Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neutral cholesterol ester hydrolase 1

Gene

Nceh1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes 2-acetyl monoalkylglycerol ether, the penultimate precursor of the pathway for de novo synthesis of platelet-activating factor. May be responsible for cholesterol ester hydrolysis in macrophages. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds.4 Publications

Enzyme regulationi

Inhibited by bulky trifluoromethyl ketones.1 Publication

pH dependencei

Optimum pH is 7.2 for cholesterol ester hydrolysis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 19111 Publication
Active sitei348 – 34811 Publication
Active sitei378 – 37811 Publication

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: InterPro
  2. phosphate ion binding Source: MGI
  3. serine hydrolase activity Source: MGI

GO - Biological processi

  1. lipid catabolic process Source: UniProtKB-KW
  2. protein dephosphorylation Source: MGI
  3. SMAD protein signal transduction Source: MGI
  4. xenobiotic metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi3.1.1.13. 3474.

Protein family/group databases

MEROPSiS09.992.

Names & Taxonomyi

Protein namesi
Recommended name:
Neutral cholesterol ester hydrolase 1 (EC:3.1.1.-)
Short name:
NCEH
Alternative name(s):
Arylacetamide deacetylase-like 1
Chlorpyrifos oxon-binding protein
Short name:
CPO-BP
Gene namesi
Name:Nceh1
Synonyms:Aadacl1, Kiaa1363
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:2443191. Nceh1.

Subcellular locationi

Membrane By similarity; Single-pass type II membrane protein By similarity. Microsome 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44CytoplasmicSequence Analysis
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini26 – 408383LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Disruption phenotypei

Mice are phenotypically normal but more sensitive to organophosphorus insecticide toxicity.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408Neutral cholesterol ester hydrolase 1PRO_0000265940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi270 – 2701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi367 – 3671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8BLF1.
PaxDbiQ8BLF1.
PRIDEiQ8BLF1.

PTM databases

PhosphoSiteiQ8BLF1.

Expressioni

Tissue specificityi

Present in brain, heart, kidney, lung, spinal cord and testis but not liver (at protein level). Expressed in peritoneal macrophages and kidney.2 Publications

Gene expression databases

BgeeiQ8BLF1.
CleanExiMM_AADACL1.
ExpressionAtlasiQ8BLF1. baseline and differential.
GenevestigatoriQ8BLF1.

Interactioni

Protein-protein interaction databases

IntActiQ8BLF1. 3 interactions.
MINTiMINT-4113633.
STRINGi10090.ENSMUSP00000045864.

Structurei

3D structure databases

ProteinModelPortaliQ8BLF1.
SMRiQ8BLF1. Positions 61-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi113 – 1153Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion holeBy similarity

Sequence similaritiesi

Belongs to the 'GDXG' lipolytic enzyme family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiQ8BLF1.
KOiK14349.
OMAiALGQQFT.
OrthoDBiEOG7HB599.
PhylomeDBiQ8BLF1.
TreeFamiTF314978.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BLF1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSCVLLAA LLALAAYYVY IPLPSAVSDP WKLMLLDATF RGAQQVSNLI
60 70 80 90 100
HSLGLNHHLI ALNFIITSFG KQSARSSPKV KVTDTDFDGV EVRVFEGSPK
110 120 130 140 150
PEEPLRRSVI YIHGGGWALA SAKISYYDQL CTTMAEELNA VIVSIEYRLV
160 170 180 190 200
PQVYFPEQIH DVIRATKYFL QPEVLDKYKV DPGRVGISGD SAGGNLAAAL
210 220 230 240 250
GQQFTYVASL KNKLKLQALV YPVLQALDFN TPSYQQSMNT PILPRHVMVR
260 270 280 290 300
YWLDYFKGNY DFVEAMIVNN HTSLDVERAA ALRARLDWTS LLPSSIKKNY
310 320 330 340 350
KPIMQTTGNA RIVQEIPQLL DAAASPLIAE QEVLEALPKT YILTCEHDVL
360 370 380 390 400
RDDGIMYAKR LESAGVNVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY

IKWLDQNL
Length:408
Mass (Da):45,740
Last modified:March 1, 2003 - v1
Checksum:iFFEC0EA1CDCB59E7
GO

Sequence cautioni

The sequence BAD32436.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931R → Q in BAC28680 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173158 mRNA. Translation: BAD32436.1. Different initiation.
AK034339 mRNA. Translation: BAC28680.1.
AK045363 mRNA. Translation: BAC32327.1.
AK135837 mRNA. Translation: BAE22685.1.
BC082569 mRNA. Translation: AAH82569.1.
CCDSiCCDS17271.1.
RefSeqiNP_848887.1. NM_178772.3.
UniGeneiMm.24576.

Genome annotation databases

EnsembliENSMUST00000046515; ENSMUSP00000045864; ENSMUSG00000027698.
GeneIDi320024.
KEGGimmu:320024.
UCSCiuc008otl.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK173158 mRNA. Translation: BAD32436.1. Different initiation.
AK034339 mRNA. Translation: BAC28680.1.
AK045363 mRNA. Translation: BAC32327.1.
AK135837 mRNA. Translation: BAE22685.1.
BC082569 mRNA. Translation: AAH82569.1.
CCDSiCCDS17271.1.
RefSeqiNP_848887.1. NM_178772.3.
UniGeneiMm.24576.

3D structure databases

ProteinModelPortaliQ8BLF1.
SMRiQ8BLF1. Positions 61-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BLF1. 3 interactions.
MINTiMINT-4113633.
STRINGi10090.ENSMUSP00000045864.

Chemistry

BindingDBiQ8BLF1.
ChEMBLiCHEMBL5428.

Protein family/group databases

MEROPSiS09.992.

PTM databases

PhosphoSiteiQ8BLF1.

Proteomic databases

MaxQBiQ8BLF1.
PaxDbiQ8BLF1.
PRIDEiQ8BLF1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000046515; ENSMUSP00000045864; ENSMUSG00000027698.
GeneIDi320024.
KEGGimmu:320024.
UCSCiuc008otl.1. mouse.

Organism-specific databases

CTDi57552.
MGIiMGI:2443191. Nceh1.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG0657.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiQ8BLF1.
KOiK14349.
OMAiALGQQFT.
OrthoDBiEOG7HB599.
PhylomeDBiQ8BLF1.
TreeFamiTF314978.

Enzyme and pathway databases

BRENDAi3.1.1.13. 3474.

Miscellaneous databases

ChiTaRSiNceh1. mouse.
NextBioi395889.
PROiQ8BLF1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BLF1.
CleanExiMM_AADACL1.
ExpressionAtlasiQ8BLF1. baseline and differential.
GenevestigatoriQ8BLF1.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamiPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFiPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic intestine.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Diencephalon.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6.
    Tissue: Eye.
  4. "Discovering potent and selective reversible inhibitors of enzymes in complex proteomes."
    Leung D., Hardouin C., Boger D.L., Cravatt B.F.
    Nat. Biotechnol. 21:687-691(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, GLYCOSYLATION.
  5. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Serine hydrolase KIAA1363: toxicological and structural features with emphasis on organophosphate interactions."
    Nomura D.K., Durkin K.A., Chiang K.P., Quistad G.B., Cravatt B.F., Casida J.E.
    Chem. Res. Toxicol. 19:1142-1150(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ACTIVE SITE, TISSUE SPECIFICITY.
  7. Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. "Dual roles of brain serine hydrolase KIAA1363 in ether lipid metabolism and organophosphate detoxification."
    Nomura D.K., Fujioka K., Issa R.S., Ward A.M., Cravatt B.F., Casida J.E.
    Toxicol. Appl. Pharmacol. 228:42-48(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiNCEH1_MOUSE
AccessioniPrimary (citable) accession number: Q8BLF1
Secondary accession number(s): Q69ZL0, Q8BZK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 1, 2003
Last modified: April 1, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.