PON1
entrez
5444
canonical
uniprot
P27169
canonical
ensembl
ENSG00000005421
resolver
ensp
ENSP00000222381
resolver
enst
ENST00000222381
resolver
genesymbol
PON1
resolver
genesymbol_syn
PON
resolver
hgnc
HGNC:9204
resolver
uniprot
B2RA40
resolver
uniprot
Q16052
resolver
uniprot
Q6B0J6
resolver
uniprot
Q9UCB1
resolver
uniprot_entry
PON1_HUMAN
resolver
uniprot_sec
B2RA40
resolver
uniprot_sec
Q16052
resolver
uniprot_sec
Q6B0J6
resolver
uniprot_sec
Q9UCB1
resolver
amino_acid_sequence
MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL
uniprot
proteins
ec_number
3.1.1.2
uniprot
proteins
ec_number
3.1.1.81
uniprot
proteins
ec_number
3.1.8.1
uniprot
proteins
function
FUNCTION: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. {ECO:0000269|PubMed:10479665, ECO:0000269|PubMed:15772423}.
uniprot
proteins
mass_dalton
39731
uniprot
proteins
mutagenesis
MUTAGEN 20..21; /note="HQ->AA: The signal peptide is cleaved; not associated with HDL."; /evidence="ECO:0000269|PubMed:10479665"; MUTAGEN 115; /note="H->Q: Reduces activity 10000-fold."; /evidence="ECO:0000269|PubMed:15098021"; MUTAGEN 134; /note="H->Q: Substantially reduced activity."; /evidence="ECO:0000269|PubMed:15098021"; MUTAGEN 284; /note="C->A,S: No loss of activity."; /evidence="ECO:0000269|PubMed:7638166
uniprot
proteins
post_translational_modification
PTM: Glycosylated. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}.; PTM: The signal sequence is not cleaved.; PTM: Present in two forms, form B contains a disulfide bond, form A does not.
uniprot
proteins
protein_family
Paraoxonase family
uniprot
proteins
pubmed
10479665
uniprot
proteins
pubmed
12690205
uniprot
proteins
pubmed
12783936
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14760718
uniprot
proteins
pubmed
15098021
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772423
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16531243
uniprot
proteins
pubmed
1657140
uniprot
proteins
pubmed
1673382
uniprot
proteins
pubmed
1718413
uniprot
proteins
pubmed
18987736
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
7638166
uniprot
proteins
pubmed
7916578
uniprot
proteins
pubmed
8098250
uniprot
proteins
pubmed
8292612
uniprot
proteins
pubmed
8382160
uniprot
proteins
pubmed
8393742
uniprot
proteins
pubmed
8393745
uniprot
proteins
pubmed
8812495
uniprot
proteins
pubmed
9261565
uniprot
proteins
sequence_length
355
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space.
uniprot
proteins