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G5EC84

- CGT2_CAEEL

UniProt

G5EC84 - CGT2_CAEEL

Protein

Ceramide glucosyltransferase 2

Gene

cgt-2

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 23 (01 Oct 2014)
      Sequence version 1 (14 Dec 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide.2 Publications

    Catalytic activityi

    UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. ceramide glucosyltransferase activity Source: UniProtKB-EC

    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

    ReactomeiREACT_197713. Glycosphingolipid metabolism.
    UniPathwayiUPA00222.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ceramide glucosyltransferase 2 (EC:2.4.1.80)
    Gene namesi
    Name:cgt-2
    ORF Names:F20B4.6
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome X

    Organism-specific databases

    WormBaseiF20B4.6; CE30960; WBGene00017625; cgt-2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Reduced brood size.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Ceramide glucosyltransferase 2PRO_0000421282Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliG5EC84.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei60 – 8021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei336 – 35621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei398 – 41821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00390000012898.
    OMAiSHETMAL.
    OrthoDBiEOG70KGPR.
    PhylomeDBiG5EC84.

    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.

    G5EC84-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGDKITGLEV EIIPEISEVQ PESLQEQNAS SLYYPLFSQY IPLLLTGTKK    50
    ILEDIDYCTC FAVFGVVFVS ALYFLHIVGL CYGKYRLHRP TKPNPSLPGV 100
    SIIKPIIGAD ANLYTNLETF FTTQYHKFEL LFCFDRSDDP AVKVVESLVK 150
    KYPSVDSTMF FGGEKIGLNP KINNMMPAYR IAKYQLIMIS DSGIFMKSDA 200
    VLDMASTMMS HETMALVTQT PYCKDRKGFA SVFEQIYFGT SHARIYLAGN 250
    CLQFNCPTGM SSMMKKEALD ECGGFAAFSG YLAEDYFFGK KLASRGYKSG 300
    ISTHPALQNS AAVTMTSFTD RVCRWVKLRM AMMPQIIFVE PLQDCFPSAL 350
    IISFSLNYIA NIDMLTTIML HVVFWITMDC MVMCKMQNKK MSFSPLKFLL 400
    IWLLRELFAP LVFIKAALDP SIRWRDNVFH LAWGGKIRSQ TSI 443
    Length:443
    Mass (Da):50,121
    Last modified:December 14, 2011 - v1
    Checksum:i2690419210CA6C93
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF364401 mRNA. Translation: AAK73018.1.
    FO081185 Genomic DNA. Translation: CCD69753.1.
    PIRiT28827.
    RefSeqiNP_510857.2. NM_078456.4.
    UniGeneiCel.19350.

    Genome annotation databases

    EnsemblMetazoaiF20B4.6; F20B4.6; WBGene00017625.
    GeneIDi181790.
    KEGGicel:CELE_F20B4.6.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF364401 mRNA. Translation: AAK73018.1 .
    FO081185 Genomic DNA. Translation: CCD69753.1 .
    PIRi T28827.
    RefSeqi NP_510857.2. NM_078456.4.
    UniGenei Cel.19350.

    3D structure databases

    ProteinModelPortali G5EC84.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai F20B4.6 ; F20B4.6 ; WBGene00017625 .
    GeneIDi 181790.
    KEGGi cel:CELE_F20B4.6.

    Organism-specific databases

    CTDi 181790.
    WormBasei F20B4.6 ; CE30960 ; WBGene00017625 ; cgt-2.

    Phylogenomic databases

    GeneTreei ENSGT00390000012898.
    OMAi SHETMAL.
    OrthoDBi EOG70KGPR.
    PhylomeDBi G5EC84.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    Reactomei REACT_197713. Glycosphingolipid metabolism.

    Miscellaneous databases

    NextBioi 915358.

    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. "Glucosylceramide synthases, a gene family responsible for the biosynthesis of glucosphingolipids in animals, plants, and fungi."
      Leipelt M., Warnecke D., Zahringer U., Ott C., Muller F., Hube B., Heinz E.
      J. Biol. Chem. 276:33621-33629(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
    2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
      The C. elegans sequencing consortium
      Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Bristol N2.
    3. "Ceramide glucosyltransferase of the nematode Caenorhabditis elegans is involved in oocyte formation and in early embryonic cell division."
      Nomura K.H., Murata D., Hayashi Y., Dejima K., Mizuguchi S., Kage-Nakadai E., Gengyo-Ando K., Mitani S., Hirabayashi Y., Ito M., Nomura K.
      Glycobiology 21:834-848(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiCGT2_CAEEL
    AccessioniPrimary (citable) accession number: G5EC84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2013
    Last sequence update: December 14, 2011
    Last modified: October 1, 2014
    This is version 23 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programCaenorhabditis annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Caenorhabditis elegans
      Caenorhabditis elegans: entries, gene names and cross-references to WormBase
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3