PON2_MOUSE
ID PON2_MOUSE Reviewed; 354 AA.
AC Q62086; Q3TAD3; Q8CFK3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Serum paraoxonase/arylesterase 2;
DE Short=PON 2;
DE EC=3.1.1.2;
DE EC=3.1.1.81;
DE AltName: Full=Aromatic esterase 2;
DE Short=A-esterase 2;
DE AltName: Full=Serum aryldialkylphosphatase 2;
GN Name=Pon2;
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=BALB/cJ, and NOD; TISSUE=Spleen;
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 STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
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=Brain, Heart, Liver, Lung, Pancreas, and Spleen;
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: Capable of hydrolyzing lactones and a number of aromatic
CC carboxylic acid esters. {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 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: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Peripheral membrane
CC protein {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; L48514; AAC42089.1; -; mRNA.
DR EMBL; AK146311; BAE27066.1; -; mRNA.
DR EMBL; AK171926; BAE42735.1; -; mRNA.
DR EMBL; CH466533; EDL13967.1; -; Genomic_DNA.
DR EMBL; BC037140; AAH37140.1; -; mRNA.
DR EMBL; BC055896; AAH55896.1; -; mRNA.
DR EMBL; BC062200; AAH62200.1; -; mRNA.
DR CCDS; CCDS19900.1; -.
DR RefSeq; NP_899131.1; NM_183308.2.
DR AlphaFoldDB; Q62086; -.
DR SMR; Q62086; -.
DR BioGRID; 236929; 1.
DR STRING; 10090.ENSMUSP00000062670; -.
DR GlyConnect; 2706; 6 N-Linked glycans (2 sites).
DR GlyGen; Q62086; 3 sites, 6 N-linked glycans (2 sites).
DR PhosphoSitePlus; Q62086; -.
DR EPD; Q62086; -.
DR jPOST; Q62086; -.
DR MaxQB; Q62086; -.
DR PaxDb; Q62086; -.
DR PeptideAtlas; Q62086; -.
DR PRIDE; Q62086; -.
DR ProteomicsDB; 291638; -.
DR Antibodypedia; 30147; 424 antibodies from 39 providers.
DR DNASU; 330260; -.
DR Ensembl; ENSMUST00000057792; ENSMUSP00000062670; ENSMUSG00000032667.
DR GeneID; 330260; -.
DR KEGG; mmu:330260; -.
DR UCSC; uc009awf.1; mouse.
DR CTD; 5445; -.
DR MGI; MGI:106687; Pon2.
DR VEuPathDB; HostDB:ENSMUSG00000032667; -.
DR eggNOG; ENOG502QUCT; Eukaryota.
DR GeneTree; ENSGT00390000008932; -.
DR HOGENOM; CLU_049839_0_1_1; -.
DR InParanoid; Q62086; -.
DR OMA; WSLTHVK; -.
DR OrthoDB; 888266at2759; -.
DR PhylomeDB; Q62086; -.
DR TreeFam; TF322436; -.
DR BRENDA; 3.1.8.1; 3474.
DR Reactome; R-MMU-2142688; Synthesis of 5-eicosatetraenoic acids.
DR BioGRID-ORCS; 330260; 1 hit in 77 CRISPR screens.
DR ChiTaRS; Pon2; mouse.
DR PRO; PR:Q62086; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q62086; protein.
DR Bgee; ENSMUSG00000032667; Expressed in epithelium of stomach and 255 other tissues.
DR Genevisible; Q62086; MM.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004064; F:arylesterase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound catabolic process; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
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; Membrane; Metal-binding;
KW Reference proteome; Signal.
FT CHAIN 1..354
FT /note="Serum paraoxonase/arylesterase 2"
FT /id="PRO_0000223288"
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 CARBOHYD 254
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 8..14
FT /note="SLLGIGL -> GFAGHRV (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="R -> S (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="A -> G (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..98
FT /note="KDERPRAL -> DERPPSLE (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..138
FT /note="KS -> SN (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="E -> A (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="T -> A (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="A -> T (in Ref. 1; AAC42089)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 39617 MW; D16C3F3C9D853CD2 CRC64;
MGRMVALSLL GIGLALLGER FLALRSRLKA SREVESVDLP NCHLIKGIET GAEDIDILPN
GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KDERPRALEL RVSWGFDLAS FNPHGISTFI
DDDDTVYLFV VNHPQFKSTV EIFKFQEEEN SLLHLKTIKH ELLPSVNDII AVGPTHFYAT
NDHYFSDPFL KYLETYLNLH WANVVYYSPE EVKLVAEGFD SANGINISPD KKYVYVADIL
AHEIHVLEKQ PNMNLTQLKV LQLGTLVDNL SIDPSSGDIW VGCHPNGQRL FVYHPNHPPA
SEVLRIQNIL SEKPSVTTVY INNGSVLQGS SVATIYDRKL LVGTLYQKAL YCEL
