ID PON1_RAT Reviewed; 355 AA. AC P55159; O08682; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 09-FEB-2010, entry version 80. DE RecName: Full=Serum paraoxonase/arylesterase 1; DE Short=PON 1; DE EC=3.1.1.2; DE EC=3.1.8.1; DE AltName: Full=Serum aryldialkylphosphatase 1; DE AltName: Full=Aromatic esterase 1; DE Short=A-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 PROTEIN SEQUENCE OF 2-11; 47-56 AND 307-316. 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 [2] RP PROTEIN SEQUENCE OF 2-26. RA Blatter M.-C.; RL Submitted (JAN-1995) to UniProtKB. RN [3] 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. RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-80, AND MASS RP SPECTROMETRY. RC TISSUE=Kidney; 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 -!- COFACTOR: Binds 2 calcium ions per subunit (By similarity). CC -!- SUBUNIT: Interacts with CLU (By similarity). CC -!- SUBCELLULAR LOCATION: Secreted, 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 IPI; IPI00231264; -. DR PIR; PT0088; PT0088. DR RefSeq; NP_114466.1; -. DR UniGene; Rn.20732; -. DR SMR; P55159; 16-355. DR STRING; P55159; -. DR PRIDE; P55159; -. DR Ensembl; ENSRNOT00000011823; ENSRNOP00000011823; ENSRNOG00000008902; Rattus norvegicus. DR GeneID; 84024; -. DR KEGG; rno:84024; -. DR UCSC; NM_032077; rat. DR CTD; 84024; -. DR RGD; 620062; Pon1. DR eggNOG; roNOG04341; -. DR HOVERGEN; P55159; -. DR InParanoid; P55159; -. DR BRENDA; 3.1.1.2; 248. DR BRENDA; 3.1.8.1; 248. DR NextBio; 616593; -. DR ArrayExpress; P55159; -. DR Genevestigator; P55159; -. DR GermOnline; ENSRNOG00000008902; Rattus norvegicus. DR GO; GO:0005792; C:microsome; IDA:RGD. DR GO; GO:0004063; F:aryldialkylphosphatase activity; ISS:UniProtKB. DR GO; GO:0004064; F:arylesterase activity; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB. DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like. DR InterPro; IPR002640; Arylesterase. DR InterPro; IPR008363; Paraoxonase1. DR Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 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; Phosphoprotein; Secreted; Signal. FT SIGNAL 1 ? Not cleaved. FT INIT_MET 1 1 Removed. FT CHAIN 2 355 Serum paraoxonase/arylesterase 1. FT /FTId=PRO_0000223284. FT ACT_SITE 115 115 Proton acceptor (By similarity). FT METAL 53 53 Calcium 1; catalytic (By similarity). FT METAL 54 54 Calcium 2 (By similarity). FT METAL 117 117 Calcium 2; via carbonyl oxygen (By FT similarity). FT METAL 168 168 Calcium 1; catalytic (By similarity). FT METAL 169 169 Calcium 2 (By similarity). FT METAL 224 224 Calcium 1; catalytic (By similarity). FT METAL 269 269 Calcium 1; catalytic (By similarity). FT METAL 270 270 Calcium 1; catalytic (By similarity). FT MOD_RES 76 76 Phosphoserine. FT MOD_RES 80 80 Phosphoserine. FT CARBOHYD 253 253 N-linked (GlcNAc...) (Potential). FT CARBOHYD 270 270 N-linked (GlcNAc...) (Potential). FT CARBOHYD 324 324 N-linked (GlcNAc...) (Potential). FT DISULFID 42 353 By similarity. FT CONFLICT 20 26 HRSSYQT -> PLXDWYR (in Ref. 2; AA FT sequence). SQ SEQUENCE 355 AA; 39496 MW; 93F8AAF7A75E402D CRC64; MAKLLGLTLV GLVLALYKNH RSSYQTRLNA FREVTPVDLP NCTLVKGIEA GAEDLEILPN GLTFFSTFLK 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 LCCYL //