PON2_CHICK
ID PON2_CHICK Reviewed; 354 AA.
AC Q90952;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Serum paraoxonase/arylesterase 2;
DE Short=PON 2;
DE EC=3.1.1.2;
DE EC=3.1.8.1;
DE AltName: Full=Aromatic esterase 2;
DE Short=A-esterase 2;
DE AltName: Full=Serum aryldialkylphosphatase 2;
GN Name=PON2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC 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).
CC -!- FUNCTION: The absence of paraoxonase activity in turkey and chicken
CC blood and in turkey liver indicates that PON2, if expressed, does not
CC hydrolyze paraoxon.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 2 calcium ions per subunit. {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; L47573; AAC42234.1; -; mRNA.
DR AlphaFoldDB; Q90952; -.
DR SMR; Q90952; -.
DR STRING; 9031.ENSGALP00000037229; -.
DR PaxDb; Q90952; -.
DR VEuPathDB; HostDB:geneid_395830; -.
DR eggNOG; ENOG502QUCT; Eukaryota.
DR InParanoid; Q90952; -.
DR PhylomeDB; Q90952; -.
DR PRO; PR:Q90952; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004063; F:aryldialkylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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_0000223294"
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 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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; 39409 MW; 30C3191289BC13EB CRC64;
MGKVLAAALV GIAAALAAER LLAFRNRLNA TREVDPVALP NCYLIKGIET GSEDIDILPN
GLAFISSGLK YPGLKSFAPD KPGEIFLMDL NEKKPKASEL RISRGFDVGS FNPHGISTYI
DKDDTVYLFV VNHPHQKSTV ELFKFMEDDN SLVHLKTIRH DLLTSVNDVV AVGPDSFYAT
NDHYFYDFIL MFLEMYLGLT WSNVVYYSPK EVKEVAAGFY SANGINISPD KKYIYIADIL
DHNVHVMEKH ADWNLTHVKT LQLDTLADNL SVDPDTGDIW TGCHPNGMKL FYDDPDNPPA
SEVLRIQNIL AEQPTVTRVY AENGSVLQGT SVATVYDGKL LIGTVFHRAL YCEL
