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Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (K-45) (Serum aryldialkylphosphatase 1)

 PON1_HUMAN              Reviewed;         355 AA.
P27169; B2RA40; Q16052; Q6B0J6; Q9UCB1;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
07-JUN-2017, entry version 190.
RecName: Full=Serum paraoxonase/arylesterase 1 {ECO:0000303|PubMed:7916578};
Short=PON 1 {ECO:0000303|PubMed:15772423};
EC=3.1.1.2 {ECO:0000269|PubMed:15098021, ECO:0000269|PubMed:15772423, ECO:0000269|PubMed:1673382, ECO:0000269|PubMed:1718413, ECO:0000269|PubMed:8393742};
EC=3.1.1.81 {ECO:0000269|PubMed:15098021, ECO:0000269|PubMed:15772423};
EC=3.1.8.1 {ECO:0000269|PubMed:15098021, ECO:0000269|PubMed:15772423, ECO:0000269|PubMed:1673382, ECO:0000269|PubMed:1718413, ECO:0000269|PubMed:8393742};
AltName: Full=Aromatic esterase 1;
Short=A-esterase 1;
AltName: Full=K-45;
AltName: Full=Serum aryldialkylphosphatase 1;
Name=PON1; Synonyms=PON;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MET-55 AND ARG-192.
TISSUE=Liver;
PubMed=1657140; DOI=10.1021/bi00106a010;
Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W.,
Omiecinski C.J., Furlong C.E.;
"Characterization of cDNA clones encoding rabbit and human serum
paraoxonase: the mature protein retains its signal sequence.";
Biochemistry 30:10141-10149(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS MET-55 AND ARG-192.
PubMed=7916578;
Adkins S., Gan K.N., Mody M., La Du B.N.;
"Molecular basis for the polymorphic forms of human serum
paraoxonase/arylesterase: glutamine or arginine at position 191, for
the respective A or B allozymes.";
Am. J. Hum. Genet. 52:598-608(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND VARIANTS MET-55
AND ARG-192.
TISSUE=Liver;
PubMed=8393742; DOI=10.1016/0009-2797(93)90022-Q;
La Du B.N., Adkins S., Kuo C.L., Lipsig D.;
"Studies on human serum paraoxonase/arylesterase.";
Chem. Biol. Interact. 87:25-34(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-55 AND ARG-192, AND
CHARACTERIZATION.
TISSUE=Liver;
PubMed=8393745; DOI=10.1016/0009-2797(93)90023-R;
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.;
"Human and rabbit paraoxonases: purification, cloning, sequencing,
mapping and role of polymorphism in organophosphate detoxification.";
Chem. Biol. Interact. 87:35-48(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-55.
TISSUE=Lymphoblast;
PubMed=8812495; DOI=10.1006/geno.1996.0401;
Clendenning J.B., Humbert R., Green E.D., Wood C., Traver D.,
Furlong C.E.;
"Structural organization of the human PON1 gene.";
Genomics 35:586-589(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=9261565; DOI=10.1038/cr.1997.9;
Wang K.K., Wan D.F., Qiu X.K., Lu P.X., Gu J.R.;
"Differential expression of a cDNA clone in human liver versus hepatic
cancer -- highly homologous to aryl-dialkyl-phosphatase.";
Cell Res. 7:79-90(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-55.
TISSUE=Liver;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-192.
SeattleSNPs variation discovery resource;
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
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.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
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.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 2-21, AND TISSUE SPECIFICITY.
PubMed=8382160; DOI=10.1111/j.1432-1033.1993.tb17620.x;
Blatter M.-C., James R.W., Messmer S., Barja F., Pometta D.;
"Identification of a distinct human high-density lipoprotein
subspecies defined by a lipoprotein-associated protein, K-45. Identity
of K-45 with paraoxonase.";
Eur. J. Biochem. 211:871-879(1993).
[14]
PROTEIN SEQUENCE OF 2-21; 234-244; 291-305 AND 350-355, INTERACTION
WITH CLU, TISSUE SPECIFICITY, AND DISULFIDE BOND.
TISSUE=Plasma;
PubMed=8292612; DOI=10.1021/bi00169a026;
Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E.,
Jordan-Starck T.C., Harmony J.A.K.;
"Apolipoprotein J is associated with paraoxonase in human plasma.";
Biochemistry 33:832-839(1994).
[15]
PROTEIN SEQUENCE OF 2-11, AND CATALYTIC ACTIVITY.
PubMed=1718413; DOI=10.1021/bi00106a009;
Furlong C.E., Richter R.J., Chapline C., Crabb J.W.;
"Purification of rabbit and human serum paraoxonase.";
Biochemistry 30:10133-10140(1991).
[16]
CATALYTIC ACTIVITY.
PubMed=1673382;
Gan K.N., Smolen A., Eckerson H.W., La Du B.N.;
"Purification of human serum paraoxonase/arylesterase. Evidence for
one esterase catalyzing both activities.";
Drug Metab. Dispos. 19:100-106(1991).
[17]
MUTAGENESIS OF CYS-284.
PubMed=7638166; DOI=10.1073/pnas.92.16.7187;
Sorenson R.C., Primo-Parmo S.L., Kuo C.-L., Adkins S., Lockridge O.,
La Du B.N.;
"Reconsideration of the catalytic center and mechanism of mammalian
paraoxonase/arylesterase.";
Proc. Natl. Acad. Sci. U.S.A. 92:7187-7191(1995).
[18]
MUTAGENESIS OF 20-HIS-GLN-21, AND FUNCTION OF THE UNCLEAVED SIGNAL
PEPTIDE.
PubMed=10479665; DOI=10.1161/01.ATV.19.9.2214;
Sorenson R.C., Bisgaier C.L., Aviram M., Hsu C., Billecke S.,
La Du B.N.;
"Human serum paraoxonase/arylesterase's retained hydrophobic N-
terminal leader sequence associates with HDLs by binding
phospholipids: apolipoprotein A-I stabilizes activity.";
Arterioscler. Thromb. Vasc. Biol. 19:2214-2225(1999).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[20]
FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
PubMed=15772423; DOI=10.1194/jlr.M400511-JLR200;
Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R.,
La Du B.N.;
"Human paraoxonases (PON1, PON2, and PON3) are lactonases with
overlapping and distinct substrate specificities.";
J. Lipid Res. 46:1239-1247(2005).
[21]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227; ASN-253 AND ASN-324.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[22]
INTERACTION WITH HPBP.
PubMed=16531243; DOI=10.1016/j.str.2005.12.012;
Morales R., Berna A., Carpentier P., Contreras-Martel C., Renault F.,
Nicodeme M., Chesne-Seck M.-L., Bernier F., Dupuy J., Schaeffer C.,
Diemer H., van Dorsselaer A., Fontecilla-Camps J.C., Masson P.,
Rochu D., Chabriere E.;
"Serendipitous discovery and X-ray structure of a human phosphate
binding apolipoprotein.";
Structure 14:601-609(2006).
[23]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253 AND ASN-324.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM IONS,
MUTAGENESIS OF HIS-115 AND HIS-134, CATALYTIC ACTIVITY, AND DISULFIDE
BOND.
PubMed=15098021; DOI=10.1038/nsmb767;
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.;
"Structure and evolution of the serum paraoxonase family of
detoxifying and anti-atherosclerotic enzymes.";
Nat. Struct. Mol. Biol. 11:412-419(2004).
[26]
VARIANT ARG-192.
PubMed=8098250; DOI=10.1038/ng0193-73;
Humbert R., Adler D.A., Disteche C.M., Hassett C., Omiecinski C.J.,
Furlong C.E.;
"The molecular basis of the human serum paraoxonase activity
polymorphism.";
Nat. Genet. 3:73-76(1993).
[27]
ASSOCIATION WITH DIABETIC RETINOPATHY SUSCEPTIBILITY.
PubMed=9661650; DOI=10.1210/jcem.83.7.5096;
Kao Y.-L., Donaghue K., Chan A., Knight J., Silink M.;
"A variant of paraoxonase (PON1) gene is associated with diabetic
retinopathy in IDDM.";
J. Clin. Endocrinol. Metab. 83:2589-2592(1998).
[28]
VARIANT VAL-102.
PubMed=12783936; DOI=10.1093/jnci/95.11.812;
Marchesani M., Hakkarainen A., Tuomainen T.P., Kaikkonen J.,
Pukkala E., Uimari P., Seppala E., Matikainen M., Kallioniemi O.-P.,
Schleutker J., Lehtimaki T., Salonen J.T.;
"New paraoxonase 1 polymorphism I102V and the risk of prostate cancer
in Finnish men.";
J. Natl. Cancer Inst. 95:812-818(2003).
[29]
VARIANT [LARGE SCALE ANALYSIS] ARG-192.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10479665,
ECO:0000269|PubMed:15772423}.
-!- CATALYTIC ACTIVITY: A phenyl acetate + H(2)O = a phenol + acetate.
{ECO:0000269|PubMed:15098021, ECO:0000269|PubMed:15772423,
ECO:0000269|PubMed:1673382, ECO:0000269|PubMed:1718413,
ECO:0000269|PubMed:8393742}.
-!- CATALYTIC ACTIVITY: An aryl dialkyl phosphate + H(2)O = dialkyl
phosphate + an aryl alcohol. {ECO:0000269|PubMed:15098021,
ECO:0000269|PubMed:15772423, ECO:0000269|PubMed:1673382,
ECO:0000269|PubMed:1718413, ECO:0000269|PubMed:8393742}.
-!- CATALYTIC ACTIVITY: An N-acyl-L-homoserine lactone + H(2)O = an N-
acyl-L-homoserine. {ECO:0000269|PubMed:15098021,
ECO:0000269|PubMed:15772423}.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- SUBUNIT: Homodimer. Heterooligomer with phosphate-binding protein
(HPBP). Interacts with CLU. {ECO:0000269|PubMed:15098021,
ECO:0000269|PubMed:15772423, ECO:0000269|PubMed:16531243,
ECO:0000269|PubMed:8292612}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Plasma, associated with HDL (at protein
level). Expressed in liver, but not in heart, brain, placenta,
lung, skeletal muscle, kidney or pancreas.
{ECO:0000269|PubMed:8292612, ECO:0000269|PubMed:8382160}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}.
-!- PTM: The signal sequence is not cleaved.
-!- PTM: Present in two forms, form B contains a disulfide bond, form
A does not.
-!- POLYMORPHISM: 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.
-!- DISEASE: 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.
-!- 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.
-!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/pon1/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=PON1";
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EMBL; M63012; AAB59538.1; -; mRNA.
EMBL; M63013; AAA60142.1; -; mRNA.
EMBL; M63014; AAA60143.1; -; mRNA.
EMBL; S56555; AAB25717.1; -; Genomic_DNA.
EMBL; S56546; AAB25717.1; JOINED; Genomic_DNA.
EMBL; S56548; AAB25717.1; JOINED; Genomic_DNA.
EMBL; S64696; AAB27899.1; -; mRNA.
EMBL; S64615; AAB27714.2; -; mRNA.
EMBL; U55885; AAB41835.1; -; Genomic_DNA.
EMBL; U55877; AAB41835.1; JOINED; Genomic_DNA.
EMBL; U55878; AAB41835.1; JOINED; Genomic_DNA.
EMBL; U55879; AAB41835.1; JOINED; Genomic_DNA.
EMBL; U55880; AAB41835.1; JOINED; Genomic_DNA.
EMBL; U55881; AAB41835.1; JOINED; Genomic_DNA.
EMBL; U55882; AAB41835.1; JOINED; Genomic_DNA.
EMBL; U55883; AAB41835.1; JOINED; Genomic_DNA.
EMBL; D84371; BAA12327.1; -; mRNA.
EMBL; U53784; AAA97957.1; -; mRNA.
EMBL; Z70723; CAA94728.1; -; mRNA.
EMBL; AK314027; BAG36737.1; -; mRNA.
EMBL; AF539592; AAM97935.1; -; Genomic_DNA.
EMBL; AC004022; AAC35293.1; -; Genomic_DNA.
EMBL; CH236949; EAL24133.1; -; Genomic_DNA.
EMBL; CH471091; EAW76771.1; -; Genomic_DNA.
EMBL; BC074719; AAH74719.1; -; mRNA.
CCDS; CCDS5638.1; -.
PIR; A45451; A45451.
RefSeq; NP_000437.3; NM_000446.5.
UniGene; Hs.370995; -.
PDB; 1V04; X-ray; 2.20 A; A=1-353.
PDB; 1XHR; Model; -; A=40-355.
PDBsum; 1V04; -.
PDBsum; 1XHR; -.
ProteinModelPortal; P27169; -.
SMR; P27169; -.
BioGrid; 111440; 7.
STRING; 9606.ENSP00000222381; -.
BindingDB; P27169; -.
ChEMBL; CHEMBL3167; -.
DrugBank; DB01327; Cefazolin.
TCDB; 1.A.6.2.6; the epithelial na(+) channel (enac) family.
iPTMnet; P27169; -.
PhosphoSitePlus; P27169; -.
BioMuta; PON1; -.
DMDM; 308153572; -.
SWISS-2DPAGE; P27169; -.
MaxQB; P27169; -.
PaxDb; P27169; -.
PeptideAtlas; P27169; -.
PRIDE; P27169; -.
Ensembl; ENST00000222381; ENSP00000222381; ENSG00000005421.
GeneID; 5444; -.
KEGG; hsa:5444; -.
UCSC; uc003uns.4; human.
CTD; 5444; -.
DisGeNET; 5444; -.
GeneCards; PON1; -.
H-InvDB; HIX0033662; -.
HGNC; HGNC:9204; PON1.
HPA; HPA001610; -.
MalaCards; PON1; -.
MIM; 168820; gene+phenotype.
MIM; 612633; phenotype.
neXtProt; NX_P27169; -.
OpenTargets; ENSG00000005421; -.
Orphanet; 803; Amyotrophic lateral sclerosis.
PharmGKB; PA33529; -.
eggNOG; ENOG410IHDV; Eukaryota.
eggNOG; ENOG4111QK7; LUCA.
GeneTree; ENSGT00390000008932; -.
HOGENOM; HOG000252960; -.
HOVERGEN; HBG003604; -.
InParanoid; P27169; -.
KO; K01045; -.
OMA; NCNLVKG; -.
OrthoDB; EOG091G0AV9; -.
PhylomeDB; P27169; -.
TreeFam; TF322436; -.
BRENDA; 3.1.1.2; 2681.
BRENDA; 3.1.1.25; 2681.
BRENDA; 3.1.8.1; 2681.
Reactome; R-HSA-2142688; Synthesis of 5-eicosatetraenoic acids.
SABIO-RK; P27169; -.
ChiTaRS; PON1; human.
EvolutionaryTrace; P27169; -.
GeneWiki; PON1; -.
GenomeRNAi; 5444; -.
PRO; PR:P27169; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000005421; -.
CleanEx; HS_PON1; -.
ExpressionAtlas; P27169; baseline and differential.
Genevisible; P27169; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0034364; C:high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0034366; C:spherical high-density lipoprotein particle; IDA:BHF-UCL.
GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; TAS:Reactome.
GO; GO:0004063; F:aryldialkylphosphatase activity; IDA:UniProtKB.
GO; GO:0004064; F:arylesterase activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005543; F:phospholipid binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
GO; GO:0019439; P:aromatic compound catabolic process; IDA:BHF-UCL.
GO; GO:0046395; P:carboxylic acid catabolic process; IDA:BHF-UCL.
GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
GO; GO:0019372; P:lipoxygenase pathway; TAS:Reactome.
GO; GO:0046434; P:organophosphate catabolic process; IDA:BHF-UCL.
GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:BHF-UCL.
GO; GO:0051099; P:positive regulation of binding; IDA:BHF-UCL.
GO; GO:0010875; P:positive regulation of cholesterol efflux; IDA:BHF-UCL.
GO; GO:0032411; P:positive regulation of transporter activity; IDA:BHF-UCL.
GO; GO:0009605; P:response to external stimulus; NAS:UniProtKB.
GO; GO:0070542; P:response to fatty acid; IEA:Ensembl.
GO; GO:1902617; P:response to fluoride; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR002640; Arylesterase.
InterPro; IPR008363; Paraoxonase1.
PANTHER; PTHR11799:SF20; PTHR11799:SF20; 1.
Pfam; PF01731; Arylesterase; 1.
PRINTS; PR01785; PARAOXONASE.
PRINTS; PR01786; PARAOXONASE1.
1: Evidence at protein level;
3D-structure; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; HDL; Hydrolase; Metal-binding;
Polymorphism; Reference proteome; Secreted; Signal.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1718413,
ECO:0000269|PubMed:8292612,
ECO:0000269|PubMed:8382160}.
CHAIN 2 355 Serum paraoxonase/arylesterase 1.
/FTId=PRO_0000223281.
SIGNAL 2 ? Not cleaved.
ACT_SITE 115 115 Proton acceptor. {ECO:0000305}.
METAL 53 53 Calcium 1; catalytic.
METAL 54 54 Calcium 2.
METAL 117 117 Calcium 2; via carbonyl oxygen.
METAL 168 168 Calcium 1; catalytic.
METAL 169 169 Calcium 2.
METAL 224 224 Calcium 1; catalytic.
METAL 269 269 Calcium 1; catalytic.
METAL 270 270 Calcium 1; catalytic.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
DISULFID 42 353 In form B. {ECO:0000269|PubMed:15098021,
ECO:0000269|PubMed:8292612}.
VARIANT 55 55 L -> M (in dbSNP:rs854560).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:1657140,
ECO:0000269|PubMed:7916578,
ECO:0000269|PubMed:8393742,
ECO:0000269|PubMed:8393745,
ECO:0000269|PubMed:8812495}.
/FTId=VAR_006043.
VARIANT 102 102 I -> V (polymorphism; may be associated
with an increased risk for prostate
cancer; associated with decreased
activity; dbSNP:rs72552787).
{ECO:0000269|PubMed:12783936}.
/FTId=VAR_015882.
VARIANT 160 160 R -> G (in dbSNP:rs13306698).
/FTId=VAR_055342.
VARIANT 192 192 Q -> R (polymorphism; important for
activity; dbSNP:rs662).
{ECO:0000269|PubMed:1657140,
ECO:0000269|PubMed:18987736,
ECO:0000269|PubMed:7916578,
ECO:0000269|PubMed:8098250,
ECO:0000269|PubMed:8393742,
ECO:0000269|PubMed:8393745,
ECO:0000269|Ref.8}.
/FTId=VAR_006044.
MUTAGEN 20 21 HQ->AA: The signal peptide is cleaved;
not associated with HDL.
{ECO:0000269|PubMed:10479665}.
MUTAGEN 115 115 H->Q: Reduces activity 10000-fold.
{ECO:0000269|PubMed:15098021}.
MUTAGEN 134 134 H->Q: Substantially reduced activity.
{ECO:0000269|PubMed:15098021}.
MUTAGEN 284 284 C->A,S: No loss of activity.
{ECO:0000269|PubMed:7638166}.
HELIX 19 27 {ECO:0000244|PDB:1V04}.
TURN 28 31 {ECO:0000244|PDB:1V04}.
STRAND 54 57 {ECO:0000244|PDB:1V04}.
STRAND 61 67 {ECO:0000244|PDB:1V04}.
STRAND 84 89 {ECO:0000244|PDB:1V04}.
STRAND 92 94 {ECO:0000244|PDB:1V04}.
STRAND 97 99 {ECO:0000244|PDB:1V04}.
STRAND 101 103 {ECO:0000244|PDB:1V04}.
STRAND 105 107 {ECO:0000244|PDB:1V04}.
HELIX 109 111 {ECO:0000244|PDB:1V04}.
STRAND 114 121 {ECO:0000244|PDB:1V04}.
STRAND 127 133 {ECO:0000244|PDB:1V04}.
STRAND 140 147 {ECO:0000244|PDB:1V04}.
TURN 148 151 {ECO:0000244|PDB:1V04}.
STRAND 152 159 {ECO:0000244|PDB:1V04}.
STRAND 165 174 {ECO:0000244|PDB:1V04}.
STRAND 177 183 {ECO:0000244|PDB:1V04}.
HELIX 189 197 {ECO:0000244|PDB:1V04}.
STRAND 203 208 {ECO:0000244|PDB:1V04}.
STRAND 213 228 {ECO:0000244|PDB:1V04}.
STRAND 232 239 {ECO:0000244|PDB:1V04}.
TURN 240 243 {ECO:0000244|PDB:1V04}.
STRAND 244 250 {ECO:0000244|PDB:1V04}.
STRAND 256 263 {ECO:0000244|PDB:1V04}.
STRAND 265 273 {ECO:0000244|PDB:1V04}.
TURN 275 277 {ECO:0000244|PDB:1V04}.
STRAND 280 286 {ECO:0000244|PDB:1V04}.
HELIX 288 292 {ECO:0000244|PDB:1V04}.
STRAND 302 308 {ECO:0000244|PDB:1V04}.
STRAND 312 314 {ECO:0000244|PDB:1V04}.
STRAND 316 323 {ECO:0000244|PDB:1V04}.
STRAND 325 328 {ECO:0000244|PDB:1V04}.
STRAND 330 337 {ECO:0000244|PDB:1V04}.
STRAND 340 348 {ECO:0000244|PDB:1V04}.
STRAND 350 353 {ECO:0000244|PDB:1V04}.
SEQUENCE 355 AA; 39731 MW; 9B5895509166167E CRC64;
MAKLIALTLL GMGLALFRNH QSSYQTRLNA LREVQPVELP NCNLVKGIET GSEDLEILPN
GLAFISSGLK YPGIKSFNPN SPGKILLMDL NEEDPTVLEL GITGSKFDVS SFNPHGISTF
TDEDNAMYLL VVNHPDAKST VELFKFQEEE KSLLHLKTIR HKLLPNLNDI VAVGPEHFYG
TNDHYFLDPY LQSWEMYLGL AWSYVVYYSP SEVRVVAEGF DFANGINISP DGKYVYIAEL
LAHKIHVYEK HANWTLTPLK SLDFNTLVDN ISVDPETGDL WVGCHPNGMK IFFYDSENPP
ASEVLRIQNI LTEEPKVTQV YAENGTVLQG STVASVYKGK LLIGTVFHKA LYCEL


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