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Q8BLF1

- NCEH1_MOUSE

UniProt

Q8BLF1 - NCEH1_MOUSE

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Protein

Neutral cholesterol ester hydrolase 1

Gene
Nceh1, Aadacl1, Kiaa1363
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 1911 Inferred
Active sitei348 – 3481 Inferred
Active sitei378 – 3781 Inferred

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. xenobiotic metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

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: Chromosome 3

Organism-specific databases

MGIiMGI:2443191. Nceh1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2521Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini26 – 408383Lumenal Reviewed predictionAdd
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...) Reviewed prediction
Glycosylationi367 – 3671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi389 – 3891N-linked (GlcNAc...) Reviewed prediction

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.
GenevestigatoriQ8BLF1.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8BLF1.
SMRiQ8BLF1. Positions 61-262, 293-385.

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 hole By similarity

Sequence similaritiesi

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

MRSSCVLLAA LLALAAYYVY IPLPSAVSDP WKLMLLDATF RGAQQVSNLI    50
HSLGLNHHLI ALNFIITSFG KQSARSSPKV KVTDTDFDGV EVRVFEGSPK 100
PEEPLRRSVI YIHGGGWALA SAKISYYDQL CTTMAEELNA VIVSIEYRLV 150
PQVYFPEQIH DVIRATKYFL QPEVLDKYKV DPGRVGISGD SAGGNLAAAL 200
GQQFTYVASL KNKLKLQALV YPVLQALDFN TPSYQQSMNT PILPRHVMVR 250
YWLDYFKGNY DFVEAMIVNN HTSLDVERAA ALRARLDWTS LLPSSIKKNY 300
KPIMQTTGNA RIVQEIPQLL DAAASPLIAE QEVLEALPKT YILTCEHDVL 350
RDDGIMYAKR LESAGVNVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY 400
IKWLDQNL 408
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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931R → Q in BAC28680. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS17271.1.
RefSeqi NP_848887.1. NM_178772.3.
UniGenei Mm.24576.

3D structure databases

ProteinModelPortali Q8BLF1.
SMRi Q8BLF1. Positions 61-262, 293-385.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8BLF1. 3 interactions.
MINTi MINT-4113633.
STRINGi 10090.ENSMUSP00000045864.

Chemistry

BindingDBi Q8BLF1.
ChEMBLi CHEMBL5428.

Protein family/group databases

MEROPSi S09.992.

PTM databases

PhosphoSitei Q8BLF1.

Proteomic databases

MaxQBi Q8BLF1.
PaxDbi Q8BLF1.
PRIDEi Q8BLF1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000046515 ; ENSMUSP00000045864 ; ENSMUSG00000027698 .
GeneIDi 320024.
KEGGi mmu:320024.
UCSCi uc008otl.1. mouse.

Organism-specific databases

CTDi 57552.
MGIi MGI:2443191. Nceh1.
Rougei Search...

Phylogenomic databases

eggNOGi COG0657.
GeneTreei ENSGT00550000074556.
HOGENOMi HOG000033738.
HOVERGENi HBG058974.
InParanoidi Q8BLF1.
KOi K14349.
OMAi ALGQQFT.
OrthoDBi EOG7HB599.
PhylomeDBi Q8BLF1.
TreeFami TF314978.

Miscellaneous databases

ChiTaRSi NCEH1. mouse.
NextBioi 395889.
PROi Q8BLF1.
SOURCEi Search...

Gene expression databases

Bgeei Q8BLF1.
CleanExi MM_AADACL1.
Genevestigatori Q8BLF1.

Family and domain databases

Gene3Di 3.40.50.1820. 2 hits.
InterProi IPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view ]
Pfami PF07859. Abhydrolase_3. 2 hits.
[Graphical view ]
PIRSFi PIRSF037251. Arylacetamide_deacetylase. 1 hit.
SUPFAMi SSF53474. SSF53474. 2 hits.
PROSITEi PS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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. 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. 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.

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: July 9, 2014
This is version 98 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