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Q9R0E0

- CEGT_RAT

UniProt

Q9R0E0 - CEGT_RAT

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Protein
Ceramide glucosyltransferase
Gene
Ugcg
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei193 – 1931May play an important role in binding to the inhibitors DEPC and PDMP

GO - Molecular functioni

  1. ceramide glucosyltransferase activity Source: RGD
Complete GO annotation...

GO - Biological processi

  1. sphingolipid metabolic process Source: UniProtKB-UniPathway
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.
ReactomeiREACT_198596. Glycosphingolipid metabolism.
UniPathwayiUPA00222.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

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
ProteomesiUP000002494: Chromosome 5

Organism-specific databases

RGDi621870. Ugcg.

Subcellular locationi

Golgi apparatus membrane; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010Lumenal Reviewed prediction
Transmembranei11 – 3222Helical; Reviewed prediction
Add
BLAST
Topological domaini33 – 195163Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei196 – 21520Helical; Reviewed prediction
Add
BLAST
Topological domaini216 – 28772Lumenal Reviewed prediction
Add
BLAST
Transmembranei288 – 30417Helical; Reviewed prediction
Add
BLAST
Topological domaini305 – 3095Cytoplasmic Reviewed prediction
Transmembranei310 – 32819Helical; Reviewed prediction
Add
BLAST
Topological domaini329 – 34820Lumenal Reviewed prediction
Add
BLAST
Transmembranei349 – 36921Helical; Reviewed prediction
Add
BLAST
Topological domaini370 – 39425Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
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
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
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 glucosyltransferase
PRO_0000059178Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9R0E0.
PRIDEiQ9R0E0.

Expressioni

Gene expression databases

GenevestigatoriQ9R0E0.

Structurei

3D structure databases

ProteinModelPortaliQ9R0E0.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
HOVERGENiHBG003997.
InParanoidiQ9R0E0.
KOiK00720.
OMAiLVWICDS.
OrthoDBiEOG70KGPR.
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

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MALLDLAQEG MALFGFVLFV VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL    50
PGVSLLKPLK GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIEVCKK 100
LLGKYPNVDA RLFIGGKKVG INPKINNLMP AYEVAKYDLI WICDSGIRVI 150
PDTLTDMVNQ MTERVGLVHG LPYVADRQGF AATLEQVYFG TSHPRSYISA 200
NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA KAIADRGWKF 250
SMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS 300
LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA 350
VAWFIRESMT IYIFLSALWD PTISWRAGRY RLRCGGTAEE ILDV 394
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:
EMBL
GenBank
DDBJ
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.
GeneIDi83626.
KEGGirno:83626.
UCSCiRGD:621870. rat.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF047707 mRNA. Translation: AAD02464.1 .
AJ224156 mRNA. Translation: CAA11853.1 .
RefSeqi NP_113983.1. NM_031795.2.
UniGenei Rn.24091.

3D structure databases

ProteinModelPortali Q9R0E0.
ModBasei Search...

Protein family/group databases

CAZyi GT21. Glycosyltransferase Family 21.

Proteomic databases

PaxDbi Q9R0E0.
PRIDEi Q9R0E0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000021110 ; ENSRNOP00000021110 ; ENSRNOG00000015644 .
GeneIDi 83626.
KEGGi rno:83626.
UCSCi RGD:621870. rat.

Organism-specific databases

CTDi 7357.
RGDi 621870. Ugcg.

Phylogenomic databases

eggNOGi COG1215.
GeneTreei ENSGT00390000012898.
HOGENOMi HOG000039663.
HOVERGENi HBG003997.
InParanoidi Q9R0E0.
KOi K00720.
OMAi LVWICDS.
OrthoDBi EOG70KGPR.
PhylomeDBi Q9R0E0.
TreeFami TF314564.

Enzyme and pathway databases

UniPathwayi UPA00222 .
BRENDAi 2.4.1.80. 5301.
Reactomei REACT_198596. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi 616199.
PROi Q9R0E0.

Gene expression databases

Genevestigatori Q9R0E0.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF13506. Glyco_transf_21. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

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 3, 2014
This is version 89 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

External Data

Dasty 3

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