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Q21054

- CGT3_CAEEL

UniProt

Q21054 - CGT3_CAEEL

Protein

Ceramide glucosyltransferase 3

Gene

cgt-3

Organism
Caenorhabditis elegans
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (01 Mar 2002)
      Previous versions | rss
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    Functioni

    Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. Seems to be the major active form in the nematode.1 Publication

    Catalytic activityi

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

    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.

    Protein family/group databases

    CAZyiGT21. Glycosyltransferase Family 21.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ceramide glucosyltransferase 3 (EC:2.4.1.80)
    Gene namesi
    Name:cgt-3
    ORF Names:F59G1.1
    OrganismiCaenorhabditis elegans
    Taxonomic identifieri6239 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
    ProteomesiUP000001940: Chromosome II

    Organism-specific databases

    WormBaseiF59G1.1a; CE29810; WBGene00019127; cgt-3.
    F59G1.1b; CE29811; WBGene00019127; cgt-3.
    F59G1.1c; CE30378; WBGene00019127; cgt-3.
    F59G1.1d; CE33409; WBGene00019127; cgt-3.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: WormBase

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Reduced brood size. Reduced glucosyl-ceramide content and expression at cell surface. Increased expression of sphingomyelins and sphingomyelin clustering at cell surface. Loss of function in the germline leads to defects in oocyte formation and early embryonic divisions and shortened body length. Loss of function in somatic cells may lead to L1 arrest.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 459459Ceramide glucosyltransferase 3PRO_0000421283Add
    BLAST

    Proteomic databases

    PaxDbiQ21054.
    PRIDEiQ21054.

    Interactioni

    Protein-protein interaction databases

    STRINGi6239.F59G1.1b.2.

    Structurei

    3D structure databases

    ProteinModelPortaliQ21054.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei77 – 9721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei367 – 38721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei415 – 43521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 2 family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1215.
    GeneTreeiENSGT00390000012898.
    HOGENOMiHOG000039663.
    KOiK00720.
    OMAiLVWICDS.

    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.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform a (identifier: Q21054-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MCKYGKSNLA AVASSTSSII GAAAAAVAEA QPSASPSTSS SFLLLEVPFR    50
    HLLRLQPPPY FIAGTRRMAA QLDVTTLIAI VGFVFVFCLY LIHIIALSYS 100
    KYRLHHKVKE DSSLPGVSII KPIVGKDNNL YENIESFFTT QYHKYELLFC 150
    FNSSDDEAVE VVKCLMKKYP KVDAKLFFGG ETVGLNPKIN NMMPAYRSAL 200
    YPLILVSDSG IFMRSDGVLD MATTMMSHEK MALVTQTPYC KDREGFDAAF 250
    EQMYFGTSHG RIYLAGNCMD FVCSTGMSSM MKKEALDECG GISNFGGYLA 300
    EDYFFGRELA NRGYKSAISS HPALQNSSSV SVSSFLDRIC RWVKLRIAML 350
    PHILLVEPLQ DCFPSGLIMA FSLNHLVGLN IMPILILHTI YWFSMDYSLM 400
    NSMQNGKLSF SPLQFMLIWL LRELTAPFVF IKALLQPTIQ WRNNVFHLAW 450
    GGQILPPKC 459
    Length:459
    Mass (Da):51,300
    Last modified:March 1, 2002 - v2
    Checksum:i55E8F89E0441281D
    GO
    Isoform b (identifier: Q21054-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-11: MCKYGKSNLAA → MEVAKAVATNLSTAANSTVLRT

    Show »
    Length:470
    Mass (Da):52,363
    Checksum:i9D7F5A8FD65763F6
    GO
    Isoform c (identifier: Q21054-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-11: MCKYGKSNLAA → MEVAKAVATNLSTAANSTVLRT
         361-368: DCFPSGLI → VIPKFTFF
         369-459: Missing.

    Show »
    Length:379
    Mass (Da):41,907
    Checksum:i820D79C95E28EBBD
    GO
    Isoform d (identifier: Q21054-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-67: Missing.

    Show »
    Length:392
    Mass (Da):44,354
    Checksum:iFB9AA9A5AE413426
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6767Missing in isoform d. 1 PublicationVSP_045383Add
    BLAST
    Alternative sequencei1 – 1111MCKYGKSNLAA → MEVAKAVATNLSTAANSTVL RT in isoform b and isoform c. 1 PublicationVSP_045384Add
    BLAST
    Alternative sequencei361 – 3688DCFPSGLI → VIPKFTFF in isoform c. 1 PublicationVSP_045385
    Alternative sequencei369 – 45991Missing in isoform c. 1 PublicationVSP_045386Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ178632 mRNA. Translation: ABD75711.1.
    DQ178633 mRNA. Translation: ABD75712.1.
    DQ178634 mRNA. Translation: ABD75713.1.
    FO081244 Genomic DNA. Translation: CCD70149.1.
    FO081244 Genomic DNA. Translation: CCD70150.1.
    FO081244 Genomic DNA. Translation: CCD70151.1.
    FO081244 Genomic DNA. Translation: CCD70152.1.
    RefSeqiNP_495181.2. NM_062780.5. [Q21054-2]
    NP_495182.2. NM_062781.4. [Q21054-1]
    NP_741005.1. NM_171006.4. [Q21054-3]
    NP_871996.1. NM_182196.3. [Q21054-4]
    UniGeneiCel.17849.
    Cel.33407.

    Genome annotation databases

    EnsemblMetazoaiF59G1.1a; F59G1.1a; WBGene00019127. [Q21054-1]
    GeneIDi174001.
    KEGGicel:CELE_F59G1.1.
    UCSCiF59G1.1b.1. c. elegans. [Q21054-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ178632 mRNA. Translation: ABD75711.1 .
    DQ178633 mRNA. Translation: ABD75712.1 .
    DQ178634 mRNA. Translation: ABD75713.1 .
    FO081244 Genomic DNA. Translation: CCD70149.1 .
    FO081244 Genomic DNA. Translation: CCD70150.1 .
    FO081244 Genomic DNA. Translation: CCD70151.1 .
    FO081244 Genomic DNA. Translation: CCD70152.1 .
    RefSeqi NP_495181.2. NM_062780.5. [Q21054-2 ]
    NP_495182.2. NM_062781.4. [Q21054-1 ]
    NP_741005.1. NM_171006.4. [Q21054-3 ]
    NP_871996.1. NM_182196.3. [Q21054-4 ]
    UniGenei Cel.17849.
    Cel.33407.

    3D structure databases

    ProteinModelPortali Q21054.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6239.F59G1.1b.2.

    Protein family/group databases

    CAZyi GT21. Glycosyltransferase Family 21.

    Proteomic databases

    PaxDbi Q21054.
    PRIDEi Q21054.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai F59G1.1a ; F59G1.1a ; WBGene00019127 . [Q21054-1 ]
    GeneIDi 174001.
    KEGGi cel:CELE_F59G1.1.
    UCSCi F59G1.1b.1. c. elegans. [Q21054-1 ]

    Organism-specific databases

    CTDi 174001.
    WormBasei F59G1.1a ; CE29810 ; WBGene00019127 ; cgt-3.
    F59G1.1b ; CE29811 ; WBGene00019127 ; cgt-3.
    F59G1.1c ; CE30378 ; WBGene00019127 ; cgt-3.
    F59G1.1d ; CE33409 ; WBGene00019127 ; cgt-3.

    Phylogenomic databases

    eggNOGi COG1215.
    GeneTreei ENSGT00390000012898.
    HOGENOMi HOG000039663.
    KOi K00720.
    OMAi LVWICDS.

    Enzyme and pathway databases

    UniPathwayi UPA00222 .
    Reactomei REACT_197713. Glycosphingolipid metabolism.

    Miscellaneous databases

    NextBioi 882053.

    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. "The frataxin-encoding operon of Caenorhabditis elegans shows complex structure and regulation."
      Vazquez-Manrique R.P., Gonzalez-Cabo P., Ortiz-Martin I., Ros S., Baylis H.A., Palau F.
      Genomics 89:392-401(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C AND D).
      Strain: Bristol N2.
    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], ALTERNATIVE SPLICING.
      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 nameiCGT3_CAEEL
    AccessioniPrimary (citable) accession number: Q21054
    Secondary accession number(s): G5EET1, G5EGR9, Q8T3D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 6, 2013
    Last sequence update: March 1, 2002
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 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