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UniProt functional annotation for P27170 | ||
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| UniProt code: P27170. |
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| Organism: | |
Oryctolagus cuniculus (Rabbit). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus. |
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| 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. {ECO:0000269|PubMed:11266077}. |
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| Catalytic activity: | |
Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000269|PubMed:1718413}; |
| Catalytic activity: | |
Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate + an aryl alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:1718413}; |
| Catalytic activity: | |
Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; Evidence={ECO:0000269|PubMed:1718413}; |
| Cofactor: | |
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P27169}; Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P27169}; |
| Subunit: | |
Homodimer. Interacts with CLU. {ECO:0000250|UniProtKB:P27169}. |
| Subcellular location: | |
Secreted, extracellular space. |
| Tissue specificity: | |
Plasma. Associated with HDL. |
| Ptm: | |
Glycosylated. |
| Ptm: | |
The signal sequence is not cleaved. |
| Polymorphism: | |
There are two allelic forms, allozyme A and B, which differ in their substrate specificity. Both forms have similar arylesterase activity but allozyme B possesses greater paraoxonase activity. Allozyme A is better at protecting LDL from oxidation. |
| 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. {ECO:0000250|UniProtKB:P27169}. |
| Similarity: | |
Belongs to the paraoxonase family. {ECO:0000305}. |
| Sequence caution: | |
Sequence=AAK06398.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.