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Protein

Neutral cholesterol ester hydrolase 1

Gene

Nceh1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei191 – 1911PROSITE-ProRule annotation
Active sitei348 – 3481PROSITE-ProRule annotation
Active sitei378 – 3781PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-RNO-73923. Lipid digestion, mobilization, and transport.

Protein family/group databases

ESTHERirat-nceh1. Hormone-sensitive_lipase_like_1.

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
Gene namesi
Name:Nceh1
Synonyms:Aadacl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1311104. Nceh1.

Subcellular locationi

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

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 408408Neutral cholesterol ester hydrolase 1PRO_0000353849Add
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

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiB2GV54.
PeptideAtlasiB2GV54.
PRIDEiB2GV54.

PTM databases

UniCarbKBiB2GV54.

Expressioni

Gene expression databases

GenevisibleiB2GV54. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017805.

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

eggNOGiKOG1515. Eukaryota.
COG0657. LUCA.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiB2GV54.
KOiK14349.
OMAiALGQQFT.
OrthoDBiEOG7HB599.
PhylomeDBiB2GV54.
TreeFamiTF314978.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR033140. Lipase_GDXG_put_SER_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.

B2GV54-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSSCVLLAA LLALVAYYVY IPLPSAVSDP WKLMLLDATF RGAQQVSNLI
60 70 80 90 100
HSLGLSHHLI TLNFIIISFG KKSARSSPRV KVTDTDFDGV EVRVFEGPPK
110 120 130 140 150
PDEPLRRSVV YIHGGGWALA SAKISYYDQL CTAMAEELNA VIVSIEYRLV
160 170 180 190 200
PQVYFPEQIH DVIRATKYFL QPEVLDKYKV DPGRVGVSGD SAGGNLAAAL
210 220 230 240 250
GQQFTYVESL KNKLKLQALI YPVLQALDFN TPSYQQSMNT PILPRHVMVR
260 270 280 290 300
YWVDYFKGNY DFVEAMIVNN HTSLDVERAA ALRARLDWTS LLPSSIKKNY
310 320 330 340 350
KPVLQTIGDA RIVKEIPQLL DAAASPLIAE QEVLQALPKT YILTCEHDVL
360 370 380 390 400
RDDGIMYAKR LESAGVNVTL DHFEDGFHGC MIFTSWPTNF SVGIRTRDSY

FKWLDQNL
Length:408
Mass (Da):45,822
Last modified:June 10, 2008 - v1
Checksum:i52E97843930778E4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473961 Genomic DNA. Translation: EDM01112.1.
BC166533 mRNA. Translation: AAI66533.1.
RefSeqiNP_001120996.1. NM_001127524.2.
UniGeneiRn.229209.

Genome annotation databases

EnsembliENSRNOT00000017805; ENSRNOP00000017805; ENSRNOG00000013313.
GeneIDi294930.
KEGGirno:294930.
UCSCiRGD:1311104. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH473961 Genomic DNA. Translation: EDM01112.1.
BC166533 mRNA. Translation: AAI66533.1.
RefSeqiNP_001120996.1. NM_001127524.2.
UniGeneiRn.229209.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000017805.

Protein family/group databases

ESTHERirat-nceh1. Hormone-sensitive_lipase_like_1.

PTM databases

UniCarbKBiB2GV54.

Proteomic databases

PaxDbiB2GV54.
PeptideAtlasiB2GV54.
PRIDEiB2GV54.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000017805; ENSRNOP00000017805; ENSRNOG00000013313.
GeneIDi294930.
KEGGirno:294930.
UCSCiRGD:1311104. rat.

Organism-specific databases

CTDi57552.
RGDi1311104. Nceh1.

Phylogenomic databases

eggNOGiKOG1515. Eukaryota.
COG0657. LUCA.
GeneTreeiENSGT00550000074556.
HOGENOMiHOG000033738.
HOVERGENiHBG058974.
InParanoidiB2GV54.
KOiK14349.
OMAiALGQQFT.
OrthoDBiEOG7HB599.
PhylomeDBiB2GV54.
TreeFamiTF314978.

Enzyme and pathway databases

ReactomeiR-RNO-73923. Lipid digestion, mobilization, and transport.

Miscellaneous databases

PROiB2GV54.

Gene expression databases

GenevisibleiB2GV54. RN.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR013094. AB_hydrolase_3.
IPR017157. Arylacetamide_deacetylase.
IPR033140. Lipase_GDXG_put_SER_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

  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "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].
    Tissue: Heart.

Entry informationi

Entry nameiNCEH1_RAT
AccessioniPrimary (citable) accession number: B2GV54
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: June 10, 2008
Last modified: July 6, 2016
This is version 55 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.