NCEH1_PONAB
ID NCEH1_PONAB Reviewed; 408 AA.
AC Q5R8Y5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Neutral cholesterol ester hydrolase 1;
DE Short=NCEH;
DE EC=3.1.1.- {ECO:0000250|UniProtKB:Q8BLF1};
DE AltName: Full=Acetylalkylglycerol acetylhydrolase {ECO:0000250|UniProtKB:Q8BLF1};
DE Short=2-acetyl MAGE hydrolase {ECO:0000250|UniProtKB:Q6PIU2};
DE EC=3.1.1.71 {ECO:0000250|UniProtKB:Q8BLF1};
DE AltName: Full=Arylacetamide deacetylase-like 1;
GN Name=NCEH1; Synonyms=AADACL1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes 2-acetyl monoalkylglycerol ether (1-O-alkyl-2-
CC acetyl-sn-glycerol), the penultimate precursor of the pathway for de
CC novo synthesis of platelet-activating factor (By similarity). May be
CC responsible for the hydrolysis of cholesterol esters (such as
CC cholesteryl (9Z-octadecenoate)) in macrophages (By similarity). Also
CC involved in organ detoxification by hydrolyzing exogenous
CC organophosphorus compounds (By similarity).
CC {ECO:0000250|UniProtKB:Q8BLF1}.
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:0000250|UniProtKB:Q6PIU2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11553;
CC Evidence={ECO:0000250|UniProtKB:Q6PIU2};
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:0000250|UniProtKB:Q8BLF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38564;
CC Evidence={ECO:0000250|UniProtKB:Q8BLF1};
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:0000250|UniProtKB:Q8BLF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36404;
CC Evidence={ECO:0000250|UniProtKB:Q8BLF1};
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:0000250|UniProtKB:Q8BLF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000250|UniProtKB:Q8BLF1};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q6PIU2};
CC Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6PIU2}.
CC Microsome {ECO:0000250|UniProtKB:Q8BLF1}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q6PIU2}.
CC -!- SIMILARITY: Belongs to the 'GDXG' lipolytic enzyme family.
CC {ECO:0000305}.
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DR EMBL; CR859612; CAH91775.1; -; mRNA.
DR RefSeq; NP_001126028.1; NM_001132556.1.
DR AlphaFoldDB; Q5R8Y5; -.
DR SMR; Q5R8Y5; -.
DR STRING; 9601.ENSPPYP00000015990; -.
DR ESTHER; ponab-nceh1; Arylacetamide_deacetylase.
DR GeneID; 100172976; -.
DR KEGG; pon:100172976; -.
DR CTD; 57552; -.
DR eggNOG; KOG1515; Eukaryota.
DR InParanoid; Q5R8Y5; -.
DR OrthoDB; 1263520at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047378; F:acetylalkylglycerol acetylhydrolase activity; IEA:RHEA.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 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 Pfam; PF07859; Abhydrolase_3; 2.
DR PIRSF; PIRSF037251; Arylacetamide_deacetylase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS01174; LIPASE_GDXG_SER; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid metabolism; Membrane; Microsome;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..408
FT /note="Neutral cholesterol ester hydrolase 1"
FT /id="PRO_0000265941"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..25
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..408
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT MOTIF 113..115
FT /note="Involved in the stabilization of the negatively
FT charged intermediate by the formation of the oxyanion hole"
FT /evidence="ECO:0000250|UniProtKB:Q5NUF3"
FT ACT_SITE 191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT ACT_SITE 378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10038"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 408 AA; 45779 MW; 62E495B28AA66916 CRC64;
MRSSCVLLTA LVALAAYYVY IPLPGSVSDP WKLMLLDATF RGAQQVSNLI HYLGLSHHLL
ALNFIIVSFG KKSAWSSAQV KVTDTDFDGV EVRVFEGPPK PEEPLKRSVV YIHGGGWALA
SAKIRYYDEL CTAMAEELNA VIVSIEYRLV PKVYFPEQIH DVVRATKYFL KPEVLQKYMV
DPGRICISGD SAGGSLAAAL GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT
PILPRYVMVK YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA ALRARLNWTS LLPASFTKNY
KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL RDDGIMYAKR
LETAGVEVTL DHFEDGFHGC MIFTSRPTNF SVGIRTRNSY IKWLDQNL
