PON1_RAT
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 03-AUG-2022, entry version 153.
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}.
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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 GlyGen; P55159; 3 sites.
DR iPTMnet; P55159; -.
DR PhosphoSitePlus; P55159; -.
DR PaxDb; P55159; -.
DR PRIDE; P55159; -.
DR GeneID; 84024; -.
DR KEGG; rno:84024; -.
DR UCSC; RGD:620062; rat.
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 OMA; NAMYLLV; -.
DR OrthoDB; 888266at2759; -.
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 tissues.
DR Genevisible; P55159; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA: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:0006629; P:lipid metabolic process; IEP:RGD.
DR GO; GO:0046434; P:organophosphate catabolic process; ISO:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; ISO:RGD.
DR GO; GO:0051099; P:positive regulation of binding; ISO:RGD.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; ISO:RGD.
DR GO; GO:0032411; P:positive regulation of transporter activity; 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:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; ISO:RGD.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR008363; Paraoxonase1.
DR PANTHER; PTHR11799:SF16; PTHR11799:SF16; 1.
DR Pfam; PF01731; Arylesterase; 1.
DR PRINTS; PR01785; PARAOXONASE.
DR PRINTS; PR01786; PARAOXONASE1.
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
