ID A0A2K6P7L3_RHIRO Unreviewed; 355 AA.
AC A0A2K6P7L3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
GN Name=PON1 {ECO:0000313|Ensembl:ENSRROP00000012526.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000012526.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000012526.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000368,
CC ECO:0000256|RuleBase:RU368025};
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:0000256|ARBA:ARBA00000450};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR602640-2,
CC ECO:0000256|RuleBase:RU368025};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC 2, ECO:0000256|RuleBase:RU368025};
CC -!- PTM: Glycosylated. {ECO:0000256|PIRSR:PIRSR602640-4}.
CC -!- SIMILARITY: Belongs to the paraoxonase family.
CC {ECO:0000256|ARBA:ARBA00008595, ECO:0000256|RuleBase:RU368025}.
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DR RefSeq; XP_010354562.1; XM_010356260.1.
DR AlphaFoldDB; A0A2K6P7L3; -.
DR STRING; 61622.ENSRROP00000012526; -.
DR Ensembl; ENSRROT00000036647.1; ENSRROP00000012526.1; ENSRROG00000030569.1.
DR GeneID; 104656585; -.
DR KEGG; rro:104656585; -.
DR CTD; 5444; -.
DR GeneTree; ENSGT00390000008932; -.
DR OMA; NAMYLLV; -.
DR OrthoDB; 2874974at2759; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0034366; C:spherical high-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004063; F:aryldialkylphosphatase activity; IEA:Ensembl.
DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:Ensembl.
DR GO; GO:0046395; P:carboxylic acid catabolic process; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:Ensembl.
DR GO; GO:0046434; P:organophosphate catabolic process; IEA:Ensembl.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:Ensembl.
DR GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR002640; Arylesterase.
DR InterPro; IPR008363; Paraoxonase1.
DR PANTHER; PTHR11799; PARAOXONASE; 1.
DR PANTHER; PTHR11799:SF16; SERUM PARAOXONASE_ARYLESTERASE 1; 1.
DR Pfam; PF01731; Arylesterase; 1.
DR PRINTS; PR01785; PARAOXONASE.
DR PRINTS; PR01786; PARAOXONASE1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR602640-2, ECO:0000256|RuleBase:RU368025};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR602640-3,
KW ECO:0000256|RuleBase:RU368025};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180, ECO:0000256|PIRSR:PIRSR602640-
KW 4};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368025};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2,
KW ECO:0000256|RuleBase:RU368025};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..355
FT /note="Paraoxonase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014333807"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT BINDING 270
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT DISULFID 42..353
FT /note="In form B"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-3"
SQ SEQUENCE 355 AA; 39790 MW; D98B9BAA6ABEF786 CRC64;
MAKLIALTLL GMGLALFKNH RFSYQTRLNA LREVQPIELP NCNLVKGIET GSEDLEILPN
GLAFISSGLK YPGIKSFDPN NPGKILLMDL NEEDQTVLEL GITGSKFDLS SFNPHGISTF
TDEDNAVYLL VVNHPDAKST VELFKFQEEE KSLLHLKTIR HKLLPNVNDI VAVGPEHFYA
TNDHYFLDPY LKSWEMYLGL AWSYVVYYSP SEVRVVAEGF DFANGINISP DGKYVYVAEL
LAHKIHVYEK HANWTLTPLK SLDFNTLVDN ISVDPETGDL WVGCHPNGMK VFFYDSENPP
ASEVLQIQNI LTEEPKVTQV YAENGTVLQG STVASVYKGK LLIGTVFHKA LYCEL
//
