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O18037 (CGT1_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 79. 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 1

EC=2.4.1.80
Gene names
Name:cgt-1
ORF Names:T06C12.10
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length466 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.2

Catalytic activity

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

Pathway

Lipid metabolism; sphingolipid metabolism. Ref.2

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Disruption phenotype

Reduced brood size. Ref.2

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 – 466466Ceramide glucosyltransferase 1
PRO_0000421281

Regions

Transmembrane70 – 9021Helical; Potential
Transmembrane354 – 37421Helical; Potential
Transmembrane403 – 42321Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
O18037 [UniParc].

Last modified March 1, 2003. Version 2.
Checksum: EBC36C0EF42C5831

FASTA46652,416
        10         20         30         40         50         60 
MEAANEVVNL FASQATTPSS LDAVTTLETV STPTFIFPEV SDSQILQLMP ATLYSGMNWL 

        70         80         90        100        110        120 
RDHLDGFSLL ALSGCIFVSV LYLVHIIAFF YSIYRLHHKV EPDPTLPGVS VIKPIVGTDK 

       130        140        150        160        170        180 
NLYQNLESFF TSQYHSFELL FCFHSEEDEA IEVVRSLIKK HPNIEAKILF EGEPVGMNPK 

       190        200        210        220        230        240 
VNNMMPAYRA ARYPLVLISD SAIFMRPDGI LDMATTMMSH EKMASVTQIP YCKDRQGFHA 

       250        260        270        280        290        300 
AFEQIFFGTS HARLYLVGNF LGVVCSSGMS SMMKKSALDE CGGMEKFGEY LAEDYFFAKA 

       310        320        330        340        350        360 
LTSRGCKAAI STHPALQNSA SVTVLSFFNR IGRWIKLRIA MMPHLMVVEP LQDCVTSGLI 

       370        380        390        400        410        420 
MAFGLNYLGG YSVYKTFGLH LFYWIVMDFS LMTSMQNGKF NFTPFLFVFI WLFREFTSPF 

       430        440        450        460 
IFIKAVLAPT IVWRNNKFKL SWGGRIRTSK NSQKVPEAVS LSKGAV 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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
Z81116 Genomic DNA. Translation: CAB03296.2.
PIRT24561.
RefSeqNP_506971.2. NM_074570.4.
UniGeneCel.23835.

3D structure databases

ProteinModelPortalO18037.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.T06C12.10.2.

Protein family/group databases

CAZyGT21. Glycosyltransferase Family 21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaT06C12.10; T06C12.10; WBGene00011517.
GeneID188169.
KEGGcel:CELE_T06C12.10.
UCSCT06C12.10.1. c. elegans.

Organism-specific databases

CTD188169.
WormBaseT06C12.10; CE31986; WBGene00011517; cgt-1.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeENSGT00390000012898.
HOGENOMHOG000039663.
InParanoidO18037.
OMAEILFCAR.
PhylomeDBO18037.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
SUPFAMSSF53448. SSF53448. 1 hit.
ProtoNetSearch...

Other

NextBio937850.

Entry information

Entry nameCGT1_CAEEL
AccessionPrimary (citable) accession number: O18037
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 79 of the entry and version 2 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