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Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (Serum aryldialkylphosphatase 1)

 PON1_RABIT              Reviewed;         359 AA.
P27170; Q9BGN1; Q9BGN2; Q9BGN3;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 124.
RecName: Full=Serum paraoxonase/arylesterase 1;
Short=PON 1;
EC=3.1.1.2 {ECO:0000269|PubMed:1718413};
EC=3.1.1.81 {ECO:0000269|PubMed:1718413};
EC=3.1.8.1 {ECO:0000269|PubMed:1718413};
AltName: Full=Aromatic esterase 1;
Short=A-esterase 1;
AltName: Full=Serum aryldialkylphosphatase 1;
Name=PON1; Synonyms=PON;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Liver;
PubMed=1657140; DOI=10.1021/bi00106a010;
Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W.,
Omiecinski C.J., Furlong C.E.;
"Characterization of cDNA clones encoding rabbit and human serum
paraoxonase: the mature protein retains its signal sequence.";
Biochemistry 30:10141-10149(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Liver;
PubMed=8393745; DOI=10.1016/0009-2797(93)90023-R;
Furlong C.E., Costa L.G., Hassett C., Richter R.J., Sundstrom J.A.,
Adler D.A., Disteche C.M., Omiecinski C.J., Chapline C., Crabb J.W.;
"Human and rabbit paraoxonases: purification, cloning, sequencing,
mapping and role of polymorphism in organophosphate detoxification.";
Chem. Biol. Interact. 87:35-48(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS SER-82; GLU-93 AND
GLY-101.
STRAIN=New Zealand white; TISSUE=Liver;
PubMed=11266077; DOI=10.1097/00008571-200103000-00003;
Watson C.E., Draganov D.I., Billecke S.S., Bisgaier C.L., La Du B.N.;
"Rabbits possess a serum paraoxonase polymorphism similar to the human
Q192R.";
Pharmacogenetics 11:123-134(2001).
[4]
PROTEIN SEQUENCE OF 2-21, AND CATALYTIC ACTIVITY.
PubMed=1718413; DOI=10.1021/bi00106a009;
Furlong C.E., Richter R.J., Chapline C., Crabb J.W.;
"Purification of rabbit and human serum paraoxonase.";
Biochemistry 30:10133-10140(1991).
-!- FUNCTION: Hydrolyzes the toxic metabolites of a variety of
organophosphorus insecticides. Capable of hydrolyzing a broad
spectrum of organophosphate substrates and lactones, and a number
of aromatic carboxylic acid esters. Mediates an enzymatic
protection of low density lipoproteins against oxidative
modification. {ECO:0000269|PubMed:11266077}.
-!- CATALYTIC ACTIVITY:
Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310;
EC=3.1.1.2; Evidence={ECO:0000269|PubMed:1718413};
-!- CATALYTIC ACTIVITY:
Reaction=An aryl dialkyl phosphate + H(2)O = dialkyl phosphate +
an aryl alcohol.; EC=3.1.8.1;
Evidence={ECO:0000269|PubMed:1718413};
-!- CATALYTIC ACTIVITY:
Reaction=an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-
homoserine + H(+); Xref=Rhea:RHEA:22576, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:55474, ChEBI:CHEBI:58921;
EC=3.1.1.81; Evidence={ECO:0000269|PubMed:1718413};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000250|UniProtKB:P27169};
Note=Binds 2 calcium ions per subunit.
{ECO:0000250|UniProtKB:P27169};
-!- SUBUNIT: Homodimer. Interacts with CLU.
{ECO:0000250|UniProtKB:P27169}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space.
-!- TISSUE SPECIFICITY: Plasma. Associated with HDL.
-!- PTM: Glycosylated.
-!- PTM: The signal sequence is not cleaved.
-!- POLYMORPHISM: There are two allelic forms, allozyme A and B, which
differ in their substrate specificity. Both forms have similar
arylesterase activity but allozyme B possesses greater paraoxonase
activity. Allozyme A is better at protecting LDL from oxidation.
-!- MISCELLANEOUS: The preferential association of PON1 with HDL is
mediated in part by its signal peptide, by binding phospholipids
directly, rather than binding apo AI. The retained signal peptide
may allow transfer of the protein between phospholipid surfaces.
{ECO:0000250|UniProtKB:P27169}.
-!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK06398.1; Type=Erroneous termination; Positions=356; Note=Translated as Ser.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M63011; AAA31452.1; -; mRNA.
EMBL; S64616; AAB27713.2; -; mRNA.
EMBL; AF220941; AAK06398.1; ALT_SEQ; mRNA.
EMBL; AF220942; AAK06399.1; -; mRNA.
EMBL; AF220943; AAK06400.1; -; mRNA.
PIR; B40354; B40354.
RefSeq; NP_001075766.1; NM_001082297.1.
UniGene; Ocu.1952; -.
ProteinModelPortal; P27170; -.
SMR; P27170; -.
STRING; 9986.ENSOCUP00000004445; -.
GeneID; 100009133; -.
KEGG; ocu:100009133; -.
CTD; 5444; -.
eggNOG; ENOG410IHDV; Eukaryota.
eggNOG; ENOG4111QK7; LUCA.
HOGENOM; HOG000252960; -.
HOVERGEN; HBG003604; -.
InParanoid; P27170; -.
KO; K01045; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
GO; GO:0016209; F:antioxidant activity; IDA:UniProtKB.
GO; GO:0004063; F:aryldialkylphosphatase activity; ISS:UniProtKB.
GO; GO:0004064; F:arylesterase activity; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0046683; P:response to organophosphorus; IDA:UniProtKB.
Gene3D; 2.120.10.30; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR002640; Arylesterase.
InterPro; IPR008363; Paraoxonase1.
PANTHER; PTHR11799:SF16; PTHR11799:SF16; 1.
Pfam; PF01731; Arylesterase; 1.
PRINTS; PR01785; PARAOXONASE.
PRINTS; PR01786; PARAOXONASE1.
1: Evidence at protein level;
Antioxidant; Calcium; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; HDL; Hydrolase; Metal-binding;
Polymorphism; Reference proteome; Secreted; Signal.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:1718413}.
CHAIN 2 359 Serum paraoxonase/arylesterase 1.
/FTId=PRO_0000223283.
SIGNAL 2 ? Not cleaved.
ACT_SITE 115 115 Proton acceptor.
{ECO:0000250|UniProtKB:P27169}.
METAL 53 53 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 54 54 Calcium 2.
{ECO:0000250|UniProtKB:P27169}.
METAL 117 117 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P27169}.
METAL 168 168 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 169 169 Calcium 2.
{ECO:0000250|UniProtKB:P27169}.
METAL 224 224 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 269 269 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
METAL 270 270 Calcium 1; catalytic.
{ECO:0000250|UniProtKB:P27169}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 324 324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 42 353 {ECO:0000250|UniProtKB:P27169}.
VARIANT 82 82 P -> S (in allele A).
{ECO:0000269|PubMed:11266077}.
VARIANT 93 93 K -> E (in allele A).
{ECO:0000269|PubMed:11266077}.
VARIANT 101 101 S -> G (in allele A).
{ECO:0000269|PubMed:11266077}.
CONFLICT 67 67 A -> S (in Ref. 3; AAK06398/AAK06399/
AAK06400). {ECO:0000305}.
CONFLICT 320 320 A -> V (in Ref. 3; AAK06398).
{ECO:0000305}.
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


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