PRDX6_CHICK
ID PRDX6_CHICK Reviewed; 224 AA.
AC Q5ZJF4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
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;
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;
DE Short=NSGPx;
GN Name=PRDX6; ORFNames=RCJMB04_18k11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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).
CC {ECO:0000250|UniProtKB:O77834, 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-46 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-176 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 EMBL; AJ720480; CAG32139.1; -; mRNA.
DR RefSeq; NP_001034418.1; NM_001039329.2.
DR AlphaFoldDB; Q5ZJF4; -.
DR SMR; Q5ZJF4; -.
DR BioGRID; 687951; 1.
DR IntAct; Q5ZJF4; 1.
DR STRING; 9031.ENSGALP00000004817; -.
DR PeroxiBase; 4421; Gga1CysPrx.
DR PaxDb; Q5ZJF4; -.
DR GeneID; 429062; -.
DR KEGG; gga:429062; -.
DR CTD; 9588; -.
DR VEuPathDB; HostDB:geneid_429062; -.
DR eggNOG; KOG0854; Eukaryota.
DR InParanoid; Q5ZJF4; -.
DR OrthoDB; 1129256at2759; -.
DR PhylomeDB; Q5ZJF4; -.
DR BRENDA; 3.1.1.4; 1306.
DR PRO; PR:Q5ZJF4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:AgBase.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Antioxidant; Cytoplasm; Hydrolase; Lipid degradation; Lipid metabolism;
KW Lysosome; Multifunctional enzyme; Oxidoreductase; Peroxidase;
KW Phosphoprotein; Redox-active center; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..224
FT /note="Peroxiredoxin-6"
FT /id="PRO_0000256863"
FT DOMAIN 4..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00691"
FT REGION 30..39
FT /note="Required and sufficient for targeting to lysosomes
FT and lamellar bodies"
FT /evidence="ECO:0000250|UniProtKB:O35244"
FT ACT_SITE 46
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000250|UniProtKB:P30041"
FT ACT_SITE 139
FT /note="For phospholipase activity"
FT /evidence="ECO:0000250|UniProtKB:O35244"
FT SITE 31
FT /note="Important for phospholipase activity"
FT /evidence="ECO:0000250|UniProtKB:O35244"
FT MOD_RES 88
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 176
FT /note="Phosphothreonine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:O35244"
SQ SEQUENCE 224 AA; 24977 MW; 4F2759FB44EC9493 CRC64;
MPGLLLGDEA PNFEADTTQG GIRFHDFLGD SWGILFSHPR DFTPVCTTEL GRAAKLAPEF
SKRNVKMIAL SIDSVPDHLA WSKDINAYNG DQPVEKLPFP IIADKDRELA VKLGMLDPDE
RDKDGMPLTA RVVFIFGPDK KLKLSILYPA TTGRNFDEIL RVVDSLQLTA YKKVATPVDW
KCGDSVMVVP TLPDEEAKKL FPKGVFTKDL PSGKKYLRYT PQPE
