PON3_MOUSE
ID PON3_MOUSE Reviewed; 354 AA.
AC Q62087; Q4FZK0; Q8C2I7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8661009; DOI=10.1006/geno.1996.0225;
RA Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N.;
RT "The human serum paraoxonase/arylesterase gene (PON1) is one member of a
RT multigene family.";
RL Genomics 33:498-507(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thyroid;
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).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=15963993; DOI=10.1016/j.febslet.2005.05.060;
RA Yang F., Wang L.H., Wang J., Dong Y.H., Hu J.Y., Zhang L.H.;
RT "Quorum quenching enzyme activity is widely conserved in the sera of
RT mammalian species.";
RL FEBS Lett. 579:3713-3717(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 Evidence={ECO:0000269|PubMed:15963993};
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:15963993};
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:15963993};
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; L76193; AAC42090.1; -; mRNA.
DR EMBL; AK088572; BAC40430.1; -; mRNA.
DR EMBL; CH466533; EDL13970.1; -; Genomic_DNA.
DR EMBL; BC099416; AAH99416.1; -; mRNA.
DR CCDS; CCDS19899.1; -.
DR RefSeq; NP_766594.1; NM_173006.1.
DR AlphaFoldDB; Q62087; -.
DR SMR; Q62087; -.
DR BioGRID; 234716; 2.
DR STRING; 10090.ENSMUSP00000031773; -.
DR GlyGen; Q62087; 3 sites.
DR iPTMnet; Q62087; -.
DR PhosphoSitePlus; Q62087; -.
DR CPTAC; non-CPTAC-3939; -.
DR EPD; Q62087; -.
DR jPOST; Q62087; -.
DR MaxQB; Q62087; -.
DR PaxDb; Q62087; -.
DR PeptideAtlas; Q62087; -.
DR PRIDE; Q62087; -.
DR ProteomicsDB; 289718; -.
DR Antibodypedia; 15863; 302 antibodies from 30 providers.
DR DNASU; 269823; -.
DR Ensembl; ENSMUST00000031773; ENSMUSP00000031773; ENSMUSG00000029759.
DR GeneID; 269823; -.
DR KEGG; mmu:269823; -.
DR UCSC; uc009awe.1; mouse.
DR CTD; 5446; -.
DR MGI; MGI:106686; Pon3.
DR VEuPathDB; HostDB:ENSMUSG00000029759; -.
DR eggNOG; ENOG502S6UP; Eukaryota.
DR GeneTree; ENSGT00390000008932; -.
DR HOGENOM; CLU_049839_0_1_1; -.
DR InParanoid; Q62087; -.
DR OMA; TFIDKDH; -.
DR OrthoDB; 888266at2759; -.
DR PhylomeDB; Q62087; -.
DR TreeFam; TF322436; -.
DR BRENDA; 3.1.1.2; 3474.
DR BRENDA; 3.1.8.1; 3474.
DR Reactome; R-MMU-2142688; Synthesis of 5-eicosatetraenoic acids.
DR Reactome; R-MMU-9754706; Atorvastatin ADME.
DR BioGRID-ORCS; 269823; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q62087; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62087; protein.
DR Bgee; ENSMUSG00000029759; Expressed in parotid gland and 160 other tissues.
DR ExpressionAtlas; Q62087; baseline and differential.
DR Genevisible; Q62087; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0018733; F:3,4-dihydrocoumarin hydrolase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019439; P:aromatic compound catabolic process; ISO:MGI.
DR GO; GO:0046395; P:carboxylic acid catabolic process; ISO:MGI.
DR GO; GO:0046226; P:coumarin catabolic process; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IDA:MGI.
DR GO; GO:0032929; P:negative regulation of superoxide anion generation; IDA:CACAO.
DR GO; GO:0010124; P:phenylacetate catabolic process; ISO:MGI.
DR GO; GO:0003096; P:renal sodium ion transport; IDA:MGI.
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 1: Evidence at protein 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_0000223291"
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"
FT CONFLICT 3
FT /note="K -> H (in Ref. 1; AAC42090)"
FT /evidence="ECO:0000305"
FT CONFLICT 8
FT /note="T -> P (in Ref. 1; AAC42090)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="K -> E (in Ref. 1; AAC42090)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="D -> A (in Ref. 1; AAC42090)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="D -> G (in Ref. 1; AAC42090)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39351 MW; D66534EAA4EB10F2 CRC64;
MGKLVALTLL GACLALIGER LLNFRERVST TREIKATEPQ NCHLIEGLEN GSEDIDILPS
GLAFISTGLK YPGMPAFAPD KPGRIFLMDL NEQNPEAQAL EISGGLDQES LNPHGISTFI
DKDNTAYLYV VNHPNMDSTV EIFKFEEQQR SLIHLKTLKH ELLKSVNDIV VLGPEQFYAT
RDHYFTSYFL VLLEMILDPH WTSVVFYSPK EVKVVAQGFS SANGITVSLD QKFVYVADVT
AKNIHIMKKH DNWDLTPVKV IQLGTLVDNL TVDPATGDIL AGCHPNPMKL LIYNPEDPPG
SEVLRIQDSL SDKPRVSTLY ANNGSVLQGS TVASVYHKRM LIGTIFHKAL YCDL
