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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)LengthDescriptionGraphical viewFeature identifierActions
Sitei193 – 1931May play an important role in binding to the inhibitors DEPC and PDMP
Active sitei236 – 2361Proton acceptor1 Publication

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

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)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010LumenalSequence analysis
Transmembranei11 – 3222HelicalSequence analysisAdd
BLAST
Topological domaini33 – 195163CytoplasmicSequence analysisAdd
BLAST
Transmembranei196 – 21520HelicalSequence analysisAdd
BLAST
Topological domaini216 – 28772LumenalSequence analysisAdd
BLAST
Transmembranei288 – 30417HelicalSequence analysisAdd
BLAST
Topological domaini305 – 3095CytoplasmicSequence analysis
Transmembranei310 – 32819HelicalSequence analysisAdd
BLAST
Topological domaini329 – 34820LumenalSequence analysisAdd
BLAST
Transmembranei349 – 36921HelicalSequence analysisAdd
BLAST
Topological domaini370 – 39425CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261H → A: Inhibits activity to less than 6%. 1 Publication
Mutagenesisi26 – 261H → D: Inhibits activity to about 10%. 1 Publication
Mutagenesisi26 – 261H → N: Inhibits activity to about 50%. 1 Publication
Mutagenesisi26 – 261H → R: No effect on activity. Decreased sensitivity to the inhibitor PDMP. 1 Publication
Mutagenesisi36 – 361H → A: No effect on activity. 1 Publication
Mutagenesisi90 – 901H → A: No effect on activity. 1 Publication
Mutagenesisi92 – 921D → A: Inhibits activity to about 20%. 1 Publication
Mutagenesisi124 – 1241K → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi144 – 1441D → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi169 – 1691H → A: Inhibits activity to about 30%. Decreased sensitivity to PDMP. 1 Publication
Mutagenesisi193 – 1931H → A: Inhibits activity to about 30%. Insensitive to the inhibitors DEPC and PDMP. 1 Publication
Mutagenesisi193 – 1931H → D: Abolishes activity. 1 Publication
Mutagenesisi193 – 1931H → N: Inhibits activity to about 20%. Insensitive to the inhibitors DEPC and PDMP. 1 Publication
Mutagenesisi193 – 1931H → R: Abolishes activity. 1 Publication
Mutagenesisi224 – 2241G → I: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi225 – 2251G → I: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi235 – 2351E → A: Inhibits activity to less than 1.5%. 1 Publication
Mutagenesisi236 – 2361D → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi247 – 2471G → I: Leads to near complete loss of activity. 1 Publication
Mutagenesisi272 – 2721R → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi275 – 2751R → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi276 – 2761W → A: Completely abolishes catalytic activity. 1 Publication
Mutagenesisi308 – 3092HH → AA: Inhibits activity to about 10%. 1 Publication
Mutagenesisi308 – 3081H → A: Inhibits activity to about 35%. 1 Publication
Mutagenesisi309 – 3091H → A: Inhibits activity to about 70%. 1 Publication
Mutagenesisi322 – 3221H → A: Inhibits activity to less than 6%. 1 Publication
Mutagenesisi322 – 3221H → D: Inhibits activity to less than 6%. 1 Publication
Mutagenesisi322 – 3221H → N: Inhibits activity to about 50%. 1 Publication
Mutagenesisi322 – 3221H → R: Abolishes activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Ceramide glucosyltransferasePRO_0000059178Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei117 – 1171N6-acetyllysineBy similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Motifi92 – 921D1Curated
Motifi144 – 1441D2Curated
Motifi236 – 2361D3Curated
Motifi272 – 2765(Q/R)XXRWCurated

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81Q → L in strain: Wistar.
Natural varianti89 – 891D → G in strain: Wistar.
Natural varianti153 – 1531T → S in strain: Wistar.
Natural varianti179 – 1791G → A in strain: Wistar.
Natural varianti387 – 3871T → I in strain: Wistar.

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

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: September 7, 2016
This is version 104 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.