expression in brain and stomach. Very low levels in intestine.
CC -!- PTM: Irreversibly inactivated by overoxidation of Cys-47 to sulfinic
CC acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative
CC stress. {ECO:0000250|UniProtKB:P30041}.
CC -!- PTM: Phosphorylation at Thr-177 by MAP kinases increases the
CC phospholipase activity of the enzyme (By similarity). The
CC phosphorylated form exhibits a greater lysophosphatidylcholine
CC acyltransferase activity compared to the non-phosphorylated form (By
CC similarity). {ECO:0000250|UniProtKB:O35244}.
CC -!- MISCELLANEOUS: The active site is a conserved redox-active cysteine
CC residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic
CC attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to
CC cysteine sulfenic acid (C(P)-SOH), which then reacts with another
CC cysteine residue, the resolving cysteine (C(R)), to form a disulfide
CC bridge. The disulfide is subsequently reduced by an appropriate
CC electron donor to complete the catalytic cycle. In this 1-Cys
CC peroxiredoxin, no C(R) is present and C(P) instead forms a disulfide
CC with a cysteine from another protein or with a small thiol molecule.
CC C(P) is reactivated by glutathionylation mediated by glutathione S-
CC transferase Pi, followed by spontaneous reduction of the enzyme with
CC glutathione. {ECO:0000250|UniProtKB:O35244}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF004670; AAC53277.1; -; mRNA.
DR EMBL; Y12883; CAA73383.1; -; mRNA.
DR EMBL; AF093852; AAC63376.1; -; mRNA.
DR EMBL; AF093853; AAC67553.1; -; Genomic_DNA.
DR EMBL; AF093857; AAD03716.1; -; Genomic_DNA.
DR EMBL; AF093854; AAD03716.1; JOINED; Genomic_DNA.
DR EMBL; AF093855; AAD03716.1; JOINED; Genomic_DNA.
DR EMBL; AF093856; AAD03716.1; JOINED; Genomic_DNA.
DR EMBL; AK030413; BAC26952.1; -; mRNA.
DR EMBL; BC013489; AAH13489.1; -; mRNA.
DR CCDS; CCDS15415.1; -.
DR RefSeq; NP_031479.1; NM_007453.4.
DR AlphaFoldDB; O08709; -.
DR SMR; O08709; -.
DR BioGRID; 198118; 20.
DR IntAct; O08709; 10.
DR MINT; O08709; -.
DR STRING; 10090.ENSMUSP00000071636; -.
DR iPTMnet; O08709; -.
DR PhosphoSitePlus; O08709; -.
DR SwissPalm; O08709; -.
DR COMPLUYEAST-2DPAGE; O08709; -.
DR REPRODUCTION-2DPAGE; O08709; -.
DR SWISS-2DPAGE; O08709; -.
DR UCD-2DPAGE; O08709; -.
DR CPTAC; non-CPTAC-3603; -.
DR EPD; O08709; -.
DR jPOST; O08709; -.
DR MaxQB; O08709; -.
DR PaxDb; O08709; -.
DR PeptideAtlas; O08709; -.
DR PRIDE; O08709; -.
DR ProteomicsDB; 291649; -.
DR TopDownProteomics; O08709; -.
DR DNASU; 11758; -.
DR GeneID; 11758; -.
DR KEGG; mmu:11758; -.
DR CTD; 9588; -.
DR MGI; MGI:894320; Prdx6.
DR eggNOG; KOG0854; Eukaryota.
DR InParanoid; O08709; -.
DR OrthoDB; 1129256at2759; -.
DR BRENDA; 1.11.1.27; 3474.
DR BRENDA; 2.3.1.23; 3474.
DR BRENDA; 3.1.1.4; 3474.
DR Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 11758; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Prdx6; mouse.
DR PRO; PR:O08709; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08709; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IMP:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISO:MGI.
DR GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004601; F:peroxidase activity; IMP:MGI.
DR GO; GO:0004623; F:phospholipase A2 activity; IMP:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0032060; P:bleb assembly; IMP:MGI.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0098869; P:cellular oxidant detoxification; ISO:MGI.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; ISO:MGI.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; ISO:MGI.
DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR CDD; cd03016; PRX_1cys; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antioxidant; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Lipid degradation; Lipid metabolism; Lysosome; Multifunctional enzyme;
KW Oxidoreductase; Peroxidase; Phosphoprotein; Redox-active center;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9205120, ECO:0000269|Ref.6"
FT CHAIN 2..224
FT /note="Peroxiredoxin-6"
FT /id="PRO_0000135103"
FT DOMAIN 5..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 31..40
FT /note="Required and sufficient for targeting to lysosomes
FT and lamellar bodies"
FT /evidence="ECO:0000250|UniProtKB:O35244"
FT ACT_SITE 47
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT ACT_SITE 140
FT /note="For phospholipase activity"
FT /evidence="ECO:0000305|PubMed:26830860"
FT SITE 32
FT /note="Important for phospholipase activity"
FT /evidence="ECO:0000305|PubMed:26830860"
FT MOD_RES 44
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT MOD_RES 63
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT MOD_RES 89
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O35244"
FT MOD_RES 209
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT MOD_RES 209
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VARIANT 124
FT /note="D -> A (in strain: C57BL/6, C57BL/6J and FVB/N)"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 26
FT /note="H->A: Loss of phospholipase activity, but no effect
FT on lysophosphatidylcholine acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26830860"
FT MUTAGEN 31
FT /note="D->A: Loss of lysophosphatidylcholine
FT acyltransferase activity, but no effect on phosholipase
FT activity."
FT /evidence="ECO:0000269|PubMed:26830860"
FT MUTAGEN 32
FT /note="S->A: Loss of phospholipase activity, but no effect
FT on lysophosphatidylcholine acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26830860"
FT MUTAGEN 47
FT /note="C->S: No loss of phospholipase or
FT lysophosphatidylcholine acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26830860"
FT MUTAGEN 140
FT /note="D->A: Loss of phospholipase activity, but no effect
FT on lysophosphatidylcholine acyltransferase activity."
FT /evidence="ECO:0000269|PubMed:26830860"
FT CONFLICT 154
FT /note="G -> S (in Ref. 3; AAC67553)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="W -> R (in Ref. 3; AAD03716)"
FT /evidence="ECO:0000305"
SQ 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
