ID G3PA32_GASAC Unreviewed; 440 AA.
AC G3PA32;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
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};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000014456.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000014456.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000014456.1}
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 AlphaFoldDB; G3PA32; -.
DR STRING; 69293.ENSGACP00000014456; -.
DR ESTHER; gasac-g3pa32; Arylacetamide_deacetylase.
DR Ensembl; ENSGACT00000014482.1; ENSGACP00000014456.1; ENSGACG00000010923.1.
DR eggNOG; KOG1515; Eukaryota.
DR GeneTree; ENSGT00940000156699; -.
DR InParanoid; G3PA32; -.
DR OMA; KCPRAYV; -.
DR TreeFam; TF314978; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000010923; Expressed in muscle tissue and 8 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:UP000007635};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 24..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 140..292
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 331..413
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 222
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1,
FT ECO:0000256|PROSITE-ProRule:PRU10038"
FT ACT_SITE 380
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
SQ SEQUENCE 440 AA; 48506 MW; 0F40D45BB025238D CRC64;
GAARRARAIA VRSPRQSERH EMRLLPAAVT LSLAVALAYY VYVPMPDAIQ EPWKLMLMDA
GFRATMQLAS VKAWLGIDHY IGSIRRSTAG FEGMMEGLLG PEQGGGVMPG VKVSDITFAG
VPVRVYEPPA GGEGHLRRGL MFIHGGGWAL GTGKRGSYDT IGRMLSDELN TVVVSVEYRL
YPEVHFPVPY LDCLAAAKHF LSPEVRARYA IDPERVAVSG DSAGGNLAAA VAQEISTDET
MSAKFSVQAL IYPVLQALDF NTPSYLQNQN IPILHRPLMV HFWLQYLGAD LSLLSQALAN
NHSALENSNI TPELRARLDW TALLPPKHKR DHKPLIPKKG FQGTWKEVPG LLDVRASPLL
AGPEVLAKCP RAYVLTCEHD VLRDEGLMYA RRLQDAGVSV TSDHYEDGFH GCLSFITWPL
EFDVGKRALR GYLDWLQDNL
//
