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Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (Serum aryldialkylphosphatase 1)

 PON1_MOUSE              Reviewed;         355 AA.
P52430; Q91X30;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 143.
RecName: Full=Serum paraoxonase/arylesterase 1;
Short=PON 1;
EC=3.1.1.2 {ECO:0000269|PubMed:15963993};
EC=3.1.1.81 {ECO:0000269|PubMed:15963993};
EC=3.1.8.1 {ECO:0000269|PubMed:15963993};
AltName: Full=Aromatic esterase 1;
Short=A-esterase 1;
AltName: Full=Serum aryldialkylphosphatase 1;
Name=Pon1; Synonyms=Pon;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=7638166; DOI=10.1073/pnas.92.16.7187;
Sorenson R.C., Primo-Parmo S.L., Kuo C.-L., Adkins S., Lockridge O.,
La Du B.N.;
"Reconsideration of the catalytic center and mechanism of mammalian
paraoxonase/arylesterase.";
Proc. Natl. Acad. Sci. U.S.A. 92:7187-7191(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6 X CBA; TISSUE=Liver;
PubMed=8601628; DOI=10.1172/JCI118589;
Shih D.M., Gu L., Hama S., Xia Y.R., Navab M., Fogelman A.M.,
Lusis A.J.;
"Genetic-dietary regulation of serum paraoxonase expression and its
role in atherogenesis in a mouse model.";
J. Clin. Invest. 97:1630-1639(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=9170151;
Li W.F., Matthews C., Disteche C.M., Costa L.G., Furlong C.E.;
"Paraoxonase (PON1) gene in mice: sequencing, chromosomal localization
and developmental expression.";
Pharmacogenetics 7:137-144(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
CATALYTIC ACTIVITY.
PubMed=15963993; DOI=10.1016/j.febslet.2005.05.060;
Yang F., Wang L.H., Wang J., Dong Y.H., Hu J.Y., Zhang L.H.;
"Quorum quenching enzyme activity is widely conserved in the sera of
mammalian species.";
FEBS Lett. 579:3713-3717(2005).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253.
STRAIN=C57BL/6J; TISSUE=Plasma;
PubMed=17330941; DOI=10.1021/pr0604559;
Bernhard O.K., Kapp E.A., Simpson R.J.;
"Enhanced analysis of the mouse plasma proteome using cysteine-
containing tryptic glycopeptides.";
J. Proteome Res. 6:987-995(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. {ECO:0000250|UniProtKB:P27169}.
-!- CATALYTIC ACTIVITY: A phenyl acetate + H(2)O = a phenol + acetate.
{ECO:0000269|PubMed:15963993}.
-!- CATALYTIC ACTIVITY: An aryl dialkyl phosphate + H(2)O = dialkyl
phosphate + an aryl alcohol. {ECO:0000269|PubMed:15963993}.
-!- CATALYTIC ACTIVITY: An N-acyl-L-homoserine lactone + H(2)O = an N-
acyl-L-homoserine. {ECO:0000269|PubMed:15963993}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
Note=Binds 2 calcium ions per subunit. {ECO:0000250};
-!- SUBUNIT: Homodimer. Interacts with CLU.
{ECO:0000250|UniProtKB:P27169}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Plasma, liver, kidney, heart, brain, small
intestine and lung. In the plasma, associated with HDL.
-!- PTM: The signal sequence is not cleaved.
{ECO:0000250|UniProtKB:P27169}.
-!- MISCELLANEOUS: The preferential association of PON1 with HDL is
mediated in part by its signal peptide, by binding phospholipids
directly, rather than binding apo AI. The retained signal peptide
may allow transfer of the protein between phospholipid surfaces.
{ECO:0000250|UniProtKB:P27169}.
-!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L40488; AAA99445.1; -; Genomic_DNA.
EMBL; U32684; AAC52496.1; -; mRNA.
EMBL; U72636; AAB17394.1; -; mRNA.
EMBL; BC012706; AAH12706.1; -; mRNA.
CCDS; CCDS19898.1; -.
PIR; T10082; T10082.
RefSeq; NP_035264.2; NM_011134.3.
UniGene; Mm.237657; -.
ProteinModelPortal; P52430; -.
SMR; P52430; -.
IntAct; P52430; 1.
MINT; MINT-4121591; -.
STRING; 10090.ENSMUSP00000002663; -.
iPTMnet; P52430; -.
PhosphoSitePlus; P52430; -.
MaxQB; P52430; -.
PaxDb; P52430; -.
PeptideAtlas; P52430; -.
PRIDE; P52430; -.
Ensembl; ENSMUST00000002663; ENSMUSP00000002663; ENSMUSG00000002588.
GeneID; 18979; -.
KEGG; mmu:18979; -.
UCSC; uc009awd.2; mouse.
CTD; 5444; -.
MGI; MGI:103295; Pon1.
eggNOG; ENOG410IHDV; Eukaryota.
eggNOG; ENOG4111QK7; LUCA.
GeneTree; ENSGT00390000008932; -.
HOGENOM; HOG000252960; -.
HOVERGEN; HBG003604; -.
InParanoid; P52430; -.
KO; K01045; -.
OMA; NCNLVKG; -.
OrthoDB; EOG091G0AV9; -.
PhylomeDB; P52430; -.
TreeFam; TF322436; -.
BRENDA; 3.1.1.2; 3474.
BRENDA; 3.1.1.25; 3474.
BRENDA; 3.1.8.1; 3474.
Reactome; R-MMU-2142688; Synthesis of 5-eicosatetraenoic acids.
PRO; PR:P52430; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000002588; -.
CleanEx; MM_PON1; -.
ExpressionAtlas; P52430; baseline and differential.
Genevisible; P52430; MM.
GO; GO:0072562; C:blood microparticle; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0034364; C:high-density lipoprotein particle; ISO:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:MGI.
GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0004063; F:aryldialkylphosphatase activity; ISS:UniProtKB.
GO; GO:0004064; F:arylesterase activity; IMP:MGI.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0008035; F:high-density lipoprotein particle binding; TAS:MGI.
GO; GO:0005543; F:phospholipid binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019439; P:aromatic compound catabolic process; ISO:MGI.
GO; GO:0008015; P:blood circulation; TAS:MGI.
GO; GO:0046395; P:carboxylic acid catabolic process; ISO:MGI.
GO; GO:0008203; P:cholesterol metabolic process; IMP:MGI.
GO; GO:0046434; P:organophosphate catabolic process; ISO:MGI.
GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:MGI.
GO; GO:0051099; P:positive regulation of binding; ISO:MGI.
GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:MGI.
GO; GO:0032411; P:positive regulation of transporter activity; ISO:MGI.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:1902617; P:response to fluoride; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IMP:MGI.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR002640; Arylesterase.
InterPro; IPR008363; Paraoxonase1.
PANTHER; PTHR11799:SF20; PTHR11799:SF20; 1.
Pfam; PF01731; Arylesterase; 1.
PRINTS; PR01785; PARAOXONASE.
PRINTS; PR01786; PARAOXONASE1.
1: Evidence at protein level;
Calcium; Complete proteome; Disulfide bond; Glycoprotein; HDL;
Hydrolase; Metal-binding; Reference proteome; Secreted; Signal.
CHAIN 1 355 Serum paraoxonase/arylesterase 1.
/FTId=PRO_0000223282.
SIGNAL 1 ? Not cleaved.
ACT_SITE 115 115 Proton acceptor.
{ECO:0000250|UniProtKB:P27169}.
METAL 53 53 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 54 54 Calcium 2.
{ECO:0000250|UniProtKB:P27169}.
METAL 117 117 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P27169}.
METAL 168 168 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 169 169 Calcium 2.
{ECO:0000250|UniProtKB:P27169}.
METAL 224 224 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 269 269 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 270 270 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17330941}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 353 {ECO:0000250|UniProtKB:P27169}.
CONFLICT 61 61 G -> E (in Ref. 4; AAH12706).
{ECO:0000305}.
CONFLICT 186 186 F -> L (in Ref. 2; AAC52496).
{ECO:0000305}.
SEQUENCE 355 AA; 39565 MW; FFA0A71445BB80B4 CRC64;
MAKLLALTLV GLVLALYKNH RSSYQTRLNA FREVTPVELP NCNLVKGIET GAEDLEILPN
GLTFFSTGLK YPGIKSFDPS KPGKILLMDL NKKEPAVSEL EIIGNTLDIS SFNPHGISTF
TDEDNTVYLL VVNHPDSSST VEVFKFQEEE RSLLHLKTIT HELLPSINDI AAIGPESFYA
TNDHYFADPY LRSWEMYLGL SWSNVVYYSP DKVQVVAEGF DFANGIGISL DGKYVYIAEL
LAHKIHVYEK HANWTLTPLK VLNFDTLVDN ISVDPVTGDL WVGCHPNGMR IFFYDAENPP
GSEVLRIQNI LSEDPKITVV YAENGTVLQG TTVASVYKGK LLIGTVFHKA LYCDL


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