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P52430 (PON1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum paraoxonase/arylesterase 1

Short name=PON 1
EC=3.1.1.2
EC=3.1.1.81
EC=3.1.8.1
Alternative name(s):
Aromatic esterase 1
Short name=A-esterase 1
Serum aryldialkylphosphatase 1
Gene names
Name:Pon1
Synonyms:Pon
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 By similarity.

Catalytic activity

A phenyl acetate + H2O = a phenol + acetate. Ref.5

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. Ref.5

An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine. Ref.5

Cofactor

Binds 2 calcium ions per subunit By similarity.

Subunit structure

Homodimer. Interacts with CLU By similarity.

Subcellular location

Secretedextracellular space.

Tissue specificity

Plasma, liver, kidney, heart, brain, small intestine and lung. In the plasma, associated with HDL.

Post-translational modification

The signal sequence is not cleaved By similarity.

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 By similarity.

Sequence similarities

Belongs to the paraoxonase family.

Ontologies

Keywords
   Cellular componentHDL
Secreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaromatic compound catabolic process

Inferred from electronic annotation. Source: Ensembl

blood circulation

Traceable author statement PubMed 10393212. Source: MGI

carboxylic acid catabolic process

Inferred from electronic annotation. Source: Ensembl

cholesterol metabolic process

Inferred from mutant phenotype PubMed 9685159. Source: MGI

dephosphorylation

Inferred from sequence or structural similarity. Source: GOC

organophosphate catabolic process

Inferred from electronic annotation. Source: Ensembl

phosphatidylcholine metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of cholesterol efflux

Inferred from electronic annotation. Source: Ensembl

positive regulation of transporter activity

Inferred from electronic annotation. Source: Ensembl

response to toxic substance

Inferred from mutant phenotype PubMed 9685159. Source: MGI

   Cellular_componentintracellular membrane-bounded organelle

Inferred from electronic annotation. Source: Ensembl

spherical high-density lipoprotein particle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionaryldialkylphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

arylesterase activity

Inferred from sequence or structural similarity. Source: UniProtKB

calcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

high-density lipoprotein particle binding

Traceable author statement PubMed 10393212PubMed 9685159. Source: MGI

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 355354Serum paraoxonase/arylesterase 1
PRO_0000223282
Signal peptide2 – ?Not cleaved

Sites

Active site1151Proton acceptor By similarity
Metal binding531Calcium 1; catalytic By similarity
Metal binding541Calcium 2 By similarity
Metal binding1171Calcium 2; via carbonyl oxygen By similarity
Metal binding1681Calcium 1; catalytic By similarity
Metal binding1691Calcium 2 By similarity
Metal binding2241Calcium 1; catalytic By similarity
Metal binding2691Calcium 1; catalytic By similarity
Metal binding2701Calcium 1; catalytic By similarity

Amino acid modifications

Glycosylation2531N-linked (GlcNAc...) Ref.6
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 353 By similarity

Experimental info

Sequence conflict611G → E in AAH12706. Ref.4
Sequence conflict1861F → L in AAC52496. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P52430 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: FFA0A71445BB80B4

FASTA35539,565
        10         20         30         40         50         60 
MAKLLALTLV GLVLALYKNH RSSYQTRLNA FREVTPVELP NCNLVKGIET GAEDLEILPN 

        70         80         90        100        110        120 
GLTFFSTGLK YPGIKSFDPS KPGKILLMDL NKKEPAVSEL EIIGNTLDIS SFNPHGISTF 

       130        140        150        160        170        180 
TDEDNTVYLL VVNHPDSSST VEVFKFQEEE RSLLHLKTIT HELLPSINDI AAIGPESFYA 

       190        200        210        220        230        240 
TNDHYFADPY LRSWEMYLGL SWSNVVYYSP DKVQVVAEGF DFANGIGISL DGKYVYIAEL 

       250        260        270        280        290        300 
LAHKIHVYEK HANWTLTPLK VLNFDTLVDN ISVDPVTGDL WVGCHPNGMR IFFYDAENPP 

       310        320        330        340        350 
GSEVLRIQNI LSEDPKITVV YAENGTVLQG TTVASVYKGK LLIGTVFHKA LYCDL 

« Hide

References

« Hide 'large scale' references
[1]"Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase."
Sorenson R.C., Primo-Parmo S.L., Kuo C.-L., Adkins S., Lockridge O., La Du B.N.
Proc. Natl. Acad. Sci. U.S.A. 92:7187-7191(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[2]"Genetic-dietary regulation of serum paraoxonase expression and its role in atherogenesis in a mouse model."
Shih D.M., Gu L., Hama S., Xia Y.R., Navab M., Fogelman A.M., Lusis A.J.
J. Clin. Invest. 97:1630-1639(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Liver.
[3]"Paraoxonase (PON1) gene in mice: sequencing, chromosomal localization and developmental expression."
Li W.F., Matthews C., Disteche C.M., Costa L.G., Furlong C.E.
Pharmacogenetics 7:137-144(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[5]"Quorum quenching enzyme activity is widely conserved in the sera of mammalian species."
Yang F., Wang L.H., Wang J., Dong Y.H., Hu J.Y., Zhang L.H.
FEBS Lett. 579:3713-3717(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[6]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L40488 Genomic DNA. Translation: AAA99445.1.
U32684 mRNA. Translation: AAC52496.1.
U72636 mRNA. Translation: AAB17394.1.
BC012706 mRNA. Translation: AAH12706.1.
CCDSCCDS19898.1.
PIRT10082.
RefSeqNP_035264.2. NM_011134.3.
UniGeneMm.237657.

3D structure databases

ProteinModelPortalP52430.
SMRP52430. Positions 20-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP52430. 1 interaction.
MINTMINT-4121591.
STRING10090.ENSMUSP00000002663.

PTM databases

PhosphoSiteP52430.

Proteomic databases

MaxQBP52430.
PaxDbP52430.
PRIDEP52430.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000002663; ENSMUSP00000002663; ENSMUSG00000002588.
GeneID18979.
KEGGmmu:18979.
UCSCuc009awd.2. mouse.

Organism-specific databases

CTD5444.
MGIMGI:103295. Pon1.

Phylogenomic databases

eggNOGNOG68009.
GeneTreeENSGT00390000008932.
HOGENOMHOG000252960.
HOVERGENHBG003604.
InParanoidQ91X30.
KOK01045.
OMANAFREVT.
OrthoDBEOG7GN2N3.
PhylomeDBP52430.
TreeFamTF322436.

Gene expression databases

ArrayExpressP52430.
BgeeP52430.
CleanExMM_PON1.
GenevestigatorP52430.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008363. Paraoxonase1.
[Graphical view]
PfamPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSPR01785. PARAOXONASE.
PR01786. PARAOXONASE1.
ProtoNetSearch...

Other

NextBio295346.
PROP52430.
SOURCESearch...

Entry information

Entry namePON1_MOUSE
AccessionPrimary (citable) accession number: P52430
Secondary accession number(s): Q91X30
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot