ID PON1_RAT STANDARD; PRT; 354 AA. AC P55159; O08682; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE SERUM PARAOXONASE/ARYLESTERASE 1 (EC 3.1.1.2) (EC 3.1.8.1) (PON 1) DE (SERUM ARYLDIAKYLPHOSPHATASE 1) (A-ESTERASE 1) (AROMATIC ESTERASE 1). GN PON1 OR PON. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. RN [1] RP SEQUENCE OF 10-354 FROM N.A. RA Leviev I.G., Blatter-Garin M.-C., James R.W.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 1-10; 46-55 AND 306-315. RC STRAIN=WISTAR; TISSUE=LIVER; RX MEDLINE; 97184641. 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 SEQUENCE OF 1-25. RA Blatter-Garin M.-C.; RL Submitted (JAN-1995) to the SWISS-PROT data bank. 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: ARYL DIALKYL PHOSPHATE + H(2)O = DIALKYL CC PHOSPHATE + AN ARYL ALCOHOL. CC -!- SUBCELLULAR LOCATION: EXTRACELLULAR. CC -!- TISSUE SPECIFICITY: PLASMA. CC -!- PTM: GLYCOSYLATED (BY SIMILARITY). CC -!- PTM: THE SIGNAL SEQUENCE IS NOT CLEAVED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PARAOXONASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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; -. DR INTERPRO; IPR002640; -. DR PFAM; PF01731; Arylesterase; 1. KW Hydrolase; Glycoprotein; Signal; Multigene family. FT INIT_MET 0 0 FT SIGNAL 1 ? NOT CLEAVED (BY SIMILARITY). FT DISULFID 41 352 BY SIMILARITY. 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 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 //