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Q6PIU2 (NCEH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
Gene names
Name:NCEH1
Synonyms:AADACL1, KIAA1363
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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, thereby contributing to the development of atherosclerosis. Also involved in organ detoxification by hydrolyzing exogenous organophosphorus compounds. May contribute to cancer pathogenesis by promoting tumor cell migration. Ref.6

Subcellular location

Membrane; Single-pass type II membrane protein Probable. Microsome By similarity Ref.5.

Tissue specificity

Expressed in monocyte-derived macrophages. Up-regulated in invasive melanoma and breast carcinoma cell lines. Ref.5 Ref.7

Post-translational modification

N-glycosylated. Ref.5

Sequence similarities

Belongs to the 'GDXG' lipolytic enzyme family.

Sequence caution

The sequence AAH28734.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH47588.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AC007919 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AC069237 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA92601.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAH13028.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAH14142.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAH14802.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PIU2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6PIU2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     123-123: K → SASWSPSDE
Isoform 3 (identifier: Q6PIU2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-133: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Neutral cholesterol ester hydrolase 1
PRO_0000265939

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 By similarity
Active site3481 By similarity
Active site3781 By similarity

Amino acid modifications

Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Ref.8
Glycosylation3891N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 133133Missing in isoform 3.
VSP_037518
Alternative sequence1231K → SASWSPSDE in isoform 2.
VSP_037519
Natural variant191V → F.
Corresponds to variant rs35316420 [ dbSNP | Ensembl ].
VAR_047099
Natural variant711K → Q.
Corresponds to variant rs2302815 [ dbSNP | Ensembl ].
VAR_047100
Natural variant3431L → M. Ref.4
Corresponds to variant rs17857335 [ dbSNP | Ensembl ].
VAR_047101

Experimental info

Sequence conflict161A → T in BAA92601. Ref.1
Sequence conflict581H → R in BAH13028. Ref.2
Sequence conflict721K → R in BAH14802. Ref.2
Sequence conflict791Q → K in AAH47588. Ref.4
Sequence conflict2541D → G in BAH14142. Ref.2
Sequence conflict3291A → S in BAH14142. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 12, 2006. Version 3.
Checksum: E5754850BE9805B5

FASTA40845,808
        10         20         30         40         50         60 
MRSSCVLLTA LVALAAYYVY IPLPGSVSDP WKLMLLDATF RGAQQVSNLI HYLGLSHHLL 

        70         80         90        100        110        120 
ALNFIIVSFG KKSAWSSAQV KVTDTDFDGV EVRVFEGPPK PEEPLKRSVV YIHGGGWALA 

       130        140        150        160        170        180 
SAKIRYYDEL CTAMAEELNA VIVSIEYRLV PKVYFPEQIH DVVRATKYFL KPEVLQKYMV 

       190        200        210        220        230        240 
DPGRICISGD SAGGNLAAAL GQQFTQDASL KNKLKLQALI YPVLQALDFN TPSYQQNVNT 

       250        260        270        280        290        300 
PILPRYVMVK YWVDYFKGNY DFVQAMIVNN HTSLDVEEAA AVRARLNWTS LLPASFTKNY 

       310        320        330        340        350        360 
KPVVQTTGNA RIVQELPQLL DARSAPLIAD QAVLQLLPKT YILTCEHDVL RDDGIMYAKR 

       370        380        390        400 
LESAGVEVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRNSY IKWLDQNL 

« Hide

Isoform 2 [UniParc].

Checksum: A315923F59D660E7
Show »

FASTA41646,627
Isoform 3 [UniParc].

Checksum: 1D5212243D62F48B
Show »

FASTA27531,168

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Brain, Hippocampus, Testis, Tongue and Trachea.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1), VARIANT MET-343.
Tissue: Brain.
[5]"Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness."
Jessani N., Liu Y., Humphrey M., Cravatt B.F.
Proc. Natl. Acad. Sci. U.S.A. 99:10335-10340(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
[6]"An enzyme that regulates ether lipid signaling pathways in cancer annotated by multidimensional profiling."
Chiang K.P., Niessen S., Saghatelian A., Cravatt B.F.
Chem. Biol. 13:1041-1050(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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: TISSUE SPECIFICITY.
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-287.
Tissue: Liver.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB037784 mRNA. Translation: BAA92601.1. Different initiation.
AK294811 mRNA. Translation: BAH11890.1.
AK295641 mRNA. Translation: BAH12137.1.
AK299422 mRNA. Translation: BAH13028.1. Different initiation.
AK304253 mRNA. Translation: BAH14142.1. Different initiation.
AK316431 mRNA. Translation: BAH14802.1. Different initiation.
AC007919 Genomic DNA. No translation available.
AC069237 Genomic DNA. No translation available.
BC028734 mRNA. Translation: AAH28734.2. Different initiation.
BC047588 mRNA. Translation: AAH47588.2. Different initiation.
RefSeqNP_001139748.1. NM_001146276.1.
NP_001139749.1. NM_001146277.1.
NP_001139750.1. NM_001146278.1.
NP_065843.3. NM_020792.4.
UniGeneHs.444099.

3D structure databases

ProteinModelPortalQ6PIU2.
SMRQ6PIU2. Positions 79-408.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ6PIU2. 1 interaction.
STRING9606.ENSP00000273512.

Chemistry

BindingDBQ6PIU2.
ChEMBLCHEMBL5048.

Protein family/group databases

MEROPSS09.992.

PTM databases

PhosphoSiteQ6PIU2.

Polymorphism databases

DMDM74737782.

Proteomic databases

PaxDbQ6PIU2.
PRIDEQ6PIU2.

Protocols and materials databases

DNASU57552.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000475381; ENSP00000418571; ENSG00000144959. [Q6PIU2-1]
ENST00000538775; ENSP00000442464; ENSG00000144959.
ENST00000543711; ENSP00000443227; ENSG00000144959. [Q6PIU2-3]
GeneID57552.
KEGGhsa:57552.
UCSCuc011bpw.2. human. [Q6PIU2-1]

Organism-specific databases

CTD57552.
GeneCardsGC03M172348.
H-InvDBHIX0003864.
HIX0163448.
HGNCHGNC:29260. NCEH1.
HPAHPA026888.
MIM613234. gene.
neXtProtNX_Q6PIU2.
PharmGKBPA165697847.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0657.
HOVERGENHBG058974.
InParanoidQ6PIU2.
KOK14349.
OMAALGQQFT.
OrthoDBEOG7HB599.
PhylomeDBQ6PIU2.

Gene expression databases

ArrayExpressQ6PIU2.
BgeeQ6PIU2.
CleanExHS_AADACL1.
GenevestigatorQ6PIU2.

Family and domain databases

InterProIPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR002168. Lipase_GDXG_AS.
[Graphical view]
PfamPF07859. Abhydrolase_3. 2 hits.
[Graphical view]
PIRSFPIRSF037251. Arylacetamide_deacetylase. 1 hit.
PROSITEPS01174. LIPASE_GDXG_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNCEH1. human.
GeneWikiNCEH1.
GenomeRNAi57552.
NextBio64018.
PROQ6PIU2.
SOURCESearch...

Entry information

Entry nameNCEH1_HUMAN
AccessionPrimary (citable) accession number: Q6PIU2
Secondary accession number(s): B7Z2K4 expand/collapse secondary AC list , B7Z3A1, B7Z5U2, B7Z906, B7ZAW6, F5H7K4, Q86WZ1, Q9P2I4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM