Q62087 · PON3_MOUSE
- ProteinSerum paraoxonase/lactonase 3
- GenePon3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids354 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents (By similarity).
Catalytic activity
- a phenyl acetate + H2O = a phenol + acetate + H+
Cofactor
Note: Binds 2 calcium ions per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 53 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 54 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 114 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 116 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 167 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 168 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 223 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 268 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 269 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | 3,4-dihydrocoumarin hydrolase activity | |
Molecular Function | acyl-L-homoserine-lactone lactonohydrolase activity | |
Molecular Function | aryldialkylphosphatase activity | |
Molecular Function | arylesterase activity | |
Molecular Function | metal ion binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | coumarin catabolic process | |
Biological Process | establishment of localization in cell | |
Biological Process | negative regulation of superoxide anion generation | |
Biological Process | phenylacetate catabolic process | |
Biological Process | renal sodium ion transport | |
Biological Process | response to toxic substance |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerum paraoxonase/lactonase 3
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ62087
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-? | Not cleaved | ||||
Chain | PRO_0000223291 | 1-354 | Serum paraoxonase/lactonase 3 | |||
Sequence: MGKLVALTLLGACLALIGERLLNFRERVSTTREIKATEPQNCHLIEGLENGSEDIDILPSGLAFISTGLKYPGMPAFAPDKPGRIFLMDLNEQNPEAQALEISGGLDQESLNPHGISTFIDKDNTAYLYVVNHPNMDSTVEIFKFEEQQRSLIHLKTLKHELLKSVNDIVVLGPEQFYATRDHYFTSYFLVLLEMILDPHWTSVVFYSPKEVKVVAQGFSSANGITVSLDQKFVYVADVTAKNIHIMKKHDNWDLTPVKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLIYNPEDPPGSEVLRIQDSLSDKPRVSTLYANNGSVLQGSTVASVYHKRMLIGTIFHKALYCDL | ||||||
Disulfide bond | 42↔352 | |||||
Sequence: CHLIEGLENGSEDIDILPSGLAFISTGLKYPGMPAFAPDKPGRIFLMDLNEQNPEAQALEISGGLDQESLNPHGISTFIDKDNTAYLYVVNHPNMDSTVEIFKFEEQQRSLIHLKTLKHELLKSVNDIVVLGPEQFYATRDHYFTSYFLVLLEMILDPHWTSVVFYSPKEVKVVAQGFSSANGITVSLDQKFVYVADVTAKNIHIMKKHDNWDLTPVKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLIYNPEDPPGSEVLRIQDSLSDKPRVSTLYANNGSVLQGSTVASVYHKRMLIGTIFHKALYC | ||||||
Glycosylation | 50 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 165 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 269 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 323 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
The signal sequence is not cleaved.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length354
- Mass (Da)39,351
- Last updated2004-07-19 v2
- ChecksumD66534EAA4EB10F2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 1; AAC42090 | ||||
Sequence: K → H | ||||||
Sequence conflict | 8 | in Ref. 1; AAC42090 | ||||
Sequence: T → P | ||||||
Sequence conflict | 248 | in Ref. 1; AAC42090 | ||||
Sequence: K → E | ||||||
Sequence conflict | 273 | in Ref. 1; AAC42090 | ||||
Sequence: D → A | ||||||
Sequence conflict | 297 | in Ref. 1; AAC42090 | ||||
Sequence: D → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L76193 EMBL· GenBank· DDBJ | AAC42090.1 EMBL· GenBank· DDBJ | mRNA | ||
AK088572 EMBL· GenBank· DDBJ | BAC40430.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466533 EMBL· GenBank· DDBJ | EDL13970.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC099416 EMBL· GenBank· DDBJ | AAH99416.1 EMBL· GenBank· DDBJ | mRNA |