Reviewed,
UniProtKB/Swiss-Prot P52430 (PON1_MOUSE)
Last modified
February 9, 2010.
Version 84.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Serum paraoxonase/arylesterase 1 Short name=PON 1 EC=3.1.1.2 EC=3.1.8.1 Alternative name(s): Serum aryldialkylphosphatase 1 Aromatic esterase 1 Short name=A-esterase 1 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › 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 a number of aromatic carboxylic acid esters. |
| Catalytic activity | A phenyl acetate + H2O = a phenol + acetate. An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. |
| Cofactor | Binds 2 calcium ions per subunit By similarity. |
| Subunit structure | Interacts with CLU By similarity. |
| Subcellular location | |
| 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 |
| Gene Ontology (GO) | |
| Biological process | blood circulation Traceable author statement. Source: MGI cholesterol metabolic processInferred from mutant phenotype. Source: MGI response to toxinInferred from mutant phenotype. Source: MGI |
| Molecular function | aryldialkylphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB arylesterase activityInferred from sequence or structural similarity. Source: UniProtKB calcium ion bindingInferred from sequence or structural similarity. Source: UniProtKB high-density lipoprotein bindingTraceable author statement. Source: MGI |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – ? | Not cleaved | |||||||||
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||||
| Chain | 2 – 355 | 354 | Serum paraoxonase/arylesterase 1 | PRO_0000223282 | |||||||
Sites | |||||||||||
| Active site | 115 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 53 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 54 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 117 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 168 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 169 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 224 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 269 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 270 | 1 | Calcium 1; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 76 | 1 | Phosphoserine By similarity | ||||||||
| Modified residue | 80 | 1 | Phosphoserine By similarity | ||||||||
| Glycosylation | 253 | 1 | N-linked (GlcNAc...) Ref.4 | ||||||||
| Glycosylation | 270 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 324 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 42 ↔ 353 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 186 | 1 | F → L in AAC52496. Ref.2 | ||||||||
Sequences
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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: 7638166] [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: 8601628] [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: 9170151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. |
| [4] | "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: 17330941] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, MASS SPECTROMETRY. 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. |
| IPI | IPI00317356. |
| PIR | T10082. |
| RefSeq | NP_035264.2. |
| UniGene | Mm.237657 |
3D structure databases | |
| SMR | P52430. Positions 16-355. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P52430. |
Proteomic databases | |
| PRIDE | P52430. |
Genome annotation databases | |
| Ensembl | ENSMUST00000002663; ENSMUSP00000002663; ENSMUSG00000002588; Mus musculus. [Genome view] |
| GeneID | 18979. |
| KEGG | mmu:18979. |
| UCSC | uc009awd.1. mouse. |
Organism-specific databases | |
| CTD | 18979. |
| MGI | MGI:103295. Pon1. |
Phylogenomic databases | |
| eggNOG | roNOG04341. |
| HOGENOM | HBG613410. |
| HOVERGEN | P52430. |
| InParanoid | P52430. |
| OMA | TNDHYFV. |
| OrthoDB | EOG912PQX. |
| PhylomeDB | P52430. |
Enzyme and pathway databases | |
| BRENDA | 3.1.1.2. 244. 3.1.8.1. 244. |
Gene expression databases | |
| ArrayExpress | P52430. |
| Bgee | P52430. |
| CleanEx | MM_PON1. |
| Genevestigator | P52430. |
| GermOnline | ENSMUSG00000002588. Mus musculus. |
Family and domain databases | |
| InterPro | IPR011042. 6-blade_b-propeller_TolB-like. IPR002640. Arylesterase. IPR008363. Paraoxonase1. [Graphical view] |
| Gene3D | G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit. |
| Pfam | PF01731. Arylesterase. 1 hit. [Graphical view] |
| PRINTS | PR01785. PARAOXONASE. PR01786. PARAOXONASE1. |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 295346. |
| SOURCE | Search... |
Entry information
| Entry name | PON1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P52430 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


