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A0A2R9BCI1 · A0A2R9BCI1_PANPA

Function

Catalytic activity

Cofactor

Ca2+ (UniProtKB | Rhea| CHEBI:29108 )

Note: Binds 2 calcium ions per subunit.

Features

Showing features for binding site, active site.

135450100150200250300350
Type
IDPosition(s)Description
Binding site53Ca2+ 1 (UniProtKB | ChEBI); catalytic
Binding site54Ca2+ 2 (UniProtKB | ChEBI)
Active site115Proton acceptor
Binding site117Ca2+ 2 (UniProtKB | ChEBI)
Binding site168Ca2+ 1 (UniProtKB | ChEBI); catalytic
Binding site169Ca2+ 2 (UniProtKB | ChEBI)
Binding site224Ca2+ 1 (UniProtKB | ChEBI); catalytic
Binding site269Ca2+ 1 (UniProtKB | ChEBI); catalytic
Binding site270Ca2+ 1 (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentspherical high-density lipoprotein particle
Molecular Functionacyl-L-homoserine-lactone lactonohydrolase activity
Molecular Functionaryldialkylphosphatase activity
Molecular Functionarylesterase activity
Molecular Functioncalcium ion binding
Molecular Functionphospholipid binding
Molecular Functionprotein homodimerization activity
Biological Processcarboxylic acid catabolic process
Biological Processcholesterol metabolic process
Biological Processlactone catabolic process
Biological Processorganophosphate catabolic process
Biological Processphosphatidylcholine metabolic process
Biological Processpositive regulation of cholesterol efflux
Biological Processresponse to toxic substance

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Paraoxonase
  • EC number

Gene names

    • Name
      PON1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pan

Accessions

  • Primary accession
    A0A2R9BCI1

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

Type
IDPosition(s)Description
Signal1-15
ChainPRO_501534031516-354Paraoxonase
Disulfide bond42↔352In form B
Glycosylation253N-linked (GlcNAc...) asparagine
Glycosylation270N-linked (GlcNAc...) asparagine
Glycosylation323N-linked (GlcNAc...) asparagine

Post-translational modification

Glycosylated.

Keywords

Expression

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the paraoxonase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    354
  • Mass (Da)
    39,638
  • Last updated
    2018-06-20 v1
  • MD5 Checksum
    A8E5DC4793141E63FB43B67D813C404A
MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKLLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLRSWEIYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJFE02030127
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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