NCEH1_BOVIN
ID NCEH1_BOVIN Reviewed; 408 AA.
AC Q1JQE6;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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; BC115993; AAI15994.2; -; mRNA.
DR RefSeq; NP_001116506.1; NM_001123034.1.
DR AlphaFoldDB; Q1JQE6; -.
DR SMR; Q1JQE6; -.
DR STRING; 9913.ENSBTAP00000026745; -.
DR ESTHER; bovin-nceh1; Arylacetamide_deacetylase.
DR PaxDb; Q1JQE6; -.
DR PRIDE; Q1JQE6; -.
DR Ensembl; ENSBTAT00000026745; ENSBTAP00000026745; ENSBTAG00000020073.
DR GeneID; 534212; -.
DR KEGG; bta:534212; -.
DR CTD; 57552; -.
DR VEuPathDB; HostDB:ENSBTAG00000020073; -.
DR VGNC; VGNC:31911; NCEH1.
DR eggNOG; KOG1515; Eukaryota.
DR GeneTree; ENSGT00940000156699; -.
DR HOGENOM; CLU_012494_12_0_1; -.
DR InParanoid; Q1JQE6; -.
DR OMA; ISDPWKL; -.
DR OrthoDB; 1263520at2759; -.
DR TreeFam; TF314978; -.
DR Reactome; R-BTA-8964038; LDL clearance.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000020073; Expressed in thymus and 99 other tissues.
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:0042301; F:phosphate ion binding; IEA:Ensembl.
DR GO; GO:0017171; F:serine hydrolase activity; IBA:GO_Central.
DR GO; GO:0046485; P:ether lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:Ensembl.
DR GO; GO:0060395; P:SMAD protein signal transduction; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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_0000352850"
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; 46026 MW; 91F33861B07ED838 CRC64;
MRSSCVLLTA LLALAAYYIY IPLPSSVSDP WKLMLLDATF RSAQQVSNLI HFLGLSHHLL
ALNFIIVSFG KKSAWSSAQV KVTDTDFDGV EVRVFEGPPK PEEPLKRSIV YIHGGGWALA
SAKIRYYDEL CTTMAEELNA VIVSIEYRLV PKVYFPEQIH DVVHATKYFL QPEVLHKYSV
DPGRVGISGD SAGGNLAAAL GQQFNQDTNL KNKLKVQALI YPVLQALDFN TPSYQQNMNT
PILPRYVMVK YWVDYFNGNY DFVQAMIVNN HTSLDVDEAS ALRARLNWTS LLPTSITKNY
KPVMQTTGNS RIVQEIPQLL DARSAPLIAD QEVLQHLPKT YILTCEHDVL RDDGIMYAKR
LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY IKWLDQNL
