ID PON1_RAT Reviewed; 355 AA. AC P55159; O08682; Q5BJN6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 29-MAY-2024, entry version 161. DE RecName: Full=Serum paraoxonase/arylesterase 1; DE Short=PON 1; DE EC=3.1.1.2 {ECO:0000250|UniProtKB:P27169}; DE EC=3.1.1.81 {ECO:0000250|UniProtKB:P27169}; DE EC=3.1.8.1 {ECO:0000250|UniProtKB:P27169}; DE AltName: Full=Aromatic esterase 1; DE Short=A-esterase 1; DE AltName: Full=Serum aryldialkylphosphatase 1; GN Name=Pon1; Synonyms=Pon; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 2-11; 47-56 AND 307-316. RC STRAIN=Wistar; TISSUE=Liver; RX PubMed=9032442; DOI=10.1042/bj3210595; RA Rodrigo L., Gil F., Hernandez A.F., Marina A., Vazquez J., Pla A.; RT "Purification and characterization of paraoxon hydrolase from rat liver."; RL Biochem. J. 321:595-601(1997). RN [4] RP PROTEIN SEQUENCE OF 2-26. RA Blatter M.-C.; RL Submitted (JAN-1995) to UniProtKB. RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-355. RA Leviev I.G., Blatter M.-C., James R.W.; RT "Rat paraoxonase partial mRNA sequence."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Hydrolyzes the toxic metabolites of a variety of CC organophosphorus insecticides. Capable of hydrolyzing a broad spectrum CC of organophosphate substrates and lactones, and a number of aromatic CC carboxylic acid esters. Mediates an enzymatic protection of low density CC lipoproteins against oxidative modification. CC {ECO:0000250|UniProtKB:P27169}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); CC Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; CC Evidence={ECO:0000250|UniProtKB:P27169}; CC -!- CATALYTIC ACTIVITY: CC Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl CC alcohol.; EC=3.1.8.1; Evidence={ECO:0000250|UniProtKB:P27169}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine CC + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:55474, ChEBI:CHEBI:58921; EC=3.1.1.81; CC Evidence={ECO:0000250|UniProtKB:P27169}; CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 2 calcium ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. Interacts with CLU. {ECO:0000250|UniProtKB:P27169}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- TISSUE SPECIFICITY: Plasma. Associated with HDL. CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P27169}. CC -!- PTM: The signal sequence is not cleaved. CC -!- MISCELLANEOUS: The preferential association of PON1 with HDL is CC mediated in part by its signal peptide, by binding phospholipids CC directly, rather than binding apo AI. The retained signal peptide may CC allow transfer of the protein between phospholipid surfaces. CC {ECO:0000250|UniProtKB:P27169}. CC -!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH473959; EDM15017.1; -; Genomic_DNA. DR EMBL; BC091403; AAH91403.1; -; mRNA. DR EMBL; U94856; AAB53441.1; -; mRNA. DR PIR; PT0088; PT0088. DR RefSeq; NP_114466.1; NM_032077.1. DR AlphaFoldDB; P55159; -. DR SMR; P55159; -. DR IntAct; P55159; 1. DR STRING; 10116.ENSRNOP00000011823; -. DR GlyCosmos; P55159; 3 sites, No reported glycans. DR GlyGen; P55159; 3 sites. DR iPTMnet; P55159; -. DR PhosphoSitePlus; P55159; -. DR PaxDb; 10116-ENSRNOP00000011823; -. DR GeneID; 84024; -. DR KEGG; rno:84024; -. DR UCSC; RGD:620062; rat. DR AGR; RGD:620062; -. DR CTD; 5444; -. DR RGD; 620062; Pon1. DR VEuPathDB; HostDB:ENSRNOG00000008902; -. DR eggNOG; ENOG502S3B5; Eukaryota. DR HOGENOM; CLU_049839_0_1_1; -. DR InParanoid; P55159; -. DR OrthoDB; 2874974at2759; -. DR PhylomeDB; P55159; -. DR TreeFam; TF322436; -. DR BRENDA; 3.1.1.2; 5301. DR BRENDA; 3.1.8.1; 5301. DR Reactome; R-RNO-2142688; Synthesis of 5-eicosatetraenoic acids. DR Reactome; R-RNO-9754706; Atorvastatin ADME. DR PRO; PR:P55159; -. DR Proteomes; UP000002494; Chromosome 4. DR Proteomes; UP000234681; Chromosome 4. DR Bgee; ENSRNOG00000008902; Expressed in liver and 16 other cell types or tissues. DR GO; GO:0005615; C:extracellular space; IDA:RGD. DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD. DR GO; GO:0034366; C:spherical high-density lipoprotein particle; ISO:RGD. DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC. DR GO; GO:0004063; F:aryldialkylphosphatase activity; IDA:RGD. DR GO; GO:0004064; F:arylesterase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR GO; GO:0005543; F:phospholipid binding; ISO:RGD. DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD. DR GO; GO:0019439; P:aromatic compound catabolic process; ISO:RGD. DR GO; GO:0046395; P:carboxylic acid catabolic process; ISO:RGD. DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD. DR GO; GO:0046434; P:organophosphate catabolic process; ISO:RGD. DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:RGD. DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD. DR GO; GO:0070542; P:response to fatty acid; IEP:RGD. DR GO; GO:1902617; P:response to fluoride; IDA:RGD. DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD. DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD. DR GO; GO:0009636; P:response to toxic substance; ISO:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD. DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR002640; Arylesterase. DR InterPro; IPR008363; Paraoxonase1. DR PANTHER; PTHR11799; PARAOXONASE; 1. DR PANTHER; PTHR11799:SF16; SERUM PARAOXONASE_ARYLESTERASE 1; 1. DR Pfam; PF01731; Arylesterase; 1. DR PRINTS; PR01785; PARAOXONASE. DR PRINTS; PR01786; PARAOXONASE1. DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1. PE 1: Evidence at protein level; KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein; HDL; KW Hydrolase; Metal-binding; Reference proteome; Secreted; Signal. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9032442, ECO:0000269|Ref.4" FT CHAIN 2..355 FT /note="Serum paraoxonase/arylesterase 1" FT /id="PRO_0000223284" FT SIGNAL 2..? FT /note="Not cleaved" FT ACT_SITE 115 FT /note="Proton acceptor" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 54 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 117 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 169 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 224 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 269 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P27169" FT BINDING 270 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:P27169" FT CARBOHYD 253 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 270 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 324 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 42..353 FT /evidence="ECO:0000250|UniProtKB:P27169" FT CONFLICT 20..26 FT /note="HRSSYQT -> PLXDWYR (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 68 FT /note="G -> F (in Ref. 5; AAB53441)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="D -> Y (in Ref. 5; AAB53441)" FT /evidence="ECO:0000305" SQ SEQUENCE 355 AA; 39358 MW; FE2886875D01E52D CRC64; MAKLLGLTLV GLVLALYKNH RSSYQTRLNA FREVTPVDLP NCTLVKGIEA GAEDLEILPN GLTFFSTGLK YPGIKSFDPS KPGKILLMDL NEKEPAVSEL AIMGNTLDMS SFNPHGISTF IDEDNTVYLL VVSHPDSSST VEVFKFQEEE RSLLHLKTIT HELLPSINDI AAVGPESFYA TNDHYFADPY LRSWEMYLGL SWSNVVYYSP DKVRVVADGF DFANGIGISL DGKYVYIAEL LAHKIHVYEK HANWTLTPLK VLSFDTLVDN ISVDPVTGDL WVGCHPNGMR IFFYDSENPP GSEVLRIQSI LSEDPKVTVV YAENGTVLQG TTVAAVYKGK LLIGTVFHRA LCCDL //