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Q8BLF1 (NCEH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neutral cholesterol ester hydrolase 1

Short name=NCEH
EC=3.1.1.-
Alternative name(s):
Arylacetamide deacetylase-like 1
Chlorpyrifos oxon-binding protein
Short name=CPO-BP
Gene names
Name:Nceh1
Synonyms:Aadacl1, Kiaa1363
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7 Ref.8

Enzyme regulation

Inhibited by bulky trifluoromethyl ketones. Ref.4

Subcellular location

Membrane; Single-pass type II membrane protein By similarity. Microsome Ref.7.

Tissue specificity

Present in brain, heart, kidney, lung, spinal cord and testis but not liver (at protein level). Expressed in peritoneal macrophages and kidney. Ref.6 Ref.7

Post-translational modification

N-glycosylated. Ref.4

Disruption phenotype

Mice are phenotypically normal but more sensitive to organophosphorus insecticide toxicity. Ref.5

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.2 for cholesterol ester hydrolysis.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Neutral cholesterol ester hydrolase 1
PRO_0000265940

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2521Helical; Signal-anchor for type II membrane protein; Potential
Topological domain26 – 408383Lumenal Potential
Motif113 – 1153Involved in the stabilization of the negatively charged intermediate by the formation of the oxyanion hole By similarity

Sites

Active site1911 Probable
Active site3481 Probable
Active site3781 Probable

Amino acid modifications

Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation3671N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict931R → Q in BAC28680. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BLF1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: FFEC0EA1CDCB59E7

FASTA40845,740
        10         20         30         40         50         60 
MRSSCVLLAA LLALAAYYVY IPLPSAVSDP WKLMLLDATF RGAQQVSNLI HSLGLNHHLI 

        70         80         90        100        110        120 
ALNFIITSFG KQSARSSPKV KVTDTDFDGV EVRVFEGSPK PEEPLRRSVI YIHGGGWALA 

       130        140        150        160        170        180 
SAKISYYDQL CTTMAEELNA VIVSIEYRLV PQVYFPEQIH DVIRATKYFL QPEVLDKYKV 

       190        200        210        220        230        240 
DPGRVGISGD SAGGNLAAAL GQQFTYVASL KNKLKLQALV YPVLQALDFN TPSYQQSMNT 

       250        260        270        280        290        300 
PILPRHVMVR YWLDYFKGNY DFVEAMIVNN HTSLDVERAA ALRARLDWTS LLPSSIKKNY 

       310        320        330        340        350        360 
KPIMQTTGNA RIVQEIPQLL DAAASPLIAE QEVLEALPKT YILTCEHDVL RDDGIMYAKR 

       370        380        390        400 
LESAGVNVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY IKWLDQNL 

« Hide

References

« Hide 'large scale' references
[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(2004) [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. expand/collapse author list , 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(2005) [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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, GLYCOSYLATION.
[5]"A brain detoxifying enzyme for organophosphorus nerve poisons."
Nomura D.K., Leung D., Chiang K.P., Quistad G.B., Cravatt B.F., Casida J.E.
Proc. Natl. Acad. Sci. U.S.A. 102:6195-6200(2005) [PubMed] [Europe PMC] [Abstract]
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(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ACTIVE SITE, TISSUE SPECIFICITY.
[7]"Identification of neutral cholesterol ester hydrolase, a key enzyme removing cholesterol from macrophages."
Okazaki H., Igarashi M., Nishi M., Sekiya M., Tajima M., Takase S., Takanashi M., Ohta K., Tamura Y., Okazaki S., Yahagi N., Ohashi K., Amemiya-Kudo M., Nakagawa Y., Nagai R., Kadowaki T., Osuga J., Ishibashi S.
J. Biol. Chem. 283:33357-33364(2008) [PubMed] [Europe PMC] [Abstract]
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(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17271.1.
RefSeqNP_848887.1. NM_178772.3.
UniGeneMm.24576.

3D structure databases

ProteinModelPortalQ8BLF1.
SMRQ8BLF1. Positions 61-262, 293-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BLF1. 3 interactions.
MINTMINT-4113633.
STRING10090.ENSMUSP00000045864.

Chemistry

BindingDBQ8BLF1.
ChEMBLCHEMBL5428.

Protein family/group databases

MEROPSS09.992.

PTM databases

PhosphoSiteQ8BLF1.

Proteomic databases

MaxQBQ8BLF1.
PaxDbQ8BLF1.
PRIDEQ8BLF1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046515; ENSMUSP00000045864; ENSMUSG00000027698.
GeneID320024.
KEGGmmu:320024.
UCSCuc008otl.1. mouse.

Organism-specific databases

CTD57552.
MGIMGI:2443191. Nceh1.
RougeSearch...

Phylogenomic databases

eggNOGCOG0657.
GeneTreeENSGT00550000074556.
HOGENOMHOG000033738.
HOVERGENHBG058974.
InParanoidQ8BLF1.
KOK14349.
OMAALGQQFT.
OrthoDBEOG7HB599.
PhylomeDBQ8BLF1.
TreeFamTF314978.

Gene expression databases

BgeeQ8BLF1.
CleanExMM_AADACL1.
GenevestigatorQ8BLF1.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFPIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMSSF53474. SSF53474. 2 hits.
PROSITEPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCEH1. mouse.
NextBio395889.
PROQ8BLF1.
SOURCESearch...

Entry information

Entry nameNCEH1_MOUSE
AccessionPrimary (citable) accession number: Q8BLF1
Secondary accession number(s): Q69ZL0, Q8BZK3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot