PON3_RAT
ID PON3_RAT Reviewed; 354 AA.
AC Q68FP2;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Has low activity towards the organophosphate paraxon and
CC aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as
CC statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and
CC 5- or 6-member ring lactones with aliphatic substituents but not simple
CC lactones or those with polar substituents (By similarity).
CC {ECO:0000250}.
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; BC079466; AAH79466.1; -; mRNA.
DR RefSeq; NP_001004086.1; NM_001004086.1.
DR AlphaFoldDB; Q68FP2; -.
DR SMR; Q68FP2; -.
DR STRING; 10116.ENSRNOP00000012050; -.
DR GlyGen; Q68FP2; 3 sites.
DR PaxDb; Q68FP2; -.
DR PRIDE; Q68FP2; -.
DR GeneID; 312086; -.
DR KEGG; rno:312086; -.
DR UCSC; RGD:1302965; rat.
DR CTD; 5446; -.
DR RGD; 1302965; Pon3.
DR VEuPathDB; HostDB:ENSRNOG00000009096; -.
DR eggNOG; ENOG502S6UP; Eukaryota.
DR HOGENOM; CLU_049839_0_1_1; -.
DR InParanoid; Q68FP2; -.
DR OMA; TFIDKDH; -.
DR OrthoDB; 888266at2759; -.
DR PhylomeDB; Q68FP2; -.
DR TreeFam; TF322436; -.
DR BRENDA; 3.1.1.2; 5301.
DR BRENDA; 3.1.1.25; 5301.
DR BRENDA; 3.1.8.1; 5301.
DR Reactome; R-RNO-2142688; Synthesis of 5-eicosatetraenoic acids.
DR Reactome; R-RNO-9754706; Atorvastatin ADME.
DR PRO; PR:Q68FP2; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000009096; Expressed in lung and 19 other tissues.
DR Genevisible; Q68FP2; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0018733; F:3,4-dihydrocoumarin hydrolase activity; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019439; P:aromatic compound catabolic process; ISO:RGD.
DR GO; GO:0046395; P:carboxylic acid catabolic process; ISO:RGD.
DR GO; GO:0046226; P:coumarin catabolic process; IDA:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; ISO:RGD.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; ISO:RGD.
DR GO; GO:0010124; P:phenylacetate catabolic process; IDA:RGD.
DR GO; GO:0003096; P:renal sodium ion transport; ISO:RGD.
DR GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT CHAIN 1..354
FT /note="Serum paraoxonase/lactonase 3"
FT /id="PRO_0000223292"
FT SIGNAL 1..?
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 /evidence="ECO:0000250"
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 CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..352
FT /evidence="ECO:0000250"
SQ SEQUENCE 354 AA; 39458 MW; 913C28243E4B0D7F CRC64;
MGKLVALTVL GASLALLGER LLNFRERVST SREIKPTEPQ NCHLIEGLEN GSEDIDILPS
GLAFISTGLK YPGMPSFAPD KPGRIFLMDL NEPYPKAQAL EISDGFDQDS LNPHGISTFI
DKDNTVYLYA VNHPHMDSTV EIFKFEEQPR SLVHLKTIKH ELFESVNDIV VLGPEQFYAT
RDHYFTSHFL VLLEMILDPH WTSVLFYSPK EVKVVAQGFS SANGITVSLD QKYVYVADVT
AKNIHIMKKH NNWDLTPVKV IQLGTLVDNL TVDPATGDIL AGCHPNPMKL LIYNPEDPPG
SEVLRIQDPL SDNPRVSTLY SNNGSVLQGS TVASVYHKKM LIGTIFHKAL YCEL
