PRDX6_MESAU
ID PRDX6_MESAU Reviewed; 50 AA.
AC P86215;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=Peroxiredoxin-6 {ECO:0000250|UniProtKB:P30041};
DE EC=1.11.1.27 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=1-Cys peroxiredoxin {ECO:0000250|UniProtKB:P30041};
DE Short=1-Cys PRX {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Acidic calcium-independent phospholipase A2 {ECO:0000250|UniProtKB:P30041};
DE Short=aiPLA2 {ECO:0000250|UniProtKB:P30041};
DE EC=3.1.1.4;
DE AltName: Full=Antioxidant protein 2 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Glutathione-dependent peroxiredoxin {ECO:0000305};
DE AltName: Full=Lysophosphatidylcholine acyltransferase 5 {ECO:0000250|UniProtKB:P30041};
DE Short=LPC acyltransferase 5;
DE Short=LPCAT-5;
DE Short=Lyso-PC acyltransferase 5;
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:P30041};
DE AltName: Full=Non-selenium glutathione peroxidase {ECO:0000250|UniProtKB:P30041};
DE Short=NSGPx {ECO:0000250|UniProtKB:P30041};
DE Flags: Fragments;
GN Name=PRDX6 {ECO:0000250|UniProtKB:P30041};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20400973; DOI=10.1038/aja.2010.19;
RA Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.;
RT "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen
RT (GP96) are unique to hamster caput epididymal spermatozoa.";
RL Asian J. Androl. 12:344-355(2010).
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 Also has phospholipase activity, and can therefore 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 (By similarity). 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 -!- 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:0000250|UniProtKB:P30041};
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:0000250|UniProtKB:P30041};
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 -!- 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 (By similarity).
CC {ECO:0000250|UniProtKB:O08709, ECO:0000250|UniProtKB:O77834,
CC ECO:0000250|UniProtKB:P30041}.
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 -!- PTM: Irreversibly inactivated by overoxidation of Cys-6 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}.
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DR AlphaFoldDB; P86215; -.
DR SMR; P86215; -.
DR STRING; 10036.XP_005071394.1; -.
DR eggNOG; KOG0854; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Acetylation; Antioxidant; Cytoplasm; Hydrolase; Lipid degradation;
KW Lipid metabolism; Lysosome; Multifunctional enzyme; Oxidoreductase;
KW Peroxidase; Phosphoprotein; Redox-active center; Reference proteome;
KW Transferase.
FT CHAIN <1..>50
FT /note="Peroxiredoxin-6"
FT /id="PRO_0000394303"
FT DOMAIN <1..>50
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT ACT_SITE 6
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT ACT_SITE 28
FT /note="For phospholipase activity"
FT /evidence="ECO:0000250|UniProtKB:O35244"
FT MOD_RES 3
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT NON_CONS 12..13
FT /evidence="ECO:0000305"
FT NON_CONS 20..21
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 50
SQ SEQUENCE 50 AA; 5686 MW; B0C0D9B70FAC32FC CRC64;
DFTPVCTTEL GRLAPEFAKR VVFIFGPDKK LKLSILYPAT TGRNFDEILR
