ID A0A455BAW6_PHYMC Unreviewed; 377 AA.
AC A0A455BAW6;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
GN Name=PON2 {ECO:0000313|RefSeq:XP_028345829.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028345829.1};
RN [1] {ECO:0000313|RefSeq:XP_028345829.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028345829.1};
RG RefSeq;
RL Submitted (NOV-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 -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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_028345829.1; XM_028490028.1.
DR AlphaFoldDB; A0A455BAW6; -.
DR InParanoid; A0A455BAW6; -.
DR OrthoDB; 2874974at2759; -.
DR Proteomes; UP000248484; Chromosome 5.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0102007; F:acyl-L-homoserine-lactone lactonohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2,
KW ECO:0000256|RuleBase:RU368025};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484}.
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT BINDING 76
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 77
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 139
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 190
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 191
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 246
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 291
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 292
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 292
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT CARBOHYD 346
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT DISULFID 65..375
FT /note="In form B"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-3"
SQ SEQUENCE 377 AA; 42662 MW; A7117D3D8387A0EF CRC64;
MLSTFSVRCA LLASCNRLQL QLLIKRCQEE EQCLCNRKHQ SWRRNIYWNR LKASREVESV
DLPNCHLIKG IEAGSEDIDI LPNGLAFFSV GLKCPGLHSF APDKPGGILM MDLKEENPRA
LELRISRGFN LASFNPHGIS TFIDSDNTVY LFVVNHPEFK NTVEIFKFEE EENSLLHLKT
IKHELLPSVN DIIAVGPAHF YATNDHYFSD PFLKYLETYL NLHWTNVIYY SPNEVKVVAE
GFDSANGINI SPDKKYIYVA DMLAHEIHVL EKHPNMNLTQ LKVLKLDTLV DNLSIDPSSG
DILVGCHPNG QKLFVYDPNN PPSSEVLRIQ NILSETPTVT TVYANNGSVL QGSSVASVYD
RKLLIGTLYH RALYCQL
//
