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P27169

- PON1_HUMAN

UniProt

P27169 - PON1_HUMAN

Protein

Serum paraoxonase/arylesterase 1

Gene

PON1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation.2 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 calcium ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi53 – 531Calcium 1; catalytic
    Metal bindingi54 – 541Calcium 2
    Active sitei115 – 1151Proton acceptorCurated
    Metal bindingi117 – 1171Calcium 2; via carbonyl oxygen
    Metal bindingi168 – 1681Calcium 1; catalytic
    Metal bindingi169 – 1691Calcium 2
    Metal bindingi224 – 2241Calcium 1; catalytic
    Metal bindingi269 – 2691Calcium 1; catalytic
    Metal bindingi270 – 2701Calcium 1; catalytic

    GO - Molecular functioni

    1. aryldialkylphosphatase activity Source: UniProtKB
    2. arylesterase activity Source: UniProtKB
    3. calcium ion binding Source: UniProtKB
    4. phospholipid binding Source: BHF-UCL
    5. 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. dephosphorylation Source: GOC
    4. organophosphate catabolic process Source: BHF-UCL
    5. phosphatidylcholine metabolic process Source: BHF-UCL
    6. positive regulation of binding Source: BHF-UCL
    7. positive regulation of cholesterol efflux Source: BHF-UCL
    8. positive regulation of transporter activity Source: BHF-UCL
    9. response to external stimulus Source: UniProtKB
    10. response to toxic substance Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.1.2. 2681.
    SABIO-RKP27169.

    Protein family/group databases

    TCDBi1.A.6.2.6. the epithelial na(+) channel (enac) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serum paraoxonase/arylesterase 1 (EC:3.1.1.2, EC:3.1.1.81, EC:3.1.8.1)
    Short name:
    PON 1
    Alternative name(s):
    Aromatic esterase 1
    Short name:
    A-esterase 1
    K-45
    Serum aryldialkylphosphatase 1
    Gene namesi
    Name:PON1
    Synonyms:PON
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9204. PON1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProt
    5. high-density lipoprotein particle Source: BHF-UCL
    6. intracellular membrane-bounded organelle Source: Ensembl
    7. spherical high-density lipoprotein particle Source: BHF-UCL

    Keywords - Cellular componenti

    HDL, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Microvascular complications of diabetes 5 (MVCD5) [MIM:612633]: Pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Homozygosity for the Leu-55 allele is strongly associated with the development of retinal disease in diabetic patients.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi20 – 212HQ → AA: The signal peptide is cleaved; not associated with HDL. 1 Publication
    Mutagenesisi115 – 1151H → Q: Reduces activity 10000-fold. 2 Publications
    Mutagenesisi134 – 1341H → Q: Substantially reduced activity. 2 Publications
    Mutagenesisi284 – 2841C → A or S: No loss of activity. 2 Publications

    Organism-specific databases

    MIMi168820. gene+phenotype.
    612633. phenotype.
    Orphaneti803. Amyotrophic lateral sclerosis.
    PharmGKBiPA33529.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 355354Serum paraoxonase/arylesterase 1PRO_0000223281Add
    BLAST
    Signal peptidei2 – ?Not cleaved

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 353In form B2 Publications
    Glycosylationi227 – 2271N-linked (GlcNAc...)1 Publication
    Glycosylationi253 – 2531N-linked (GlcNAc...)3 Publications
    Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    Glycosylated.3 Publications
    The signal sequence is not cleaved.
    Present in two forms, form B contains a disulfide bond, form A does not.

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP27169.
    PaxDbiP27169.
    PeptideAtlasiP27169.
    PRIDEiP27169.

    2D gel databases

    SWISS-2DPAGEP27169.

    PTM databases

    PhosphoSiteiP27169.

    Expressioni

    Tissue specificityi

    Plasma, associated with HDL (at protein level). Expressed in liver, but not in heart, brain, placenta, lung, skeletal muscle, kidney or pancreas.2 Publications

    Gene expression databases

    ArrayExpressiP27169.
    BgeeiP27169.
    CleanExiHS_PON1.
    GenevestigatoriP27169.

    Organism-specific databases

    HPAiHPA001610.

    Interactioni

    Subunit structurei

    Homodimer. Heterooligomer with phosphate-binding protein (HPBP). Interacts with CLU.4 Publications

    Protein-protein interaction databases

    BioGridi111440. 2 interactions.
    STRINGi9606.ENSP00000222381.

    Structurei

    Secondary structure

    1
    355
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 279
    Turni28 – 314
    Beta strandi54 – 574
    Beta strandi61 – 677
    Beta strandi84 – 896
    Beta strandi92 – 943
    Beta strandi97 – 993
    Beta strandi101 – 1033
    Beta strandi105 – 1073
    Helixi109 – 1113
    Beta strandi114 – 1218
    Beta strandi127 – 1337
    Beta strandi140 – 1478
    Turni148 – 1514
    Beta strandi152 – 1598
    Beta strandi165 – 17410
    Beta strandi177 – 1837
    Helixi189 – 1979
    Beta strandi203 – 2086
    Beta strandi213 – 22816
    Beta strandi232 – 2398
    Turni240 – 2434
    Beta strandi244 – 2507
    Beta strandi256 – 2638
    Beta strandi265 – 2739
    Turni275 – 2773
    Beta strandi280 – 2867
    Helixi288 – 2925
    Beta strandi302 – 3087
    Beta strandi312 – 3143
    Beta strandi316 – 3238
    Beta strandi325 – 3284
    Beta strandi330 – 3378
    Beta strandi340 – 3489
    Beta strandi350 – 3534

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V04X-ray2.20A1-353[»]
    1XHRmodel-A40-355[»]
    ProteinModelPortaliP27169.
    SMRiP27169. Positions 20-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27169.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the paraoxonase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG68009.
    HOGENOMiHOG000252960.
    HOVERGENiHBG003604.
    InParanoidiP27169.
    KOiK01045.
    OMAiMVEFSIT.
    PhylomeDBiP27169.
    TreeFamiTF322436.

    Family and domain databases

    Gene3Di2.120.10.30. 1 hit.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR002640. Arylesterase.
    IPR008363. Paraoxonase1.
    [Graphical view]
    PfamiPF01731. Arylesterase. 1 hit.
    [Graphical view]
    PRINTSiPR01785. PARAOXONASE.
    PR01786. PARAOXONASE1.

    Sequencei

    Sequence statusi: Complete.

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

    P27169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKLIALTLL GMGLALFRNH QSSYQTRLNA LREVQPVELP NCNLVKGIET    50
    GSEDLEILPN GLAFISSGLK YPGIKSFNPN SPGKILLMDL NEEDPTVLEL 100
    GITGSKFDVS SFNPHGISTF TDEDNAMYLL VVNHPDAKST VELFKFQEEE 150
    KSLLHLKTIR HKLLPNLNDI VAVGPEHFYG TNDHYFLDPY LQSWEMYLGL 200
    AWSYVVYYSP SEVRVVAEGF DFANGINISP DGKYVYIAEL LAHKIHVYEK 250
    HANWTLTPLK SLDFNTLVDN ISVDPETGDL WVGCHPNGMK IFFYDSENPP 300
    ASEVLRIQNI LTEEPKVTQV YAENGTVLQG STVASVYKGK LLIGTVFHKA 350
    LYCEL 355
    Length:355
    Mass (Da):39,731
    Last modified:October 5, 2010 - v3
    Checksum:i9B5895509166167E
    GO

    Polymorphismi

    The allelic form of the enzyme with Gln-192 (allozyme A) hydrolyzes paraoxon with a low turnover number and the one with Arg-192 (allozyme B) with a high turnover number.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551L → M.6 Publications
    Corresponds to variant rs854560 [ dbSNP | Ensembl ].
    VAR_006043
    Natural varianti102 – 1021I → V Polymorphism associated with decreased activity that seems to be associated with an increased risk for prostate cancer. 1 Publication
    VAR_015882
    Natural varianti160 – 1601R → G.
    Corresponds to variant rs13306698 [ dbSNP | Ensembl ].
    VAR_055342
    Natural varianti192 – 1921Q → R Polymorphism important for activity. 7 Publications
    Corresponds to variant rs662 [ dbSNP | Ensembl ].
    VAR_006044

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63012 mRNA. Translation: AAB59538.1.
    M63013 mRNA. Translation: AAA60142.1.
    M63014 mRNA. Translation: AAA60143.1.
    S56555, S56546, S56548 Genomic DNA. Translation: AAB25717.1.
    S64696 mRNA. Translation: AAB27899.1.
    S64615 mRNA. Translation: AAB27714.2.
    U55885
    , U55877, U55878, U55879, U55880, U55881, U55882, U55883 Genomic DNA. Translation: AAB41835.1.
    D84371 mRNA. Translation: BAA12327.1.
    U53784 mRNA. Translation: AAA97957.1.
    Z70723 mRNA. Translation: CAA94728.1.
    AK314027 mRNA. Translation: BAG36737.1.
    AF539592 Genomic DNA. Translation: AAM97935.1.
    AC004022 Genomic DNA. Translation: AAC35293.1.
    CH236949 Genomic DNA. Translation: EAL24133.1.
    CH471091 Genomic DNA. Translation: EAW76771.1.
    BC074719 mRNA. Translation: AAH74719.1.
    CCDSiCCDS5638.1.
    PIRiA45451.
    RefSeqiNP_000437.3. NM_000446.5.
    UniGeneiHs.370995.

    Genome annotation databases

    EnsembliENST00000222381; ENSP00000222381; ENSG00000005421.
    GeneIDi5444.
    KEGGihsa:5444.
    UCSCiuc003uns.3. human.

    Polymorphism databases

    DMDMi308153572.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63012 mRNA. Translation: AAB59538.1 .
    M63013 mRNA. Translation: AAA60142.1 .
    M63014 mRNA. Translation: AAA60143.1 .
    S56555 , S56546 , S56548 Genomic DNA. Translation: AAB25717.1 .
    S64696 mRNA. Translation: AAB27899.1 .
    S64615 mRNA. Translation: AAB27714.2 .
    U55885
    , U55877 , U55878 , U55879 , U55880 , U55881 , U55882 , U55883 Genomic DNA. Translation: AAB41835.1 .
    D84371 mRNA. Translation: BAA12327.1 .
    U53784 mRNA. Translation: AAA97957.1 .
    Z70723 mRNA. Translation: CAA94728.1 .
    AK314027 mRNA. Translation: BAG36737.1 .
    AF539592 Genomic DNA. Translation: AAM97935.1 .
    AC004022 Genomic DNA. Translation: AAC35293.1 .
    CH236949 Genomic DNA. Translation: EAL24133.1 .
    CH471091 Genomic DNA. Translation: EAW76771.1 .
    BC074719 mRNA. Translation: AAH74719.1 .
    CCDSi CCDS5638.1.
    PIRi A45451.
    RefSeqi NP_000437.3. NM_000446.5.
    UniGenei Hs.370995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V04 X-ray 2.20 A 1-353 [» ]
    1XHR model - A 40-355 [» ]
    ProteinModelPortali P27169.
    SMRi P27169. Positions 20-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111440. 2 interactions.
    STRINGi 9606.ENSP00000222381.

    Chemistry

    BindingDBi P27169.
    ChEMBLi CHEMBL3167.
    DrugBanki DB01076. Atorvastatin.
    DB01327. Cefazolin.

    Protein family/group databases

    TCDBi 1.A.6.2.6. the epithelial na(+) channel (enac) family.

    PTM databases

    PhosphoSitei P27169.

    Polymorphism databases

    DMDMi 308153572.

    2D gel databases

    SWISS-2DPAGE P27169.

    Proteomic databases

    MaxQBi P27169.
    PaxDbi P27169.
    PeptideAtlasi P27169.
    PRIDEi P27169.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222381 ; ENSP00000222381 ; ENSG00000005421 .
    GeneIDi 5444.
    KEGGi hsa:5444.
    UCSCi uc003uns.3. human.

    Organism-specific databases

    CTDi 5444.
    GeneCardsi GC07M094926.
    H-InvDB HIX0033662.
    HGNCi HGNC:9204. PON1.
    HPAi HPA001610.
    MIMi 168820. gene+phenotype.
    612633. phenotype.
    neXtProti NX_P27169.
    Orphaneti 803. Amyotrophic lateral sclerosis.
    PharmGKBi PA33529.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG68009.
    HOGENOMi HOG000252960.
    HOVERGENi HBG003604.
    InParanoidi P27169.
    KOi K01045.
    OMAi MVEFSIT.
    PhylomeDBi P27169.
    TreeFami TF322436.

    Enzyme and pathway databases

    BRENDAi 3.1.1.2. 2681.
    SABIO-RK P27169.

    Miscellaneous databases

    ChiTaRSi PON1. human.
    EvolutionaryTracei P27169.
    GeneWikii PON1.
    GenomeRNAii 5444.
    NextBioi 21069.
    PROi P27169.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27169.
    Bgeei P27169.
    CleanExi HS_PON1.
    Genevestigatori P27169.

    Family and domain databases

    Gene3Di 2.120.10.30. 1 hit.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR002640. Arylesterase.
    IPR008363. Paraoxonase1.
    [Graphical view ]
    Pfami PF01731. Arylesterase. 1 hit.
    [Graphical view ]
    PRINTSi PR01785. PARAOXONASE.
    PR01786. PARAOXONASE1.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence."
      Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W., Omiecinski C.J., Furlong C.E.
      Biochemistry 30:10141-10149(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-55 AND ARG-192.
      Tissue: Liver.
    2. "Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes."
      Adkins S., Gan K.N., Mody M., La Du B.N.
      Am. J. Hum. Genet. 52:598-608(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS MET-55 AND ARG-192.
    3. "Studies on human serum paraoxonase/arylesterase."
      La Du B.N., Adkins S., Kuo C.L., Lipsig D.
      Chem. Biol. Interact. 87:25-34(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, VARIANTS MET-55 AND ARG-192.
      Tissue: Liver.
    4. "Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification."
      Furlong C.E., Costa L.G., Hassett C., Richter R.J., Sundstrom J.A., Adler D.A., Disteche C.M., Omiecinski C.J., Chapline C., Crabb J.W.
      Chem. Biol. Interact. 87:35-48(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-55 AND ARG-192, CHARACTERIZATION.
      Tissue: Liver.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-55.
      Tissue: Lymphoblast.
    6. "Differential expression of a cDNA clone in human liver versus hepatic cancer -- highly homologous to aryl-dialkyl-phosphatase."
      Wang K.K., Wan D.F., Qiu X.K., Lu P.X., Gu J.R.
      Cell Res. 7:79-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT MET-55.
      Tissue: Liver.
    8. SeattleSNPs variation discovery resource
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-192.
    9. "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].
    10. "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].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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: Brain.
    13. "Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45. Identity of K-45 with paraoxonase."
      Blatter M.-C., James R.W., Messmer S., Barja F., Pometta D.
      Eur. J. Biochem. 211:871-879(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-21, TISSUE SPECIFICITY.
    14. Cited for: PROTEIN SEQUENCE OF 2-21; 234-244; 291-305 AND 350-355, INTERACTION WITH CLU, TISSUE SPECIFICITY, DISULFIDE BOND.
      Tissue: Plasma.
    15. "Purification of rabbit and human serum paraoxonase."
      Furlong C.E., Richter R.J., Chapline C., Crabb J.W.
      Biochemistry 30:10133-10140(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-11, CATALYTIC ACTIVITY.
    16. "Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities."
      Gan K.N., Smolen A., Eckerson H.W., La Du B.N.
      Drug Metab. Dispos. 19:100-106(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    17. "Reconsideration of the catalytic center and mechanism of mammalian paraoxonase/arylesterase."
      Sorenson R.C., Primo-Parmo S.L., Kuo C.-L., Adkins S., Lockridge O., La Du B.N.
      Proc. Natl. Acad. Sci. U.S.A. 92:7187-7191(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-284.
    18. "Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: apolipoprotein A-I stabilizes activity."
      Sorenson R.C., Bisgaier C.L., Aviram M., Hsu C., Billecke S., La Du B.N.
      Arterioscler. Thromb. Vasc. Biol. 19:2214-2225(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF 20-HIS-GLN-21, FUNCTION OF THE UNCLEAVED SIGNAL PEPTIDE.
    19. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253.
      Tissue: Plasma.
    20. "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.
    21. "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-227; ASN-253 AND ASN-324.
      Tissue: Plasma.
    22. Cited for: INTERACTION WITH HPBP.
    23. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253 AND ASN-324.
      Tissue: Liver.
    24. "Structure and evolution of the serum paraoxonase family of detoxifying and anti-atherosclerotic enzymes."
      Harel M., Aharoni A., Gaidukov L., Brumshtein B., Khersonsky O., Meged R., Dvir H., Ravelli R.B.G., McCarthy A., Toker L., Silman I., Sussman J.L., Tawfik D.S.
      Nat. Struct. Mol. Biol. 11:412-419(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS, MUTAGENESIS OF HIS-115 AND HIS-134, CATALYTIC ACTIVITY, DISULFIDE BOND.
    25. "The molecular basis of the human serum paraoxonase activity polymorphism."
      Humbert R., Adler D.A., Disteche C.M., Hassett C., Omiecinski C.J., Furlong C.E.
      Nat. Genet. 3:73-76(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ARG-192.
    26. "A variant of paraoxonase (PON1) gene is associated with diabetic retinopathy in IDDM."
      Kao Y.-L., Donaghue K., Chan A., Knight J., Silink M.
      J. Clin. Endocrinol. Metab. 83:2589-2592(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH DIABETIC RETINOPATHY SUSCEPTIBILITY.
    27. Cited for: VARIANT VAL-102.
    28. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-192.

    Entry informationi

    Entry nameiPON1_HUMAN
    AccessioniPrimary (citable) accession number: P27169
    Secondary accession number(s): B2RA40
    , Q16052, Q6B0J6, Q9UCB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 165 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

    Miscellaneous

    The preferential association of PON1 with HDL is mediated in part by its signal peptide, by binding phospholipids directly, rather than binding apo AI. The retained signal peptide may allow transfer of the protein between phospholipid surfaces.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3