ID PON1_RAT Reviewed; 354 AA. AC P55159; O08682; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 12-DEC-2006, entry version 45. 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. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, AND MASS RP SPECTROMETRY. RX PubMed=16641100; DOI=10.1073/pnas.0600895103; RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: RT regulation of aquaporin-2 phosphorylation at two sites."; RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). 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: A phenyl acetate + H(2)O = a phenol + acetate. CC -!- CATALYTIC ACTIVITY: An aryl dialkyl phosphate + H(2)O = dialkyl CC phosphate + an aryl alcohol. 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 PDB; 1V04; X-ray; A=-. DR SMR; P55159; 15-354. DR GermOnline; ENSRNOG00000008902; Rattus norvegicus. DR Ensembl; ENSRNOG00000008902; Rattus norvegicus. DR RGD; 620062; Pon1. DR ArrayExpress; P55159; -. DR GO; GO:0004063; F:aryldialkylphosphatase activity; IDA:RGD. DR GO; GO:0006629; P:lipid metabolism; IEP:RGD. 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 Phosphorylation; Signal. FT INIT_MET 0 0 FT CHAIN 1 354 Serum paraoxonase/arylesterase 1. FT /FTId=PRO_0000223284. FT SIGNAL 1 ? Not cleaved. FT MOD_RES 75 75 Phosphoserine. FT MOD_RES 79 79 Phosphoserine. 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 //