Q6AXM8 (PON2_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 65.
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 | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 354 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript 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. An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine. |
| 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) | |
| Biological process | response to oxidative stress Inferred from expression pattern. Source: RGD |
| Cellular component | extracellular region Inferred from electronic annotation. Source: InterPro lysosomeInferred from direct assay. Source: RGD microsomeInferred from direct assay. Source: RGD mitochondrionInferred from direct assay. Source: RGD nucleusInferred from direct assay. Source: RGD |
| 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_0000223289 | |||||||
| 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 | |||||||||
Sequences
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References
| [1] | "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]. Tissue: Lung. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC079462 mRNA. Translation: AAH79462.1. |
| IPI | IPI00464486. |
| RefSeq | NP_001013100.1. NM_001013082.1. |
| UniGene | Rn.1100. |
3D structure databases | |
| ProteinModelPortal | Q6AXM8. |
| SMR | Q6AXM8. Positions 23-354. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6AXM8. |
Proteomic databases | |
| PRIDE | Q6AXM8. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000036460; ENSRNOP00000033943; ENSRNOG00000009112. |
| GeneID | 296851. |
| KEGG | rno:296851. |
| NMPDR | fig|10116.3.peg.20803. |
| UCSC | NM_001013082. rat. |
Organism-specific databases | |
| CTD | 5445. |
| RGD | 1309954. Pon2. |
Phylogenomic databases | |
| eggNOG | roNOG06389. |
| GeneTree | ENSGT00390000008932. |
| HOVERGEN | HBG003604. |
| InParanoid | Q6AXM8. |
| OMA | HTIEIFE. |
| OrthoDB | EOG4XD3RN. |
| PhylomeDB | Q6AXM8. |
Gene expression databases | |
| ArrayExpress | Q6AXM8. |
| Genevestigator | Q6AXM8. |
| GermOnline | ENSRNOG00000009112. Rattus norvegicus. |
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 | 641839. |
Entry information
| Entry name | PON2_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6AXM8 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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