PON2_RAT
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 03-AUG-2022, entry version 111.
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}.
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DR EMBL; BC079462; AAH79462.1; -; mRNA.
DR RefSeq; NP_001013100.1; NM_001013082.1.
DR AlphaFoldDB; Q6AXM8; -.
DR SMR; Q6AXM8; -.
DR STRING; 10116.ENSRNOP00000033943; -.
DR GlyGen; Q6AXM8; 3 sites.
DR jPOST; Q6AXM8; -.
DR PaxDb; Q6AXM8; -.
DR PRIDE; Q6AXM8; -.
DR GeneID; 296851; -.
DR KEGG; rno:296851; -.
DR UCSC; RGD:1309954; rat.
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 OMA; WSLTHVK; -.
DR OrthoDB; 888266at2759; -.
DR PhylomeDB; Q6AXM8; -.
DR TreeFam; TF322436; -.
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 tissues.
DR Genevisible; Q6AXM8; RN.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019439; P:aromatic compound 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 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; 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
