ID F7BEV5_CALJA Unreviewed; 399 AA.
AC F7BEV5;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 67.
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|EMBL:JAB03708.1,
GN ECO:0000313|Ensembl:ENSCJAP00000001864.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000001864.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000001864.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB03708.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB03708.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000001864.1}
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; GAMT01008153; JAB03708.1; -; mRNA.
DR RefSeq; XP_002759529.1; XM_002759483.4.
DR STRING; 9483.ENSCJAP00000001864; -.
DR ESTHER; calja-f7bev5; Arylacetamide_deacetylase.
DR MEROPS; S09.991; -.
DR Ensembl; ENSCJAT00000001977.4; ENSCJAP00000001864.1; ENSCJAG00000001084.4.
DR GeneID; 100393374; -.
DR KEGG; cjc:100393374; -.
DR eggNOG; KOG1515; Eukaryota.
DR GeneTree; ENSGT00940000155975; -.
DR HOGENOM; CLU_012494_12_0_1; -.
DR OMA; QNQYMPI; -.
DR OrthoDB; 1144477at2759; -.
DR TreeFam; TF314978; -.
DR Proteomes; UP000008225; Chromosome 17.
DR Bgee; ENSCJAG00000001084; Expressed in liver and 1 other cell type or tissue.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:InterPro.
DR GO; GO:0019213; F:deacetylase activity; IEA:Ensembl.
DR GO; GO:0017171; F:serine hydrolase activity; IEA:Ensembl.
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 2: Evidence at transcript level;
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:UP000008225};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 107..266
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 315..376
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT ACT_SITE 189
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1,
FT ECO:0000256|PROSITE-ProRule:PRU10038"
FT ACT_SITE 343
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
FT ACT_SITE 373
FT /evidence="ECO:0000256|PIRSR:PIRSR037251-1"
SQ SEQUENCE 399 AA; 45984 MW; 3EAE8D3D8AEA4819 CRC64;
MGRKSLYLLI VGIFVAYYIY IPLPDNIEEP WRIMWFNTQF TTAEKLAAFV ELLGLHHIMD
CLKFSLSIYE VPPTSDENVT VTETKFNNIL VRVYVPKRKS EALRRGLFYI HGGGWGLGSA
ALHDYDLLSR WTADRLDAVV ISTNYRLAPK YHFPIQFEDV YNSLRWFLRK NVLAKYGVNP
ERIGISGDSA GGNLAAAVTQ QLLDDPDVKI KFKIQALIYP ALQPLDVDSP SYQENSHFPF
LHKSLMVRFW SEYFTTDRSL EKAMLSRQHV PVESSHLFKF VNWSSLLPER FIKGYIYSNP
NYGSSELAKK YPGFLDVRAA PLLADDNKLH GLPLTYVVTC QYDVLRDDGL MYVTRLRNAG
VQVTHNHIED GFHGAFSFLE LKISHRLINQ YIEWLKENL
//
