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Protein

Ceramide glucosyltransferase 2

Gene

cgt-2

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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: GO_Central

GO - Biological processi

  1. glucosylceramide biosynthetic process Source: GO_Central
Complete GO annotation...

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

Topology

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

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane Source: GO_Central
Complete GO annotation...

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...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000012898.
InParanoidiG5EC84.
OMAiFRECISI.
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

        10         20         30         40         50
MGDKITGLEV EIIPEISEVQ PESLQEQNAS SLYYPLFSQY IPLLLTGTKK
60 70 80 90 100
ILEDIDYCTC FAVFGVVFVS ALYFLHIVGL CYGKYRLHRP TKPNPSLPGV
110 120 130 140 150
SIIKPIIGAD ANLYTNLETF FTTQYHKFEL LFCFDRSDDP AVKVVESLVK
160 170 180 190 200
KYPSVDSTMF FGGEKIGLNP KINNMMPAYR IAKYQLIMIS DSGIFMKSDA
210 220 230 240 250
VLDMASTMMS HETMALVTQT PYCKDRKGFA SVFEQIYFGT SHARIYLAGN
260 270 280 290 300
CLQFNCPTGM SSMMKKEALD ECGGFAAFSG YLAEDYFFGK KLASRGYKSG
310 320 330 340 350
ISTHPALQNS AAVTMTSFTD RVCRWVKLRM AMMPQIIFVE PLQDCFPSAL
360 370 380 390 400
IISFSLNYIA NIDMLTTIML HVVFWITMDC MVMCKMQNKK MSFSPLKFLL
410 420 430 440
IWLLRELFAP LVFIKAALDP SIRWRDNVFH LAWGGKIRSQ TSI
Length:443
Mass (Da):50,121
Last modified:December 14, 2011 - v1
Checksum:i2690419210CA6C93
GO

Sequence databases

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

3D structure databases

ProteinModelPortaliG5EC84.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi181790.
WormBaseiF20B4.6; CE30960; WBGene00017625; cgt-2.

Phylogenomic databases

GeneTreeiENSGT00390000012898.
InParanoidiG5EC84.
OMAiFRECISI.
OrthoDBiEOG70KGPR.
PhylomeDBiG5EC84.

Enzyme and pathway databases

UniPathwayiUPA00222.
ReactomeiREACT_197713. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi915358.

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...

Publicationsi

« Hide 'large scale' publications
  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: February 4, 2015
This is version 26 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

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 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.