PON3_RABIT
ID PON3_RABIT Reviewed; 354 AA.
AC Q9BGN0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Serum paraoxonase/lactonase 3;
DE EC=3.1.1.2;
DE EC=3.1.1.81;
DE EC=3.1.8.1;
GN Name=PON3;
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], PROTEIN SEQUENCE OF 2-20, AND FUNCTION.
RC STRAIN=New Zealand white; TISSUE=Serum;
RX PubMed=10931838; DOI=10.1074/jbc.m004543200;
RA Draganov D.I., Stetson P.L., Watson C.E., Billecke S.S., La Du B.N.;
RT "Rabbit serum paraoxonase 3 (PON3) is a high density lipoprotein-associated
RT lactonase and protects low density lipoprotein against oxidation.";
RL J. Biol. Chem. 275:33435-33442(2000).
CC -!- FUNCTION: Has low activity towards the organophosphate paraxon and
CC aromatic carboxylic acid esters (By similarity). Rapidly hydrolyzes
CC lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic
CC lactones and 5- or 6-member ring lactones with aliphatic substituents
CC but not simple lactones or those with polar substituents. {ECO:0000250,
CC ECO:0000269|PubMed:10931838}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl
CC alcohol.; EC=3.1.8.1;
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: Glycosylated. {ECO:0000250}.
CC -!- PTM: The signal sequence is not cleaved. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the paraoxonase family. {ECO:0000305}.
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DR EMBL; AF220944; AAK06401.1; -; mRNA.
DR RefSeq; NP_001075547.1; NM_001082078.2.
DR AlphaFoldDB; Q9BGN0; -.
DR SMR; Q9BGN0; -.
DR PRIDE; Q9BGN0; -.
DR GeneID; 100008754; -.
DR KEGG; ocu:100008754; -.
DR CTD; 5446; -.
DR InParanoid; Q9BGN0; -.
DR OrthoDB; 888266at2759; -.
DR BRENDA; 3.1.1.2; 1749.
DR BRENDA; 3.1.1.25; 1749.
DR BRENDA; 3.1.8.1; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004063; F:aryldialkylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.120.10.30; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR008364; Paraoxonase2.
DR Pfam; PF01731; Arylesterase; 1.
DR PRINTS; PR01785; PARAOXONASE.
DR PRINTS; PR01787; PARAOXONASE2.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Hydrolase; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
KW Signal.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10931838"
FT CHAIN 2..354
FT /note="Serum paraoxonase/lactonase 3"
FT /id="PRO_0000223293"
FT SIGNAL 2..?
FT /note="Not cleaved"
FT /evidence="ECO:0000255"
FT ACT_SITE 114
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
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"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
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"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15166"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..352
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 39507 MW; DE782A7F2DA16603 CRC64;
MAKLLLLTLL GASLAFVGER LLAFRNSFGA VQELEPVEPQ NCVLIEGLEN GSEDIDILPS
GLAFISSGLK YPGMPNFAPD EPGKIFLIDM NEKNPRAQEL EISNGFEKES FNPHGISTFI
DKDHTVYLYV VNHPHMKSTV EIFKFEEQQR SLVHLKTIKH ELLKSVNNIV VLGPEQFYAT
RDHYFTNYVL ALLEMFLDLH WTSVLFYSPK EVKVVAKGFS SANGITVSLD KKYVYVADAT
AKNVHVMEKH DNWDLTELKV IHLDTLVDNL SVDPATGDIL AGCHPNGMKL LNYNPEDPPG
SEVLRIQNVL SEKPRVSTVY TNDGSVLQGS TVASVYQGKI LIGTIFHKTL YCVL
