Prdx6
entrez
94167
canonical
uniprot
O35244
canonical
ensembl
ENSRNOG00000081976
resolver
ensp
ENSRNOP00000103996
resolver
enst
ENSRNOT00000165363
resolver
genesymbol
Prdx6
resolver
genesymbol_syn
Aipla2
resolver
genesymbol_syn
Aop2
resolver
genesymbol_syn
Tsa
resolver
uniprot_entry
PRDX6_RAT
resolver
amino_acid_sequence
MPGGLLLGDEAPNFEANTTIGHIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHFAWSKDINAYNGAAPTEKLPFPIIDDKDRDLAILLGMLDPAEKDEKGMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTASNPVATPVDWKKGESVMVLPTLPEEEAKQLFPKGVFTKELPSGKKYLRYTPQP
uniprot
proteins
ec_number
1.11.1.27
uniprot
proteins
ec_number
2.3.1.23
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
function
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively (PubMed:15004285). Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides (By similarity). Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity) (PubMed:15004285, PubMed:17652308, PubMed:8999971). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH (By similarity). Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis (By similarity). Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (PubMed:26830860). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate (By similarity). {ECO:0000250|UniProtKB:P30041, ECO:0000269|PubMed:15004285, ECO:0000269|PubMed:17652308, ECO:0000269|PubMed:26830860, ECO:0000269|PubMed:8999971}.
uniprot
proteins
mass_dalton
24819
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="H->A: Abolishes lipid binding."; /evidence="ECO:0000269|PubMed:17652308"; MUTAGEN 32; /note="S->A: Abolishes lipid binding."; /evidence="ECO:0000269|PubMed:17652308"; MUTAGEN 140; /note="D->A: Abolishes phospholipase activity, but does not impair lipid binding."; /evidence="ECO:0000269|PubMed:17652308
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (PubMed:19140803). Phosphorylated form exhibits a greater lysophosphatidylcholine acyltransferase activity compared to the non-phosphorylated form (PubMed:26830860). {ECO:0000269|PubMed:19140803, ECO:0000269|PubMed:26830860}.; 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}.
uniprot
proteins
protein_family
Peroxiredoxin family
uniprot
proteins
protein_family
Prx6 subfamily
uniprot
proteins
pubmed
15004285
uniprot
proteins
pubmed
17652308
uniprot
proteins
pubmed
19140803
uniprot
proteins
pubmed
19700648
uniprot
proteins
pubmed
26830860
uniprot
proteins
pubmed
8999971
uniprot
proteins
sequence_length
224
uniprot
proteins
subcellular_location
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}.
uniprot
proteins