Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9R0E0

- CEGT_RAT

UniProt

Q9R0E0 - CEGT_RAT

Protein

Ceramide glucosyltransferase

Gene

Ugcg

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    GO - Biological processi

    1. sphingolipid metabolic process Source: UniProtKB-UniPathway

    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 1 Publication; Multi-pass membrane protein 1 Publication

    GO - Cellular componenti

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

    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 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

    GenevestigatoriQ9R0E0.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R0E0.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1010LumenalSequence Analysis
    Topological domaini33 – 195163CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini216 – 28772LumenalSequence AnalysisAdd
    BLAST
    Topological domaini305 – 3095CytoplasmicSequence Analysis
    Topological domaini329 – 34820LumenalSequence AnalysisAdd
    BLAST
    Topological domaini370 – 39425CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei11 – 3222HelicalSequence AnalysisAdd
    BLAST
    Transmembranei196 – 21520HelicalSequence AnalysisAdd
    BLAST
    Transmembranei288 – 30417HelicalSequence AnalysisAdd
    BLAST
    Transmembranei310 – 32819HelicalSequence AnalysisAdd
    BLAST
    Transmembranei349 – 36921HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated

    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

    « Hide

    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...
    MobiDBi 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: October 1, 2014
    This is version 90 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