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Q9R0E0 (CEGT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. Able to use UDP-galactose to synthesize galactosylceramide with 10% of efficiency with which it utilizes UDP-glucose. May also serve as a "flippase". Ref.1

Catalytic activity

UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. Ref.1

Pathway

Lipid metabolism; sphingolipid metabolism.

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein Ref.3.

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Sphingolipid metabolism
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   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 direct assay Ref.1. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Ceramide glucosyltransferase
PRO_0000059178

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

Amino acid modifications

Modified residue1171N6-acetyllysine By similarity

Natural variations

Natural variant81Q → L in strain: Wistar.
Natural variant891D → G in strain: Wistar.
Natural variant1531T → S in strain: Wistar.
Natural variant1791G → A in strain: Wistar.
Natural variant3871T → I in strain: Wistar.

Experimental info

Mutagenesis261H → A: Inhibits activity to less than 6%. Ref.1
Mutagenesis261H → D: Inhibits activity to about 10%. Ref.1
Mutagenesis261H → N: Inhibits activity to about 50%. Ref.1
Mutagenesis261H → R: No effect on activity. Decreased sensitivity to the inhibitor PDMP. Ref.1
Mutagenesis361H → A: No effect on activity. Ref.1
Mutagenesis901H → A: No effect on activity. Ref.1
Mutagenesis1691H → A: Inhibits activity to about 30%. Decreased sensitivity to PDMP. Ref.1
Mutagenesis1931H → A: Inhibits activity to about 30%. Insensitive to the inhibitors DEPC and PDMP. Ref.1
Mutagenesis1931H → D: Abolishes activity. Ref.1
Mutagenesis1931H → N: Inhibits activity to about 20%. Insensitive to the inhibitors DEPC and PDMP. Ref.1
Mutagenesis1931H → R: Abolishes activity. Ref.1
Mutagenesis308 – 3092HH → AA: Inhibits activity to about 10%. Ref.1
Mutagenesis3081H → A: Inhibits activity to about 35%. Ref.1
Mutagenesis3091H → A: Inhibits activity to about 70%. Ref.1
Mutagenesis3221H → A: Inhibits activity to less than 6%. Ref.1
Mutagenesis3221H → D: Inhibits activity to less than 6%. Ref.1
Mutagenesis3221H → N: Inhibits activity to about 50%. Ref.1
Mutagenesis3221H → R: Abolishes activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R0E0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 214581C0B8D9152C

FASTA39444,823
        10         20         30         40         50         60 
MALLDLAQEG MALFGFVLFV VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK 

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

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

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

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

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

       370        380        390 
IYIFLSALWD PTISWRAGRY RLRCGGTAEE ILDV 

« Hide

References

[1]"Histidine-193 of rat glucosylceramide synthase resides in a UDP-glucose- and inhibitor (D-threo-1-phenyl-2-decanoylamino-3-morpholinopropan-1-ol)-binding region: a biochemical and mutational study."
Wu K., Marks D.L., Watanabe R., Paul P., Rajan N., Pagano R.E.
Biochem. J. 341:395-400(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-26; HIS-36; HIS-90; HIS-169; HIS-193; HIS-308; HIS-309; 308-HIS-HIS-309 AND HIS-322.
Strain: Sprague-Dawley.
Tissue: Brain.
[2]"Purification and characterization of glucosylceramide synthase."
Buenning C., Orci L., Hirabayashi Y., Wieland F.T., Jeckel D.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[3]"Oligomerization and topology of the Golgi membrane protein glucosylceramide synthase."
Marks D.L., Wu K., Paul P., Kamisaka Y., Watanabe R., Pagano R.E.
J. Biol. Chem. 274:451-456(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF047707 mRNA. Translation: AAD02464.1.
AJ224156 mRNA. Translation: CAA11853.1.
RefSeqNP_113983.1. NM_031795.2.
UniGeneRn.24091.

3D structure databases

ProteinModelPortalQ9R0E0.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT21. Glycosyltransferase Family 21.

Proteomic databases

PaxDbQ9R0E0.
PRIDEQ9R0E0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000021110; ENSRNOP00000021110; ENSRNOG00000015644.
GeneID83626.
KEGGrno:83626.
UCSCRGD:621870. rat.

Organism-specific databases

CTD7357.
RGD621870. Ugcg.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeENSGT00390000012898.
HOGENOMHOG000039663.
HOVERGENHBG003997.
InParanoidQ9R0E0.
KOK00720.
OMALVWICDS.
OrthoDBEOG70KGPR.
PhylomeDBQ9R0E0.
TreeFamTF314564.

Enzyme and pathway databases

BRENDA2.4.1.80. 5301.
UniPathwayUPA00222.

Gene expression databases

GenevestigatorQ9R0E0.

Family and domain databases

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

Other

NextBio616199.
PROQ9R0E0.

Entry information

Entry nameCEGT_RAT
AccessionPrimary (citable) accession number: Q9R0E0
Secondary accession number(s): O55149
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 87 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