H3BK03 · H3BK03_MOUSE
- ProteinParaoxonase
- GenePon1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids256 (go to sequence)
- Protein existenceEvidence at protein level
- 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 | 202 | Ca2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 203 | 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
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionH3BK03
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-15 | |||||
Sequence: MAKLLALTLVGLVLA | ||||||
Chain | PRO_5016283790 | 16-256 | Paraoxonase | |||
Sequence: LYKNHRSSYQTRLNAFREVTPVELPNCNLVKGIETGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNKKEPAVSELEIIGNTLDISSFNPHGISTFTDEDNTVYLLVVNHPDSSSTVEVFKFQEEERSLLHLKTITHELLPRYVYIAELLAHKIHVYEKHANWTLTPLKVLNFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDAENPPGSEVLRIQNILSEDPKITVVYAE | ||||||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 203 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Structure
Sequence
- Sequence statusFragment
- Length256
- Mass (Da)28,760
- Last updated2018-10-10 v9
- ChecksumFBA2842FD441B41B
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 256 | |||||
Sequence: E |
Keywords
- Technical term