A0A6P5Q309 · A0A6P5Q309_MUSCR
- ProteinParaoxonase
- GenePon1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids355 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
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 | 115 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 117 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 168 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 169 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 224 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N | ||||||
Binding site | 269 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 270 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | acyl-L-homoserine-lactone lactonohydrolase activity | |
Molecular Function | arylesterase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameParaoxonase
- EC number
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionA0A6P5Q309
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-15 | |||||
Sequence: MAKLLALTLVGLVLA | ||||||
Chain | PRO_5028139359 | 16-355 | Paraoxonase | |||
Sequence: LYKNHRSSYQTRLNAFREVTPVELPNCNLVKGIETGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNKKEPAVSELEIIGNTLDISSFNPHGISTFTDEDNTVYLLVVNHPDSSSTVEVFKFQEEESSLLHLKTITHELLPSINDIAAIGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDKVQVVAEGFDFANGIGISLDGKYVYIAELLAHKIHVYEKHANWTLTPLKVLDFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDAENPPGSEVLRIQNILSEDPKVTVVYAENGTILQGTTVASVYKGKLLIGTVFHKALYCDL | ||||||
Disulfide bond | 42↔353 | In form B | ||||
Sequence: CNLVKGIETGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNKKEPAVSELEIIGNTLDISSFNPHGISTFTDEDNTVYLLVVNHPDSSSTVEVFKFQEEESSLLHLKTITHELLPSINDIAAIGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDKVQVVAEGFDFANGIGISLDGKYVYIAELLAHKIHVYEKHANWTLTPLKVLDFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDAENPPGSEVLRIQNILSEDPKVTVVYAENGTILQGTTVASVYKGKLLIGTVFHKALYC | ||||||
Glycosylation | 253 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 270 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 324 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length355
- Mass (Da)39,497
- Last updated2020-12-02 v1
- ChecksumDC061D858A0F4333