Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

G5EC84 (CGT2_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ceramide glucosyltransferase 2

EC=2.4.1.80
Gene names
Name:cgt-2
ORF Names:F20B4.6
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length443 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. Ref.1 Ref.3

Catalytic activity

UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. Ref.1 Ref.3

Pathway

Lipid metabolism; sphingolipid metabolism. Ref.1 Ref.3

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Disruption phenotype

Reduced brood size. Ref.3

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Sphingolipid metabolism
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processsphingolipid metabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionceramide glucosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 443443Ceramide glucosyltransferase 2
PRO_0000421282

Regions

Transmembrane60 – 8021Helical; Potential
Transmembrane336 – 35621Helical; Potential
Transmembrane398 – 41821Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
G5EC84 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: 2690419210CA6C93

FASTA44350,121
        10         20         30         40         50         60 
MGDKITGLEV EIIPEISEVQ PESLQEQNAS SLYYPLFSQY IPLLLTGTKK ILEDIDYCTC 

        70         80         90        100        110        120 
FAVFGVVFVS ALYFLHIVGL CYGKYRLHRP TKPNPSLPGV SIIKPIIGAD ANLYTNLETF 

       130        140        150        160        170        180 
FTTQYHKFEL LFCFDRSDDP AVKVVESLVK KYPSVDSTMF FGGEKIGLNP KINNMMPAYR 

       190        200        210        220        230        240 
IAKYQLIMIS DSGIFMKSDA VLDMASTMMS HETMALVTQT PYCKDRKGFA SVFEQIYFGT 

       250        260        270        280        290        300 
SHARIYLAGN CLQFNCPTGM SSMMKKEALD ECGGFAAFSG YLAEDYFFGK KLASRGYKSG 

       310        320        330        340        350        360 
ISTHPALQNS AAVTMTSFTD RVCRWVKLRM AMMPQIIFVE PLQDCFPSAL IISFSLNYIA 

       370        380        390        400        410        420 
NIDMLTTIML HVVFWITMDC MVMCKMQNKK MSFSPLKFLL IWLLRELFAP LVFIKAALDP 

       430        440 
SIRWRDNVFH LAWGGKIRSQ TSI 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF364401 mRNA. Translation: AAK73018.1.
FO081185 Genomic DNA. Translation: CCD69753.1.
PIRT28827.
RefSeqNP_510857.2. NM_078456.4.
UniGeneCel.19350.

3D structure databases

ProteinModelPortalG5EC84.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF20B4.6; F20B4.6; F20B4.6.
GeneID181790.
KEGGcel:CELE_F20B4.6.

Organism-specific databases

CTD181790.
WormBaseF20B4.6; CE30960; WBGene00017625; cgt-2.

Phylogenomic databases

OMASHETMAL.
OrthoDBEOG70KGPR.
PhylomeDBG5EC84.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

InterProIPR025993. Ceramide_glucosylTrfase.
[Graphical view]
PfamPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio915358.

Entry information

Entry nameCGT2_CAEEL
AccessionPrimary (citable) accession number: G5EC84
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: December 14, 2011
Last modified: April 16, 2014
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormBase