Reviewed, UniProtKB/Swiss-Prot P27169 (PON1_HUMAN)

Names and origin

Protein names

Recommended name:
    Serum paraoxonase/arylesterase 1
      Short name=PON 1
    EC=3.1.1.2
    EC=3.1.8.1
Alternative name(s):
    Serum aryldialkylphosphatase 1
    A-esterase 1
    Aromatic esterase 1
    K-45

Gene names

Name:	PON1
Synonyms:	PON

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters. May mediate an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. Ref.18
Catalytic activity	A phenyl acetate + H2O = a phenol + acetate. Ref.3 Ref.15 Ref.16 An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. Ref.3 Ref.15 Ref.16
Subunit structure	Heterooligomer with phosphate-binding protein (HPBP). Interacts with CLU. Ref.14 Ref.21
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. Ref.14 Ref.13
Post-translational modification	Glycosylated. Ref.19 Ref.20 Ref.22 The signal sequence is not cleaved. 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.
Involvement in disease	Genetic variation in PON1 is associated with susceptibility to diabetic retinopathy [MIM:612633]; also called microvascular complications of diabetes type 5 (MVCD5). Diabetic retinopathy is a major cause of blindness in diabetic patients. Retinal disease results from adverse effects on the blood vessels which supply the retina.
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.
Sequence similarities	Belongs to the paraoxonase family.

Ontologies

Keywords
Cellular component	HDL Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	aromatic compound catabolic process Inferred from direct assay. Source: UniProtKB carboxylic acid catabolic process Ref.17 Inferred from direct assay. Source: UniProtKB organophosphate catabolic process Ref.17 Inferred from direct assay. Source: UniProtKB phosphatidylcholine metabolic process Inferred from direct assay. Source: UniProtKB positive regulation of binding Inferred from direct assay. Source: UniProtKB positive regulation of cholesterol efflux Inferred from direct assay. Source: UniProtKB positive regulation of transporter activity Inferred from direct assay. Source: UniProtKB response to external stimulus Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	spherical high-density lipoprotein particle Inferred from direct assay. Source: UniProtKB
Molecular function	aryldialkylphosphatase activity Ref.17 Inferred from direct assay. Source: UniProtKB arylesterase activity Ref.16 Ref.17 Non-traceable author statement. Source: UniProtKB phospholipid binding Ref.18 Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.15 Ref.14 Ref.13

Chain

2 – 355

354

Serum paraoxonase/arylesterase 1

PRO_0000223281

Signal peptide

2 – ?

Not cleaved

Amino acid modifications

Modified residue

76

1

Phosphoserine By similarity

Glycosylation

227

1

N-linked (GlcNAc...) Ref.20

Glycosylation

253

1

N-linked (GlcNAc...) Ref.19 Ref.20 Ref.22

Glycosylation

270

1

N-linked (GlcNAc...) Potential

Glycosylation

324

1

N-linked (GlcNAc...) Ref.20 Ref.22

Disulfide bond

42 ↔ 353

In form B Ref.14

Natural variations

Natural variant

55

1

M → L Associated with susceptibility to diabetic retinopathy. dbSNP rs854560. Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.25

VAR_006043

Natural variant

102

1

I → V Polymorphism associated with decreased activity that seems to be associated with an increased risk for prostate cancer. Ref.26

VAR_015882

Natural variant

160

1

R → G: dbSNP rs13306698.

VAR_055342

Natural variant

192

1

Q → R Polymorphism important for activity. dbSNP rs662. Ref.3 Ref.1 Ref.4 Ref.8 Ref.2 Ref.24 Ref.27

VAR_006044

Experimental info

Mutagenesis

20 – 21

2

HQ → AA: The signal peptide is cleaved; not associated with HDL. Ref.18

Mutagenesis

284

1

C → A or S: No loss of activity. Ref.18 Ref.17

Secondary structure

1

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355

Helix Strand Turn

Details...

Helix

18 – 26

9

Turn

27 – 30

4

Beta strand

53 – 56

4

Beta strand

60 – 66

7

Beta strand

83 – 88

6

Beta strand

91 – 93

3

Beta strand

96 – 98

3

Beta strand

100 – 102

3

Beta strand

104 – 106

3

Helix

108 – 110

3

Beta strand

113 – 120

8

Beta strand

126 – 132

7

Beta strand

139 – 146

8

Turn

147 – 150

4

Beta strand

151 – 158

8

Beta strand

164 – 173

10

Beta strand

176 – 182

7

Helix

188 – 196

9

Beta strand

202 – 207

6

Beta strand

212 – 227

16

Beta strand

231 – 238

8

Turn

239 – 242

4

Beta strand

243 – 249

7

Beta strand

255 – 262

8

Beta strand

264 – 272

9

Turn

274 – 276

3

Beta strand

279 – 285

7

Helix

287 – 291

5

Beta strand

301 – 307

7

Beta strand

311 – 313

3

Beta strand

315 – 322

8

Beta strand

324 – 327

4

Beta strand

329 – 336

8

Beta strand

339 – 347

9

Beta strand

349 – 353

5

Sequences

	Sequence		Length	Mass (Da)
	P27169-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 9A2F4E3DE036536A	FASTA	355	39,749
	10 20 30 40 50 60 MAKLIALTLL GMGLALFRNH QSSYQTRLNA LREVQPVELP NCNLVKGIET GSEDMEILPN 70 80 90 100 110 120 GLAFISSGLK YPGIKSFNPN SPGKILLMDL NEEDPTVLEL GITGSKFDVS SFNPHGISTF 130 140 150 160 170 180 TDEDNAMYLL VVNHPDAKST VELFKFQEEE KSLLHLKTIR HKLLPNLNDI VAVGPEHFYG 190 200 210 220 230 240 TNDHYFLDPY LQSWEMYLGL AWSYVVYYSP SEVRVVAEGF DFANGINISP DGKYVYIAEL 250 260 270 280 290 300 LAHKIHVYEK HANWTLTPLK SLDFNTLVDN ISVDPETGDL WVGCHPNGMK IFFYDSENPP 310 320 330 340 350 ASEVLRIQNI LTEEPKVTQV YAENGTVLQG STVASVYKGK LLIGTVFHKA LYCEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1657140] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-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: 7916578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT 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: 8393742] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, VARIANT 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: 8393745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-55 AND ARG-192, CHARACTERIZATION. Tissue: Liver.
[5]	"Structural organization of the human PON1 gene." Clendenning J.B., Humbert R., Green E.D., Wood C., Traver D., Furlong C.E. Genomics 35:586-589(1996) [PubMed: 8812495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LEU-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: 9261565] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-55. 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[8]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-55 AND 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: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-55.
[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: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-55.
[11]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-55.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-55. 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: 8382160] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, TISSUE SPECIFICITY.
[14]	"Apolipoprotein J is associated with paraoxonase in human plasma." Kelso G.J., Stuart W.D., Richter R.J., Furlong C.E., Jordan-Starck T.C., Harmony J.A.K. Biochemistry 33:832-839(1994) [PubMed: 8292612] [Abstract] 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: 1718413] [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: 1673382] [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: 7638166] [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: 10479665] [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: 14760718] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, MASS SPECTROMETRY. Tissue: Plasma.
[20]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-227; ASN-253 AND ASN-324, MASS SPECTROMETRY. Tissue: Plasma.
[21]	"Serendipitous discovery and X-ray structure of a human phosphate binding apolipoprotein." 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. Structure 14:601-609(2006) [PubMed: 16531243] [Abstract] Cited for: INTERACTION WITH HPBP.
[22]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253 AND ASN-324, MASS SPECTROMETRY. Tissue: Liver.
[23]	"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., McCarthy A., Toker L., Silman I., Sussman J.L., Tawfik D.S. Nat. Struct. Mol. Biol. 11:412-419(2004) [PubMed: 15098021] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[24]	"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: 8098250] [Abstract] Cited for: VARIANT ARG-192.
[25]	"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: 9661650] [Abstract] Cited for: VARIANT LEU-55, ASSOCIATION WITH DIABETIC RETINOPATHY SUSCEPTIBILITY.
[26]	"New paraoxonase 1 polymorphism I102V and the risk of prostate cancer in Finnish men." 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. J. Natl. Cancer Inst. 95:812-818(2003) [PubMed: 12783936] [Abstract] Cited for: VARIANT VAL-102.
[27]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." 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. Nature 456:66-72(2008) [PubMed: 18987736] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-192.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBLGenBankDDBJ

M63012 mRNA. Translation: AAB59538.1.
M63013 mRNA. Translation: AAA60142.1.
M63014 mRNA. Translation: AAA60143.1.
S56555, S56546, S56548 Genomic DNA. Translation: AAB25717.1.
S64696 Unassigned DNA. 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.

IPI

IPI00218732.

PIR

A45451.

RefSeq

NP_000437.3.

UniGene

Hs.370995

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1V04	X-ray	2.20	A	1-353	[»]
1XHR	model	-	A	40-355	[»]

SMR

P27169. Positions 16-355.

ModBase

Search...

Protein-protein interaction databases

STRING

P27169.

2-D gel databases

SWISS-2DPAGE

P27169.

Proteomic databases

PeptideAtlas

P27169.

PRIDE

P27169.

Genome annotation databases

Ensembl

ENST00000222381; ENSP00000222381; ENSG00000005421; Homo sapiens. [Genome view]
ENST00000433729; ENSP00000407359; ENSG00000005421; Homo sapiens. [Genome view]

GeneID

5444.

KEGG

hsa:5444.

UCSC

uc003uns.1. human.

Organism-specific databases

CTD

5444.

GeneCards

GC07M094764.

H-InvDB

HIX0033662.

HGNC

HGNC:9204. PON1.

HPA

HPA001610.

MIM

168820. gene+phenotype.
612633. phenotype.

PharmGKB

PA33529.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P27169.

HOVERGEN

P27169.

Enzyme and pathway databases

BRENDA

3.1.1.2. 247.
3.1.8.1. 247.

Gene expression databases

ArrayExpress

P27169.

Bgee

P27169.

CleanEx

HS_PON1.

Genevestigator

P27169.

GermOnline

ENSG00000005421. Homo sapiens.

Family and domain databases

InterPro

IPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008363. Paraoxonase1.
[Graphical view]

Gene3D

G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.

Pfam

PF01731. Arylesterase. 1 hit.
[Graphical view]

PRINTS

PR01785. PARAOXONASE.
PR01786. PARAOXONASE1.

ProtoNet

Search...

Other Resources

DrugBank

DB01076. Atorvastatin.
DB01327. Cefazolin.

NextBio

21069.

SOURCE

Search...

Entry information

Entry name

PON1_HUMAN

Accession

Primary (citable) accession number: P27169
Secondary accession number(s): B2RA40 , Q16052, Q6B0J6, Q9UCB1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	January 23, 2007
Last modified:	October 13, 2009
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.