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O88693 (CEGT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Ceramide glucosyltransferase

EC=2.4.1.80
Alternative name(s):
GLCT-1
Glucosylceramide synthase
Short name=GCS
UDP-glucose ceramide glucosyltransferase
UDP-glucose:N-acylsphingosine D-glucosyltransferase
Gene names
Name:Ugcg
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase" By similarity.

Catalytic activity

UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. UniProtKB Q16739

Pathway

Lipid metabolism; sphingolipid metabolism.

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Sphingolipid metabolism
   Cellular componentGolgi apparatus
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsphingolipid metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionceramide glucosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Ceramide glucosyltransferase
PRO_0000059177

Regions

Topological domain1 – 1010Lumenal Potential
Transmembrane11 – 3222Helical; Potential
Topological domain33 – 195163Cytoplasmic Potential
Transmembrane196 – 21520Helical; Potential
Topological domain216 – 28772Lumenal Potential
Transmembrane288 – 30417Helical; Potential
Topological domain305 – 3095Cytoplasmic Potential
Transmembrane310 – 32819Helical; Potential
Topological domain329 – 34820Lumenal Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 39425Cytoplasmic Potential

Sites

Site1931May play an important role in binding to the inhibitors DEPC and PDMP By similarity

Amino acid modifications

Modified residue1171N6-acetyllysine Ref.6

Sequences

Sequence LengthMass (Da)Tools
O88693 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 8B18D09437CACE0E

FASTA39444,839
        10         20         30         40         50         60 
MALLDLAQEG MALFGFVLFV VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK 

        70         80         90        100        110        120 
GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG 

       130        140        150        160        170        180 
INPKINNLMP AYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF 

       190        200        210        220        230        240 
AATLEQVYFG TSHPRSYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA 

       250        260        270        280        290        300 
KAIADRGWRF SMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS 

       310        320        330        340        350        360 
LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT 

       370        380        390 
IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of the mouse ceramide glucosyltransferase gene."
Ichikawa S., Ozawa K., Hirabayashi Y.
Biochem. Biophys. Res. Commun. 253:707-711(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[2]"Molecular cloning and expression of mouse ceramide glucosyltransferase."
Ichikawa S., Ozawa K., Hirabayashi Y.
Biochem. Mol. Biol. Int. 44:1193-1202(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Brain.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Limb.
[6]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012807 Genomic DNA. Translation: BAA33558.1.
D89866 mRNA. Translation: BAA28782.1.
AL808112 Genomic DNA. Translation: CAM26180.1.
CH466565 Genomic DNA. Translation: EDL02214.1.
BC050828 mRNA. Translation: AAH50828.1.
RefSeqNP_035803.1. NM_011673.3.
UniGeneMm.198803.

3D structure databases

ProteinModelPortalO88693.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBO88693.
ChEMBLCHEMBL6013.

Protein family/group databases

CAZyGT21. Glycosyltransferase Family 21.

PTM databases

PhosphoSiteO88693.

Proteomic databases

PRIDEO88693.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030074; ENSMUSP00000030074; ENSMUSG00000028381.
GeneID22234.
KEGGmmu:22234.
UCSCuc008szr.1. mouse.

Organism-specific databases

CTD7357.
MGIMGI:1332243. Ugcg.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeENSGT00390000012898.
HOGENOMHOG000039663.
HOVERGENHBG003997.
InParanoidA2AN90.
KOK00720.
OMALVWICDS.
OrthoDBEOG70KGPR.
PhylomeDBO88693.
TreeFamTF314564.

Enzyme and pathway databases

UniPathwayUPA00222.

Gene expression databases

BgeeO88693.
CleanExMM_UGCG.
GenevestigatorO88693.

Family and domain databases

InterProIPR025993. Ceramide_glucosylTrfase.
[Graphical view]
PfamPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUGCG. mouse.
NextBio302281.
PROO88693.
SOURCESearch...

Entry information

Entry nameCEGT_MOUSE
AccessionPrimary (citable) accession number: O88693
Secondary accession number(s): A2AN90
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 99 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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