Neutral cholesterol ester hydrolase 1

Preferred order of sections

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Protein existence	Evidence 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.5
Subcellular location	Membrane; Single-pass type II membrane protein Probable. Microsome By similarity Ref.4.
Tissue specificity	Expressed in monocyte-derived macrophages. Up-regulated in invasive melanoma and breast carcinoma cell lines. Ref.4 Ref.6
Post-translational modification	N-glycosylated. Ref.4 Ref.7
Sequence similarities	Belongs to the 'GDXG' lipolytic enzyme family.
Sequence caution	The sequence AAH28734.2 differs from that shown. Reason: Erroneous initiation. The sequence AAH47588.2 differs from that shown. Reason: Erroneous initiation. The sequence BAA92601.1 differs from that shown. Reason: Erroneous initiation. The sequence BAH13028.1 differs from that shown. Reason: Erroneous initiation. The sequence BAH14142.1 differs from that shown. Reason: Erroneous initiation. The sequence BAH14802.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Hydrolase
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	carboxylesterase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 408

408

Neutral cholesterol ester hydrolase 1

PRO_0000265939

Regions

Topological domain

1 – 4

4

Cytoplasmic Potential

Transmembrane

5 – 25

21

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

26 – 408

383

Lumenal Potential

Sites

Active site

191

1

By similarity

Active site

348

1

By similarity

Active site

378

1

By similarity

Amino acid modifications

Glycosylation

270

1

N-linked (GlcNAc...) Potential

Glycosylation

287

1

N-linked (GlcNAc...) Ref.7

Glycosylation

389

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 133

133

Missing in isoform 3.

VSP_037518

Alternative sequence

123

1

K → SASWSPSDE in isoform 2.

VSP_037519

Natural variant

19

1

V → F.
Corresponds to variant rs35316420 [ dbSNP | Ensembl ].

VAR_047099

Natural variant

71

1

K → Q.
Corresponds to variant rs2302815 [ dbSNP | Ensembl ].

VAR_047100

Natural variant

343

1

L → M. Ref.3
Corresponds to variant rs17857335 [ dbSNP | Ensembl ].

VAR_047101

Experimental info

Sequence conflict

16

1

A → T in BAA92601. Ref.1

Sequence conflict

58

1

H → R in BAH13028. Ref.2

Sequence conflict

72

1

K → R in BAH14802. Ref.2

Sequence conflict

79

1

Q → K in AAH47588. Ref.3

Sequence conflict

254

1

D → G in BAH14142. Ref.2

Sequence conflict

329

1

A → S in BAH14142. Ref.2

Sequences

Sequence		Length	Mass (Da)
Isoform 1 [UniParc]. Last modified December 12, 2006. Version 3. Checksum: E5754850BE9805B5 Show »	FASTA	408	45,808
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 »	FASTA	416	46,627
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 SASASWSPSD EIRYYDELCT AMAEELNAVI VSIEYRLVPK VYFPEQIHDV VRATKYFLKP 190 200 210 220 230 240 EVLQKYMVDP GRICISGDSA GGNLAAALGQ QFTQDASLKN KLKLQALIYP VLQALDFNTP 250 260 270 280 290 300 SYQQNVNTPI LPRYVMVKYW VDYFKGNYDF VQAMIVNNHT SLDVEEAAAV RARLNWTSLL 310 320 330 340 350 360 PASFTKNYKP VVQTTGNARI VQELPQLLDA RSAPLIADQA VLQLLPKTYI LTCEHDVLRD 370 380 390 400 410 DGIMYAKRLE SAGVEVTLDH FEDGFHGCMI FTSWPTNFSV GIRTRNSYIK WLDQNL « Hide
Isoform 3 [UniParc]. Checksum: 1D5212243D62F48B Show »	FASTA	275	31,168
10 20 30 40 50 60 MAEELNAVIV SIEYRLVPKV YFPEQIHDVV RATKYFLKPE VLQKYMVDPG RICISGDSAG 70 80 90 100 110 120 GNLAAALGQQ FTQDASLKNK LKLQALIYPV LQALDFNTPS YQQNVNTPIL PRYVMVKYWV 130 140 150 160 170 180 DYFKGNYDFV QAMIVNNHTS LDVEEAAAVR ARLNWTSLLP ASFTKNYKPV VQTTGNARIV 190 200 210 220 230 240 QELPQLLDAR SAPLIADQAV LQLLPKTYIL TCEHDVLRDD GIMYAKRLES AGVEVTLDHF 250 260 270 EDGFHGCMIF TSWPTNFSVG IRTRNSYIKW LDQNL « Hide

References

	« Hide 'large scale' referencesShow '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: 10718198] [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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Brain, Hippocampus, Testis, Tongue and Trachea.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-343. Tissue: Brain.
[4]	"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: 12149457] [Abstract] Cited for: TISSUE SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION.
[5]	"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: 17052608] [Abstract] Cited for: FUNCTION.
[6]	"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: 18782767] [Abstract] Cited for: TISSUE SPECIFICITY.
[7]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-287, MASS SPECTROMETRY. Tissue: Liver.
+	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. BC028734 mRNA. Translation: AAH28734.2. Different initiation. BC047588 mRNA. Translation: AAH47588.2. Different initiation.
IPI	IPI00002230. IPI00790972. IPI00924788.
RefSeq	NP_001139748.1. NM_001146276.1. NP_001139749.1. NM_001146277.1. NP_001139750.1. NM_001146278.1. NP_065843.3. NM_020792.4.
UniGene	Hs.444099.
3D structure databases
HSSP	HSSP built from PDB template 2C7B based on UniProtKB Q5G935.
ProteinModelPortal	Q6PIU2.
SMR	Q6PIU2. Positions 79-408.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6PIU2. 1 interaction.
STRING	Q6PIU2.
Protein family/group databases
MEROPS	S09.992.
PTM databases
PhosphoSite	Q6PIU2.
Polymorphism databases
DMDM	74737782.
Proteomic databases
PRIDE	Q6PIU2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000273512; ENSP00000273512; ENSG00000144959. ENST00000475381; ENSP00000418571; ENSG00000144959.
GeneID	57552.
KEGG	hsa:57552.
UCSC	uc003fig.1. human.
Organism-specific databases
CTD	57552.
GeneCards	GC03M172348.
H-InvDB	HIX0003864.
HGNC	HGNC:29260. NCEH1.
HPA	HPA026888.
MIM	613234. gene.
neXtProt	NX_Q6PIU2.
PharmGKB	PA142670462. PA165697847.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07972.
GeneTree	ENSGT00550000074556.
HOVERGEN	HBG058974.
InParanoid	Q6PIU2.
OrthoDB	EOG4PVP02.
Gene expression databases
ArrayExpress	Q6PIU2.
Bgee	Q6PIU2.
CleanEx	HS_AADACL1.
Genevestigator	Q6PIU2.
GermOnline	ENSG00000144959. Homo sapiens.
Family and domain databases
InterPro	IPR013094. AB_hydrolase_3. IPR017157. Arylacetamide_deacetylase. IPR002168. Lipase_GDXG_AS. [Graphical view]
KO	K14349.
Pfam	PF07859. Abhydrolase_3. 2 hits. [Graphical view]
PIRSF	PIRSF037251. Arylacetamide_deacetylase. 1 hit.
PROSITE	PS01173. LIPASE_GDXG_HIS. False negative. PS01174. LIPASE_GDXG_SER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	64018.
SOURCE	Search...

Entry information

Entry name

NCEH1_HUMAN

Accession

Primary (citable) accession number: Q6PIU2
Secondary accession number(s): B7Z2K4

Q9P2I4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 12, 2006
Last sequence update:	December 12, 2006
Last modified:	January 25, 2012
This is version 69 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents