ID   PON2_RAT                Reviewed;         354 AA.
AC   Q6AXM8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   02-SEP-2026, entry version 127.
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   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: 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   -!- 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: 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC079462; AAH79462.1; -; mRNA.
DR   RefSeq; NP_001013100.1; NM_001013082.1.
DR   AlphaFoldDB; Q6AXM8; -.
DR   SMR; Q6AXM8; -.
DR   FunCoup; Q6AXM8; 436.
DR   STRING; 10116.ENSRNOP00000033943; -.
DR   GlyCosmos; Q6AXM8; 3 sites, No reported glycans.
DR   GlyGen; Q6AXM8; 4 sites.
DR   PhosphoSitePlus; Q6AXM8; -.
DR   PaxDb; 10116-ENSRNOP00000033943; -.
DR   GeneID; 296851; -.
DR   KEGG; rno:296851; -.
DR   UCSC; RGD:1309954; rat.
DR   AGR; RGD:1309954; -.
DR   CTD; 5445; -.
DR   RGD; 1309954; Pon2.
DR   VEuPathDB; HostDB:ENSRNOG00000009112; -.
DR   eggNOG; ENOG502QUCT; Eukaryota.
DR   HOGENOM; CLU_049839_0_1_1; -.
DR   InParanoid; Q6AXM8; -.
DR   OrthoDB; 31337at9989; -.
DR   PhylomeDB; Q6AXM8; -.
DR   Reactome; R-RNO-2142688; Synthesis of 5-eicosatetraenoic acids.
DR   PRO; PR:Q6AXM8; -.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000009112; Expressed in lung and 20 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; ISO:RGD.
DR   GO; GO:0004064; F:arylesterase activity; IBA:GO_Central.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0046395; P:carboxylic acid catabolic process; IBA:GO_Central.
DR   GO; GO:1901335; P:lactone catabolic process; ISO:RGD.
DR   GO; GO:0006979; P:response to oxidative stress; IEP:RGD.
DR   GO; GO:0009636; P:response to toxic substance; IBA:GO_Central.
DR   FunFam; 2.120.10.30:FF:000023; Serum paraoxonase/arylesterase 2; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase-like.
DR   InterPro; IPR008364; Paraoxonase2.
DR   PANTHER; PTHR11799; PARAOXONASE; 1.
DR   PANTHER; PTHR11799:SF17; SERUM PARAOXONASE_ARYLESTERASE 2; 1.
DR   Pfam; PF01731; Arylesterase; 1.
DR   PRINTS; PR01785; PARAOXONASE.
DR   PRINTS; PR01787; PARAOXONASE2.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   2: Evidence at transcript 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_0000223289"
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"
SQ   SEQUENCE   354 AA;  39617 MW;  69D77678C781859D CRC64;
     MGRLVALSLL GIGLALLGER FLALRSRLKA SREVESVDLP NCRLIKGIET GAEDIDILPN
     GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KEEKPRALEL RVSWGFDLAS FNPHGISTFI
     DDDDTVYLFV VNHPEFKNTV EIFKFQEEEN SLLHLKTIKH ELLPSVNDVI AVGPSHFYAT
     NDHYFSDPFL KYLETYLNLR WANVVYYSPE EVKLVAEGFD SANGINISPD KKYVYVADIL
     AHEIHVLEKQ PNMNLTQLKV LQLGTLVDNL SIDPSSGDIW VGCHPNGQKL FVYDPNHPPS
     SEVLRIQNIL SEKPSVTTVY INNGSVLQGS SVATIYDRKL LVGTLYQRAL YCEL
//