ID PON1_RAT STANDARD; PRT; 354 AA. AC P55159; O08682; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 04-APR-2006, entry version 40. DE Serum paraoxonase/arylesterase 1 (EC 3.1.1.2) (EC 3.1.8.1) (PON 1) DE (Serum aryldialkylphosphatase 1) (A-esterase 1) (Aromatic esterase 1). GN Name=Pon1; Synonyms=Pon; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-354. 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. RN [2] RP PROTEIN SEQUENCE OF 1-10; 46-55 AND 306-315. RC STRAIN=Wistar; TISSUE=Liver; RX MEDLINE=97184641; PubMed=9032442; RA Rodrigo L., Gil F., Hernandez A.F., Marina A., Vazquez J., Pla A.; RT "Purification and characterization of paraoxon hydrolase from rat RT liver."; RL Biochem. J. 321:595-601(1997). RN [3] RP PROTEIN SEQUENCE OF 1-25. RA Blatter M.-C.; RL Submitted (JAN-1995) to Swiss-Prot. CC -!- FUNCTION: Hydrolyzes the toxic metabolites of a variety of CC organophosphorus insecticides. Capable of hydrolyzing a broad CC spectrum of organophosphate substrates and a number of aromatic CC carboxylic acid esters. CC -!- CATALYTIC ACTIVITY: An aryl dialkyl phosphate + H(2)O = dialkyl CC phosphate + an aryl alcohol. CC -!- CATALYTIC ACTIVITY: A phenyl acetate + H(2)O = a phenol + acetate. CC -!- SUBCELLULAR LOCATION: Secreted protein; extracellular space. CC -!- TISSUE SPECIFICITY: Plasma. Associated with HDL. CC -!- PTM: Glycosylated (By similarity). 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 CC may allow transfer of the protein between phospholipid surfaces CC (By similarity). CC -!- SIMILARITY: Belongs to the paraoxonase family. 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; U94856; AAB53441.1; -; mRNA. DR UniGene; Rn.20732; -. DR PDB; 1V04; X-ray; A=-. DR SMR; P55159; 15-354. DR Ensembl; ENSRNOG00000008902; Rattus norvegicus. DR RGD; 620062; Pon1. DR GO; GO:0004063; F:aryldialkylphosphatase activity; IDA. DR InterPro; IPR002640; Arylesterase. DR InterPro; IPR008363; Paraoxonase1. DR Pfam; PF01731; Arylesterase; 1. DR PRINTS; PR01785; PARAOXONASE. DR PRINTS; PR01786; PARAOXONASE1. KW 3D-structure; Direct protein sequencing; Glycoprotein; HDL; Hydrolase; KW Signal. FT INIT_MET 0 0 FT CHAIN 1 354 Serum paraoxonase/arylesterase 1. FT /FTId=PRO_0000223284. FT SIGNAL 1 ? Not cleaved. FT CARBOHYD 252 252 N-linked (GlcNAc...) (Potential). FT CARBOHYD 269 269 N-linked (GlcNAc...) (Potential). FT CARBOHYD 323 323 N-linked (GlcNAc...) (Potential). FT DISULFID 41 352 By similarity. FT CONFLICT 19 25 HRSSYQT -> PLXDWYR (in Ref. 3). SQ SEQUENCE 354 AA; 39365 MW; 43F374025D91F50A CRC64; AKLLGLTLVG LVLALYKNHR SSYQTRLNAF REVTPVDLPN CTLVKGIEAG AEDLEILPNG LTFFSTFLKY PGIKSFDPSK PGKILLMDLN EKEPAVSELA IMGNTLDMSS FNPHGISTFI DEDNTVYLLV VSHPDSSSTV EVFKFQEEER SLLHLKTITH ELLPSINDIA AVGPESFYAT NDHYFADPYL RSWEMYLGLS WSNVVYYSPD KVRVVADGFD FANGIGISLD GKYVYIAELL AHKIHVYEKH ANWTLTPLKV LSFDTLVDNI SVDPVTGDLW VGCHPNGMRI FFYDSENPPG SEVLRIQSIL SEDPKVTVVY AENGTVLQGT TVAAVYKGKL LIGTVFHRAL CCYL //