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Protein

Serum paraoxonase/lactonase 3

Gene

PON3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

A phenyl acetate + H2O = a phenol + acetate.1 Publication
An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.1 Publication
An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine.1 Publication

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi53Calcium 1; catalyticBy similarity1
Metal bindingi54Calcium 2By similarity1
Active sitei114Proton acceptorBy similarity1
Metal bindingi116Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi167Calcium 1; catalyticBy similarity1
Metal bindingi168Calcium 2By similarity1
Metal bindingi223Calcium 1; catalyticBy similarity1
Metal bindingi268Calcium 1; catalyticBy similarity1
Metal bindingi269Calcium 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

  • aromatic compound catabolic process Source: BHF-UCL
  • carboxylic acid catabolic process Source: BHF-UCL
  • coumarin catabolic process Source: Ensembl
  • negative regulation of superoxide anion generation Source: Ensembl
  • phenylacetate catabolic process Source: Ensembl
  • response to external stimulus Source: UniProtKB
  • response to toxic substance Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105852-MONOMER.
BRENDAi3.1.1.2. 2681.
3.1.1.25. 2681.
3.1.8.1. 2681.
ReactomeiR-HSA-2142688. Synthesis of 5-eicosatetraenoic acids.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum paraoxonase/lactonase 3 (EC:3.1.1.2, EC:3.1.1.81, EC:3.1.8.1)
Gene namesi
Name:PON3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9206. PON3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi5446.
MalaCardsiPON3.
OpenTargetsiENSG00000105852.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA33531.

Chemistry databases

DrugBankiDB00974. Edetic Acid.
DB00227. Lovastatin.

Polymorphism and mutation databases

BioMutaiPON3.
DMDMi50403778.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002232902 – 354Serum paraoxonase/lactonase 3Add BLAST353
Signal peptidei2 – ?Not cleavedSequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi42 ↔ 352By similarity
Modified residuei165PhosphoserineCombined sources1
Glycosylationi269N-linked (GlcNAc...)Sequence analysis1
Glycosylationi323N-linked (GlcNAc...)1 Publication1

Post-translational modificationi

The signal sequence is not cleaved.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiQ15166.
MaxQBiQ15166.
PaxDbiQ15166.
PeptideAtlasiQ15166.
PRIDEiQ15166.

PTM databases

iPTMnetiQ15166.
PhosphoSitePlusiQ15166.

Expressioni

Gene expression databases

BgeeiENSG00000105852.
CleanExiHS_PON3.
ExpressionAtlasiQ15166. baseline and differential.
GenevisibleiQ15166. HS.

Organism-specific databases

HPAiCAB025250.
HPA014848.

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi111442. 2 interactors.
IntActiQ15166. 1 interactor.
STRINGi9606.ENSP00000265627.

Structurei

3D structure databases

ProteinModelPortaliQ15166.
SMRiQ15166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the paraoxonase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHDV. Eukaryota.
ENOG4111QK7. LUCA.
GeneTreeiENSGT00390000008932.
HOVERGENiHBG003604.
InParanoidiQ15166.
KOiK01045.
OMAiQKYVYVA.
OrthoDBiEOG091G0AV9.
PhylomeDBiQ15166.
TreeFamiTF322436.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008364. Paraoxonase2.
[Graphical view]
PfamiPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSiPR01785. PARAOXONASE.
PR01787. PARAOXONASE2.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKLVALVLL GVGLSLVGEM FLAFRERVNA SREVEPVEPE NCHLIEELES
60 70 80 90 100
GSEDIDILPS GLAFISSGLK YPGMPNFAPD EPGKIFLMDL NEQNPRAQAL
110 120 130 140 150
EISGGFDKEL FNPHGISIFI DKDNTVYLYV VNHPHMKSTV EIFKFEEQQR
160 170 180 190 200
SLVYLKTIKH ELLKSVNDIV VLGPEQFYAT RDHYFTNSLL SFFEMILDLR
210 220 230 240 250
WTYVLFYSPR EVKVVAKGFC SANGITVSAD QKYVYVADVA AKNIHIMEKH
260 270 280 290 300
DNWDLTQLKV IQLGTLVDNL TVDPATGDIL AGCHPNPMKL LNYNPEDPPG
310 320 330 340 350
SEVLRIQNVL SEKPRVSTVY ANNGSVLQGT SVASVYHGKI LIGTVFHKTL

YCEL
Length:354
Mass (Da):39,607
Last modified:July 19, 2004 - v3
Checksum:i1B861B35E8533921
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18G → E in AAC41996 (PubMed:8661009).Curated1
Sequence conflicti32R → Q in AAC41996 (PubMed:8661009).Curated1
Sequence conflicti50S → N in AAH70374 (PubMed:15489334).Curated1
Sequence conflicti58 – 59LP → FL in AAK07629 (Ref. 1) Curated2
Sequence conflicti63A → S in AAC41996 (PubMed:8661009).Curated1
Sequence conflicti68G → E in AAC41996 (PubMed:8661009).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021082146E → K.1 PublicationCorresponds to variant rs17878827dbSNPEnsembl.1
Natural variantiVAR_021083179A → D.1 PublicationCorresponds to variant rs17883013dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320003 mRNA. Translation: AAK07629.1.
AF329433 mRNA. Translation: AAO15365.1.
AY805220 Genomic DNA. Translation: AAV50000.1.
AC004022 Genomic DNA. No translation available.
AC005021 Genomic DNA. No translation available.
CH236949 Genomic DNA. Translation: EAL24132.1.
CH471091 Genomic DNA. Translation: EAW76768.1.
BC070374 mRNA. Translation: AAH70374.1.
L48516 mRNA. Translation: AAC41996.1.
CCDSiCCDS5639.1.
RefSeqiNP_000931.1. NM_000940.2.
UniGeneiHs.440967.

Genome annotation databases

EnsembliENST00000265627; ENSP00000265627; ENSG00000105852.
GeneIDi5446.
KEGGihsa:5446.
UCSCiuc003unt.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF320003 mRNA. Translation: AAK07629.1.
AF329433 mRNA. Translation: AAO15365.1.
AY805220 Genomic DNA. Translation: AAV50000.1.
AC004022 Genomic DNA. No translation available.
AC005021 Genomic DNA. No translation available.
CH236949 Genomic DNA. Translation: EAL24132.1.
CH471091 Genomic DNA. Translation: EAW76768.1.
BC070374 mRNA. Translation: AAH70374.1.
L48516 mRNA. Translation: AAC41996.1.
CCDSiCCDS5639.1.
RefSeqiNP_000931.1. NM_000940.2.
UniGeneiHs.440967.

3D structure databases

ProteinModelPortaliQ15166.
SMRiQ15166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111442. 2 interactors.
IntActiQ15166. 1 interactor.
STRINGi9606.ENSP00000265627.

Chemistry databases

DrugBankiDB00974. Edetic Acid.
DB00227. Lovastatin.

PTM databases

iPTMnetiQ15166.
PhosphoSitePlusiQ15166.

Polymorphism and mutation databases

BioMutaiPON3.
DMDMi50403778.

Proteomic databases

EPDiQ15166.
MaxQBiQ15166.
PaxDbiQ15166.
PeptideAtlasiQ15166.
PRIDEiQ15166.

Protocols and materials databases

DNASUi5446.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265627; ENSP00000265627; ENSG00000105852.
GeneIDi5446.
KEGGihsa:5446.
UCSCiuc003unt.4. human.

Organism-specific databases

CTDi5446.
DisGeNETi5446.
GeneCardsiPON3.
HGNCiHGNC:9206. PON3.
HPAiCAB025250.
HPA014848.
MalaCardsiPON3.
MIMi602720. gene.
neXtProtiNX_Q15166.
OpenTargetsiENSG00000105852.
Orphaneti803. Amyotrophic lateral sclerosis.
PharmGKBiPA33531.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHDV. Eukaryota.
ENOG4111QK7. LUCA.
GeneTreeiENSGT00390000008932.
HOVERGENiHBG003604.
InParanoidiQ15166.
KOiK01045.
OMAiQKYVYVA.
OrthoDBiEOG091G0AV9.
PhylomeDBiQ15166.
TreeFamiTF322436.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000105852-MONOMER.
BRENDAi3.1.1.2. 2681.
3.1.1.25. 2681.
3.1.8.1. 2681.
ReactomeiR-HSA-2142688. Synthesis of 5-eicosatetraenoic acids.

Miscellaneous databases

GeneWikiiPON3.
GenomeRNAii5446.
PROiQ15166.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000105852.
CleanExiHS_PON3.
ExpressionAtlasiQ15166. baseline and differential.
GenevisibleiQ15166. HS.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008364. Paraoxonase2.
[Graphical view]
PfamiPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSiPR01785. PARAOXONASE.
PR01787. PARAOXONASE2.
ProtoNetiSearch...

Entry informationi

Entry nameiPON3_HUMAN
AccessioniPrimary (citable) accession number: Q15166
Secondary accession number(s): A4D1H8
, O75855, O76060, Q6IRU9, Q8IX97, Q9BZH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2004
Last modified: November 30, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.