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Database: UniProt
Entry: G5AJS7_HETGA
LinkDB: G5AJS7_HETGA
Original site: G5AJS7_HETGA 
ID   G5AJS7_HETGA            Unreviewed;       354 AA.
AC   G5AJS7;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE            EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
GN   Name=PON2 {ECO:0000313|EMBL:JAO02735.1};
GN   ORFNames=GW7_01714 {ECO:0000313|EMBL:EHA97286.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA97286.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHA97286.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
RN   [2] {ECO:0000313|EMBL:JAO02735.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Skin {ECO:0000313|EMBL:JAO02735.1};
RA   Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA   Platzer M., Szafranski K.;
RT   "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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   EMBL; JH165528; EHA97286.1; -; Genomic_DNA.
DR   EMBL; GEBF01000898; JAO02735.1; -; Transcribed_RNA.
DR   RefSeq; XP_004862770.1; XM_004862713.1.
DR   AlphaFoldDB; G5AJS7; -.
DR   STRING; 10181.G5AJS7; -.
DR   Ensembl; ENSHGLT00000084368; ENSHGLP00000052171; ENSHGLG00000044448.
DR   Ensembl; ENSHGLT00100044288; ENSHGLP00100057855; ENSHGLG00100037534.
DR   GeneID; 101697694; -.
DR   KEGG; hgl:101697694; -.
DR   CTD; 5445; -.
DR   eggNOG; ENOG502QUCT; Eukaryota.
DR   InParanoid; G5AJS7; -.
DR   OMA; RIQNVHS; -.
DR   OrthoDB; 2874974at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000000791; Expressed in pituitary gland and 10 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019439; P:aromatic compound catabolic process; 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; 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}; Hydrolase {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:UP000006813}.
FT   ACT_SITE        114
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         116
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         167
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         223
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         268
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   CARBOHYD        269
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-4"
FT   DISULFID        42..352
FT                   /note="In form B"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-3"
SQ   SEQUENCE   354 AA;  39453 MW;  D484F26810FD50D2 CRC64;
     MGRLVTLGLL GIAVALLGER LLALRNRLKA SREIESIDLP NCHLIKGIEA GSEDIDILPN
     GLAFFSVGLQ FPGLHSFAPD KPGGILMMDL NEDKPRALEL RISRGFDLAS FNPHGISTFI
     DNDDTVYLFV VNHPEFKNTI EIFKFEEEEN SLLHLKTIKH ELLPSTNDII AIGPMHFYAT
     NDHYFSDPFL KYLETYLNLH WANVVYYSPN EVKVVAEGFD SANGINISPD KKYIYVADLL
     AHEIHVLKKQ PDMNLTQAKV LSLDTLVDNL SIEPFSGDIW AGCHPNGQKL FVYDPSNPPS
     SEVLRIQNIL SEKPTVTTVY ANNGSVLQGS SVASVYNGKL LIGTLYHRAL YCEL
//
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