Q62086 (PON2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 90.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Serum paraoxonase/arylesterase 2 Short name=PON 2 EC=3.1.1.2 EC=3.1.1.81 Alternative name(s): Aromatic esterase 2 Short name=A-esterase 2 Serum aryldialkylphosphatase 2 | ||
| 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 › Mus |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters By similarity. |
| Catalytic activity | A phenyl acetate + H2O = a phenol + acetate. 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 | Homotrimer By similarity. |
| Subcellular location | Membrane; Peripheral membrane protein By similarity. |
| Post-translational modification | Glycosylated By similarity. The signal sequence is not cleaved By similarity. |
| Sequence similarities | Belongs to the paraoxonase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: InterPro |
| Molecular function | arylesterase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 354 | 354 | Serum paraoxonase/arylesterase 2 | PRO_0000223288 | |||||||
| Signal peptide | 1 – ? | Not cleaved Potential | |||||||||
Sites | |||||||||||
| Active site | 114 | 1 | Proton acceptor By similarity | ||||||||
| Metal binding | 53 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 54 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 116 | 1 | Calcium 2; via carbonyl oxygen By similarity | ||||||||
| Metal binding | 167 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 168 | 1 | Calcium 2 By similarity | ||||||||
| Metal binding | 223 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 268 | 1 | Calcium 1; catalytic By similarity | ||||||||
| Metal binding | 269 | 1 | Calcium 1; catalytic By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 254 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 269 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 323 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 42 ↔ 352 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 8 – 14 | 7 | SLLGIGL → GFAGHRV in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 25 | 1 | R → S in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 30 | 1 | A → G in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 91 – 98 | 8 | KDERPRAL → DERPPSLE in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 137 – 138 | 2 | KS → SN in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 148 | 1 | E → A in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 175 | 1 | T → A in AAC42089. Ref.1 | ||||||||
| Sequence conflict | 300 | 1 | A → T in AAC42089. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family." Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N. Genomics 33:498-507(1996) [PubMed: 8661009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c and NOD. Tissue: Spleen. |
| [3] | Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Colon and Mammary tumor. |
| [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: 15963993] [Abstract] Cited for: CATALYTIC ACTIVITY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L48514 mRNA. Translation: AAC42089.1. AK146311 mRNA. Translation: BAE27066.1. AK171926 mRNA. Translation: BAE42735.1. CH466533 Genomic DNA. Translation: EDL13967.1. BC037140 mRNA. Translation: AAH37140.1. BC055896 mRNA. Translation: AAH55896.1. BC062200 mRNA. Translation: AAH62200.1. |
| IPI | IPI00310567. |
| RefSeq | NP_899131.1. NM_183308.2. |
| UniGene | Mm.126984. Mm.460999. |
3D structure databases | |
| ProteinModelPortal | Q62086. |
| SMR | Q62086. Positions 23-354. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q62086. |
Proteomic databases | |
| PRIDE | Q62086. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000057792; ENSMUSP00000062670; ENSMUSG00000032667. |
| GeneID | 330260. |
| KEGG | mmu:330260. |
| UCSC | uc009awf.1. mouse. |
Organism-specific databases | |
| CTD | 5445. |
| MGI | MGI:106687. Pon2. |
Phylogenomic databases | |
| GeneTree | ENSGT00390000008932. |
| HOGENOM | HBG613410. |
| HOVERGEN | HBG003604. |
| InParanoid | Q62086. |
| OMA | HTIEIFE. |
| OrthoDB | EOG4XD3RN. |
| PhylomeDB | Q62086. |
Gene expression databases | |
| ArrayExpress | Q62086. |
| Bgee | Q62086. |
| CleanEx | MM_PON2. |
| Genevestigator | Q62086. |
| GermOnline | ENSMUSG00000032667. Mus musculus. |
Family and domain databases | |
| InterPro | IPR011042. 6-blade_b-propeller_TolB-like. IPR002640. Arylesterase. IPR008364. Paraoxonase2. [Graphical view] |
| Gene3D | G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit. |
| KO | K01045. |
| Pfam | PF01731. Arylesterase. 1 hit. [Graphical view] |
| PRINTS | PR01785. PARAOXONASE. PR01787. PARAOXONASE2. |
| ProtoNet | Search... |
Other | |
| NextBio | 399259. |
| SOURCE | Search... |
Entry information
| Entry name | PON2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q62086 Secondary accession number(s): Q3TAD3, Q8CFK3 | ||||||||
| Entry history |
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| 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 |

Clusters with