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Q15166

- PON3_HUMAN

UniProt

Q15166 - PON3_HUMAN

Protein

Serum paraoxonase/lactonase 3

Gene

PON3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 3 (19 Jul 2004)
      Previous versions | rss
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    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

    Binds 2 calcium ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Calcium 1; catalyticBy similarity
    Metal bindingi54 – 541Calcium 2By similarity
    Active sitei114 – 1141Proton acceptorBy similarity
    Metal bindingi116 – 1161Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi167 – 1671Calcium 1; catalyticBy similarity
    Metal bindingi168 – 1681Calcium 2By similarity
    Metal bindingi223 – 2231Calcium 1; catalyticBy similarity
    Metal bindingi268 – 2681Calcium 1; catalyticBy similarity
    Metal bindingi269 – 2691Calcium 1; catalyticBy similarity

    GO - Molecular functioni

    1. 3,4-dihydrocoumarin hydrolase activity Source: Ensembl
    2. aryldialkylphosphatase activity Source: UniProtKB-EC
    3. arylesterase activity Source: UniProtKB
    4. dihydrocoumarin hydrolase activity Source: Ensembl
    5. metal ion binding Source: UniProtKB-KW
    6. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. aromatic compound catabolic process Source: BHF-UCL
    2. carboxylic acid catabolic process Source: BHF-UCL
    3. coumarin catabolic process Source: Ensembl
    4. phenylacetate catabolic process Source: Ensembl
    5. response to external stimulus Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    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
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9206. PON3.

    Subcellular locationi

    Secretedextracellular space By similarity

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. intracellular membrane-bounded organelle Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA33531.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 354353Serum paraoxonase/lactonase 3PRO_0000223290Add
    BLAST
    Signal peptidei2 – ?Not cleavedSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi42 ↔ 352By similarity
    Modified residuei165 – 1651Phosphoserine1 Publication
    Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi323 – 3231N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    The signal sequence is not cleaved.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ15166.
    PaxDbiQ15166.
    PeptideAtlasiQ15166.
    PRIDEiQ15166.

    PTM databases

    PhosphoSiteiQ15166.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15166.
    BgeeiQ15166.
    CleanExiHS_PON3.
    GenevestigatoriQ15166.

    Organism-specific databases

    HPAiCAB025250.
    HPA014848.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    IntActiQ15166. 1 interaction.
    STRINGi9606.ENSP00000265627.

    Structurei

    3D structure databases

    ProteinModelPortaliQ15166.
    SMRiQ15166. Positions 23-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the paraoxonase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG68009.
    HOVERGENiHBG003604.
    InParanoidiQ15166.
    KOiK01045.
    OMAiHVLFYSP.
    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

    MGKLVALVLL GVGLSLVGEM FLAFRERVNA SREVEPVEPE NCHLIEELES    50
    GSEDIDILPS GLAFISSGLK YPGMPNFAPD EPGKIFLMDL NEQNPRAQAL 100
    EISGGFDKEL FNPHGISIFI DKDNTVYLYV VNHPHMKSTV EIFKFEEQQR 150
    SLVYLKTIKH ELLKSVNDIV VLGPEQFYAT RDHYFTNSLL SFFEMILDLR 200
    WTYVLFYSPR EVKVVAKGFC SANGITVSAD QKYVYVADVA AKNIHIMEKH 250
    DNWDLTQLKV IQLGTLVDNL TVDPATGDIL AGCHPNPMKL LNYNPEDPPG 300
    SEVLRIQNVL SEKPRVSTVY ANNGSVLQGT SVASVYHGKI LIGTVFHKTL 350
    YCEL 354
    Length:354
    Mass (Da):39,607
    Last modified:July 19, 2004 - v3
    Checksum:i1B861B35E8533921
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181G → E in AAC41996. (PubMed:8661009)Curated
    Sequence conflicti32 – 321R → Q in AAC41996. (PubMed:8661009)Curated
    Sequence conflicti50 – 501S → N in AAH70374. (PubMed:15489334)Curated
    Sequence conflicti58 – 592LP → FL in AAK07629. 1 PublicationCurated
    Sequence conflicti63 – 631A → S in AAC41996. (PubMed:8661009)Curated
    Sequence conflicti68 – 681G → E in AAC41996. (PubMed:8661009)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti146 – 1461E → K.1 Publication
    Corresponds to variant rs17878827 [ dbSNP | Ensembl ].
    VAR_021082
    Natural varianti179 – 1791A → D.1 Publication
    Corresponds to variant rs17883013 [ dbSNP | Ensembl ].
    VAR_021083

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human.

    Polymorphism databases

    DMDMi50403778.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5639.1.
    RefSeqi NP_000931.1. NM_000940.2.
    UniGenei Hs.440967.

    3D structure databases

    ProteinModelPortali Q15166.
    SMRi Q15166. Positions 23-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q15166. 1 interaction.
    STRINGi 9606.ENSP00000265627.

    PTM databases

    PhosphoSitei Q15166.

    Polymorphism databases

    DMDMi 50403778.

    Proteomic databases

    MaxQBi Q15166.
    PaxDbi Q15166.
    PeptideAtlasi Q15166.
    PRIDEi Q15166.

    Protocols and materials databases

    DNASUi 5446.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265627 ; ENSP00000265627 ; ENSG00000105852 .
    GeneIDi 5446.
    KEGGi hsa:5446.
    UCSCi uc003unt.3. human.

    Organism-specific databases

    CTDi 5446.
    GeneCardsi GC07M094989.
    HGNCi HGNC:9206. PON3.
    HPAi CAB025250.
    HPA014848.
    MIMi 602720. gene.
    neXtProti NX_Q15166.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    PharmGKBi PA33531.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68009.
    HOVERGENi HBG003604.
    InParanoidi Q15166.
    KOi K01045.
    OMAi HVLFYSP.
    PhylomeDBi Q15166.
    TreeFami TF322436.

    Miscellaneous databases

    GeneWikii PON3.
    GenomeRNAii 5446.
    NextBioi 21079.
    PROi Q15166.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15166.
    Bgeei Q15166.
    CleanExi HS_PON3.
    Genevestigatori Q15166.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR002640. Arylesterase.
    IPR008364. Paraoxonase2.
    [Graphical view ]
    Pfami PF01731. Arylesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR01785. PARAOXONASE.
    PR01787. PARAOXONASE2.
    ProtoNeti Search...

    Publicationsi

    1. "Human paraoxanase-3 is an HDL-associated enzyme."
      Reddy S.T., Wadleigh D.J., Grijalva V., Ng C., Hama S., Gangopadhyay A., Khorsan R., Shih D., Lusis A.J., Navab M., Fogelman A.M.
      Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hepatoma.
    2. "Human PON3 has lactonase activity."
      Draganov D.I., Watson C.E.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    3. SeattleSNPs variation discovery resource
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-146 AND ASP-179.
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    8. "The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family."
      Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N.
      Genomics 33:498-507(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-354.
      Tissue: Liver.
    9. "Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities."
      Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., La Du B.N.
      J. Lipid Res. 46:1239-1247(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-323.
      Tissue: Plasma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.

    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: October 1, 2014
    This is version 119 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

    External Data

    Dasty 3