PON1_RABIT
ID PON1_RABIT Reviewed; 359 AA.
AC P27170; Q9BGN1; Q9BGN2; Q9BGN3;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Serum paraoxonase/arylesterase 1;
DE Short=PON 1;
DE EC=3.1.1.2 {ECO:0000269|PubMed:1718413};
DE EC=3.1.1.81 {ECO:0000269|PubMed:1718413};
DE EC=3.1.8.1 {ECO:0000269|PubMed:1718413};
DE AltName: Full=Aromatic esterase 1;
DE Short=A-esterase 1;
DE AltName: Full=Serum aryldialkylphosphatase 1;
GN Name=PON1; Synonyms=PON;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=1657140; DOI=10.1021/bi00106a010;
RA Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W.,
RA Omiecinski C.J., Furlong C.E.;
RT "Characterization of cDNA clones encoding rabbit and human serum
RT paraoxonase: the mature protein retains its signal sequence.";
RL Biochemistry 30:10141-10149(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Liver;
RX PubMed=8393745; DOI=10.1016/0009-2797(93)90023-r;
RA Furlong C.E., Costa L.G., Hassett C., Richter R.J., Sundstrom J.A.,
RA Adler D.A., Disteche C.M., Omiecinski C.J., Chapline C., Crabb J.W.;
RT "Human and rabbit paraoxonases: purification, cloning, sequencing, mapping
RT and role of polymorphism in organophosphate detoxification.";
RL Chem. Biol. Interact. 87:35-48(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS SER-82; GLU-93 AND
RP GLY-101.
RC STRAIN=New Zealand white; TISSUE=Liver;
RX PubMed=11266077; DOI=10.1097/00008571-200103000-00003;
RA Watson C.E., Draganov D.I., Billecke S.S., Bisgaier C.L., La Du B.N.;
RT "Rabbits possess a serum paraoxonase polymorphism similar to the human
RT Q192R.";
RL Pharmacogenetics 11:123-134(2001).
RN [4]
RP PROTEIN SEQUENCE OF 2-21, AND CATALYTIC ACTIVITY.
RX PubMed=1718413; DOI=10.1021/bi00106a009;
RA Furlong C.E., Richter R.J., Chapline C., Crabb J.W.;
RT "Purification of rabbit and human serum paraoxonase.";
RL Biochemistry 30:10133-10140(1991).
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:0000269|PubMed:11266077}.
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:0000269|PubMed:1718413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl
CC alcohol.; EC=3.1.8.1; Evidence={ECO:0000269|PubMed:1718413};
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:0000269|PubMed:1718413};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P27169};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:P27169};
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.
CC -!- PTM: The signal sequence is not cleaved.
CC -!- POLYMORPHISM: There are two allelic forms, allozyme A and B, which
CC differ in their substrate specificity. Both forms have similar
CC arylesterase activity but allozyme B possesses greater paraoxonase
CC activity. Allozyme A is better at protecting LDL from oxidation.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK06398.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; M63011; AAA31452.1; -; mRNA.
DR EMBL; S64616; AAB27713.2; -; mRNA.
DR EMBL; AF220941; AAK06398.1; ALT_SEQ; mRNA.
DR EMBL; AF220942; AAK06399.1; -; mRNA.
DR EMBL; AF220943; AAK06400.1; -; mRNA.
DR PIR; B40354; B40354.
DR RefSeq; NP_001075766.1; NM_001082297.1.
DR AlphaFoldDB; P27170; -.
DR SMR; P27170; -.
DR STRING; 9986.ENSOCUP00000004445; -.
DR PRIDE; P27170; -.
DR GeneID; 100009133; -.
DR KEGG; ocu:100009133; -.
DR CTD; 5444; -.
DR eggNOG; ENOG502S3B5; Eukaryota.
DR InParanoid; P27170; -.
DR OrthoDB; 888266at2759; -.
DR BRENDA; 3.1.1.2; 1749.
DR BRENDA; 3.1.8.1; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
DR GO; GO:0004063; F:aryldialkylphosphatase activity; ISS:UniProtKB.
DR GO; GO:0004064; F:arylesterase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0046683; P:response to organophosphorus; IDA:UniProtKB.
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 Antioxidant; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; HDL; Hydrolase; Metal-binding; Reference proteome; Secreted;
KW Signal.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1718413"
FT CHAIN 2..359
FT /note="Serum paraoxonase/arylesterase 1"
FT /id="PRO_0000223283"
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 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 VARIANT 82
FT /note="P -> S (in allele A)"
FT /evidence="ECO:0000269|PubMed:11266077"
FT VARIANT 93
FT /note="K -> E (in allele A)"
FT /evidence="ECO:0000269|PubMed:11266077"
FT VARIANT 101
FT /note="S -> G (in allele A)"
FT /evidence="ECO:0000269|PubMed:11266077"
FT CONFLICT 67
FT /note="A -> S (in Ref. 3; AAK06398/AAK06399/AAK06400)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="A -> V (in Ref. 3; AAK06398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40010 MW; 535124A736EE312A CRC64;
MAKLTALTLL GLGLALFDGQ KSSFQTRFNV HREVTPVELP NCNLVKGIDN GSEDLEILPN
GLAFISAGLK YPGIMSFDPD KPGKILLMDL NEKDPVVLEL SITGSTFDLS SFNPHGISTF
TDEDNIVYLM VVNHPDSKST VELFKFQEKE KSLLHLKTIR HKLLPSVNDI VAVGPEHFYA
TNDHYFIDPY LKSWEMHLGL AWSFVTYYSP NDVRVVAEGF DFANGINISP DGKYVYIAEL
LAHKIHVYEK HANWTLTPLK SLDFNTLVDN ISVDPVTGDL WVGCHPNGMR IFYYDPKNPP
ASEVLRIQDI LSKEPKVTVA YAENGTVLQG STVAAVYKGK MLVGTVFHKA LYCELSQAN
