Serum paraoxonase/arylesterase 1 - Mus musculus (Mouse)

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P52430 (PON1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 107. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular 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 component	HDL Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: Compara blood circulation Traceable author statement PubMed 10393212. Source: MGI carboxylic acid catabolic process Inferred from electronic annotation. Source: Compara cholesterol metabolic process Inferred from mutant phenotype PubMed 9685159. Source: MGI organophosphate catabolic process Inferred from electronic annotation. Source: Compara phosphatidylcholine metabolic process Inferred from electronic annotation. Source: Compara positive regulation of binding Inferred from electronic annotation. Source: Compara positive regulation of cholesterol efflux Inferred from electronic annotation. Source: Compara positive regulation of transporter activity Inferred from electronic annotation. Source: Compara response to toxic substance Inferred from mutant phenotype PubMed 9685159. Source: MGI
Cellular_component	intracellular membrane-bounded organelle Inferred from electronic annotation. Source: Compara spherical high-density lipoprotein particle Inferred from electronic annotation. Source: Compara
Molecular_function	aryldialkylphosphatase 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 10393212 PubMed 9685159. Source: MGI phospholipid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 355

354

Serum paraoxonase/arylesterase 1

PRO_0000223282

Signal peptide

2 – ?

Not cleaved

Sites

Active site

115

Proton acceptor By similarity

Metal binding

Calcium 1; catalytic By similarity

Metal binding

Calcium 2 By similarity

Metal binding

117

Calcium 2; via carbonyl oxygen By similarity

Metal binding

168

Calcium 1; catalytic By similarity

Metal binding

169

Calcium 2 By similarity

Metal binding

224

Calcium 1; catalytic By similarity

Metal binding

269

Calcium 1; catalytic By similarity

Metal binding

270

Calcium 1; catalytic By similarity

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

Phosphoserine By similarity

Glycosylation

253

N-linked (GlcNAc...) Ref.6

Glycosylation

270

N-linked (GlcNAc...) Potential

Glycosylation

324

N-linked (GlcNAc...) Potential

Disulfide bond

42 ↔ 353

By similarity

Experimental info

Sequence conflict

G → E in AAH12706. Ref.4

Sequence conflict

186

F → L in AAC52496. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P52430 [UniParc].

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

355

39,565

        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' referencesShow '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, MASS SPECTROMETRY. 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.
IPI	IPI00317356.
PIR	T10082.
RefSeq	NP_035264.2. NM_011134.3.
UniGene	Mm.237657.
3D structure databases
ProteinModelPortal	P52430.
SMR	P52430. Positions 20-355.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-4121591.
STRING	10090.ENSMUSP00000002663.
PTM databases
PhosphoSite	P52430.
Proteomic databases
PaxDb	P52430.
PRIDE	P52430.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000002663; ENSMUSP00000002663; ENSMUSG00000002588.
GeneID	18979.
KEGG	mmu:18979.
UCSC	uc009awd.2. mouse.
Organism-specific databases
CTD	5444.
MGI	MGI:103295. Pon1.
Phylogenomic databases
eggNOG	NOG68009.
GeneTree	ENSGT00390000008932.
HOGENOM	HOG000252960.
HOVERGEN	HBG003604.
InParanoid	Q91X30.
KO	K01045.
OMA	RSSYQTR.
OrthoDB	EOG4XD3RN.
Gene expression databases
ArrayExpress	P52430.
Bgee	P52430.
CleanEx	MM_PON1.
Genevestigator	P52430.
GermOnline	ENSMUSG00000002588. Mus musculus.
Family and domain databases
Gene3D	2.120.10.30. 1 hit.
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR002640. Arylesterase. IPR008363. Paraoxonase1. [Graphical view]
Pfam	PF01731. Arylesterase. 1 hit. [Graphical view]
PRINTS	PR01785. PARAOXONASE. PR01786. PARAOXONASE1.
ProtoNet	Search...
Other
NextBio	295346.
SOURCE	Search...

Entry information

Entry name

PON1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents