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Protein

Ceramide glucosyltransferase

Gene

Ugcg

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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".1 Publication

Catalytic activityi

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

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei193May play an important role in binding to the inhibitors DEPC and PDMP1
Active sitei236Proton acceptor1 Publication1

GO - Molecular functioni

  • ceramide glucosyltransferase activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BRENDAi2.4.1.80. 5301.
ReactomeiR-RNO-1660662. Glycosphingolipid metabolism.
UniPathwayiUPA00222.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

Chemistry databases

SwissLipidsiSLP:000000912.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Ugcg
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi621870. Ugcg.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10LumenalSequence analysis10
Transmembranei11 – 32HelicalSequence analysisAdd BLAST22
Topological domaini33 – 195CytoplasmicSequence analysisAdd BLAST163
Transmembranei196 – 215HelicalSequence analysisAdd BLAST20
Topological domaini216 – 287LumenalSequence analysisAdd BLAST72
Transmembranei288 – 304HelicalSequence analysisAdd BLAST17
Topological domaini305 – 309CytoplasmicSequence analysis5
Transmembranei310 – 328HelicalSequence analysisAdd BLAST19
Topological domaini329 – 348LumenalSequence analysisAdd BLAST20
Transmembranei349 – 369HelicalSequence analysisAdd BLAST21
Topological domaini370 – 394CytoplasmicSequence analysisAdd BLAST25

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi26H → A: Inhibits activity to less than 6%. 1 Publication1
Mutagenesisi26H → D: Inhibits activity to about 10%. 1 Publication1
Mutagenesisi26H → N: Inhibits activity to about 50%. 1 Publication1
Mutagenesisi26H → R: No effect on activity. Decreased sensitivity to the inhibitor PDMP. 1 Publication1
Mutagenesisi36H → A: No effect on activity. 1 Publication1
Mutagenesisi90H → A: No effect on activity. 1 Publication1
Mutagenesisi92D → A: Inhibits activity to about 20%. 1 Publication1
Mutagenesisi124K → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi144D → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi169H → A: Inhibits activity to about 30%. Decreased sensitivity to PDMP. 1 Publication1
Mutagenesisi193H → A: Inhibits activity to about 30%. Insensitive to the inhibitors DEPC and PDMP. 1 Publication1
Mutagenesisi193H → D: Abolishes activity. 1 Publication1
Mutagenesisi193H → N: Inhibits activity to about 20%. Insensitive to the inhibitors DEPC and PDMP. 1 Publication1
Mutagenesisi193H → R: Abolishes activity. 1 Publication1
Mutagenesisi224G → I: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi225G → I: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi235E → A: Inhibits activity to less than 1.5%. 1 Publication1
Mutagenesisi236D → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi247G → I: Leads to near complete loss of activity. 1 Publication1
Mutagenesisi272R → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi275R → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi276W → A: Completely abolishes catalytic activity. 1 Publication1
Mutagenesisi308 – 309HH → AA: Inhibits activity to about 10%. 1 Publication2
Mutagenesisi308H → A: Inhibits activity to about 35%. 1 Publication1
Mutagenesisi309H → A: Inhibits activity to about 70%. 1 Publication1
Mutagenesisi322H → A: Inhibits activity to less than 6%. 1 Publication1
Mutagenesisi322H → D: Inhibits activity to less than 6%. 1 Publication1
Mutagenesisi322H → N: Inhibits activity to about 50%. 1 Publication1
Mutagenesisi322H → R: Abolishes activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591781 – 394Ceramide glucosyltransferaseAdd BLAST394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei117N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9R0E0.
PRIDEiQ9R0E0.

Expressioni

Gene expression databases

BgeeiENSRNOG00000015644.
GenevisibleiQ9R0E0. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021110.

Structurei

3D structure databases

ProteinModelPortaliQ9R0E0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi92D1Curated1
Motifi144D2Curated1
Motifi236D3Curated1
Motifi272 – 276(Q/R)XXRWCurated5

Domaini

The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS active site, involved in catalysis and UDP-sugar binding.1 Publication

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2547. Eukaryota.
COG1215. LUCA.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
HOVERGENiHBG003997.
InParanoidiQ9R0E0.
KOiK00720.
OMAiLETFFTM.
OrthoDBiEOG091G0G3M.
PhylomeDBiQ9R0E0.
TreeFamiTF314564.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9R0E0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALLDLAQEG MALFGFVLFV VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL
60 70 80 90 100
PGVSLLKPLK GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIEVCKK
110 120 130 140 150
LLGKYPNVDA RLFIGGKKVG INPKINNLMP AYEVAKYDLI WICDSGIRVI
160 170 180 190 200
PDTLTDMVNQ MTERVGLVHG LPYVADRQGF AATLEQVYFG TSHPRSYISA
210 220 230 240 250
NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA KAIADRGWKF
260 270 280 290 300
SMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS
310 320 330 340 350
LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA
360 370 380 390
VAWFIRESMT IYIFLSALWD PTISWRAGRY RLRCGGTAEE ILDV
Length:394
Mass (Da):44,823
Last modified:May 1, 2000 - v1
Checksum:i214581C0B8D9152C
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti8Q → L in strain: Wistar. 1
Natural varianti89D → G in strain: Wistar. 1
Natural varianti153T → S in strain: Wistar. 1
Natural varianti179G → A in strain: Wistar. 1
Natural varianti387T → I in strain: Wistar. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047707 mRNA. Translation: AAD02464.1.
AJ224156 mRNA. Translation: CAA11853.1.
RefSeqiNP_113983.1. NM_031795.2.
UniGeneiRn.24091.

Genome annotation databases

EnsembliENSRNOT00000021110; ENSRNOP00000021110; ENSRNOG00000015644.
ENSRNOT00000088872; ENSRNOP00000075148; ENSRNOG00000015644.
GeneIDi83626.
KEGGirno:83626.
UCSCiRGD:621870. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF047707 mRNA. Translation: AAD02464.1.
AJ224156 mRNA. Translation: CAA11853.1.
RefSeqiNP_113983.1. NM_031795.2.
UniGeneiRn.24091.

3D structure databases

ProteinModelPortaliQ9R0E0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021110.

Chemistry databases

SwissLipidsiSLP:000000912.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

Proteomic databases

PaxDbiQ9R0E0.
PRIDEiQ9R0E0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021110; ENSRNOP00000021110; ENSRNOG00000015644.
ENSRNOT00000088872; ENSRNOP00000075148; ENSRNOG00000015644.
GeneIDi83626.
KEGGirno:83626.
UCSCiRGD:621870. rat.

Organism-specific databases

CTDi7357.
RGDi621870. Ugcg.

Phylogenomic databases

eggNOGiKOG2547. Eukaryota.
COG1215. LUCA.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
HOVERGENiHBG003997.
InParanoidiQ9R0E0.
KOiK00720.
OMAiLETFFTM.
OrthoDBiEOG091G0G3M.
PhylomeDBiQ9R0E0.
TreeFamiTF314564.

Enzyme and pathway databases

UniPathwayiUPA00222.
BRENDAi2.4.1.80. 5301.
ReactomeiR-RNO-1660662. Glycosphingolipid metabolism.

Miscellaneous databases

PROiQ9R0E0.

Gene expression databases

BgeeiENSRNOG00000015644.
GenevisibleiQ9R0E0. RN.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCEGT_RAT
AccessioniPrimary (citable) accession number: Q9R0E0
Secondary accession number(s): O55149
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 1, 2000
Last modified: November 2, 2016
This is version 105 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.