ID W5M1R6_LEPOC Unreviewed; 406 AA.
AC W5M1R6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Neutral cholesterol ester hydrolase 1 {ECO:0000256|ARBA:ARBA00044162};
DE EC=3.1.1.71 {ECO:0000256|ARBA:ARBA00044060};
DE AltName: Full=Acetylalkylglycerol acetylhydrolase {ECO:0000256|ARBA:ARBA00044219};
DE AltName: Full=Arylacetamide deacetylase-like 1 {ECO:0000256|ARBA:ARBA00044256};
GN Name=AADAC {ECO:0000313|Ensembl:ENSLOCP00000002324.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002324.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002324.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycerol + H2O = 1-O-hexadecyl-sn-
CC glycerol + acetate + H(+); Xref=Rhea:RHEA:38563, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:34115,
CC ChEBI:CHEBI:75936; Evidence={ECO:0000256|ARBA:ARBA00023406};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564;
CC Evidence={ECO:0000256|ARBA:ARBA00023406};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycerol + H2O = 1-O-alkyl-sn-glycerol
CC + acetate + H(+); Xref=Rhea:RHEA:11552, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15850, ChEBI:CHEBI:16291,
CC ChEBI:CHEBI:30089; EC=3.1.1.71;
CC Evidence={ECO:0000256|ARBA:ARBA00043796};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11553;
CC Evidence={ECO:0000256|ARBA:ARBA00043796};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a cholesterol ester + H2O = a fatty acid + cholesterol + H(+);
CC Xref=Rhea:RHEA:36403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16113, ChEBI:CHEBI:17002, ChEBI:CHEBI:28868;
CC Evidence={ECO:0000256|ARBA:ARBA00043699};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36404;
CC Evidence={ECO:0000256|ARBA:ARBA00043699};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000256|ARBA:ARBA00023350};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000256|ARBA:ARBA00023350};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC protein {ECO:0000256|ARBA:ARBA00004606}. Microsome
CC {ECO:0000256|ARBA:ARBA00004144}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000256|ARBA:ARBA00010515}.
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DR EMBL; AHAT01022483; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M1R6; -.
DR STRING; 7918.ENSLOCP00000002324; -.
DR ESTHER; lepoc-w5m1r6; Arylacetamide_deacetylase.
DR Ensembl; ENSLOCT00000002329.1; ENSLOCP00000002324.1; ENSLOCG00000002005.1.
DR eggNOG; KOG1515; Eukaryota.
DR GeneTree; ENSGT00940000155975; -.
DR HOGENOM; CLU_012494_12_0_1; -.
DR InParanoid; W5M1R6; -.
DR OMA; QNQYMPI; -.
DR Proteomes; UP000018468; Linkage group LG14.
DR Bgee; ENSLOCG00000002005; Expressed in intestine and 9 other cell types or tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR017157; Arylacetamide_deacetylase.
DR InterPro; IPR033140; Lipase_GDXG_put_SER_AS.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF33; SIMILAR TO HYPOTHETICAL PROTEIN C130079G13; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Microsome {ECO:0000256|ARBA:ARBA00022848};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 113..273
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 314..379
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 195
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1,
FT ECO:0000256|PROSITE-ProRule:PRU10038"
FT ACT_SITE 346
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT ACT_SITE 376
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
SQ SEQUENCE 406 AA; 45873 MW; 1AD5747FC625B234 CRC64;
IFECRMGSKG IILLLIGSLT AYYIYSPIPD EIEDKWKLMI TDSFFRSLSH LADALELVGL
KDYMDVMMLI TLAERVTPAA DRDTTVAEAL FDGVEVLVYE PRRESAGAPR RAVIYLHGGG
WCLGSARMAP YDLLSRRIAS ELNAVVVSVE YRLAPAHHFP VPFEDVYRAV KYFLTEDTVS
RYSVDINRIA VSGDSAGGNL AAAVAQQLQL DKDVQAELKA QALLYPVLQA LDLNTPSYQQ
NEHMPILPKT LMVRFWSEYF TSDKSLFRSM MANSHNSLES SHLLRCVNWS ALLPEPFRRK
YNYTALSADP SRSMAALADP RASPLLAADA QLRALPRAYI LTCEYDVLRD DGIMYATRLR
DAGVQVRHEH YKGGFHGAMM FSVWPTDFKI AHRMLNNYIR WLDENL
//
