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Q21054 (CGT3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ceramide glucosyltransferase 3

EC=2.4.1.80
Gene names
Name:cgt-3
ORF Names:F59G1.1
OrganismCaenorhabditis elegans [Reference proteome]
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length459 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. Seems to be the major active form in the nematode. Ref.3

Catalytic activity

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

Pathway

Lipid metabolism; sphingolipid metabolism. Ref.3

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Disruption phenotype

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. Ref.3

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Sphingolipid metabolism
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   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

plasma membrane

Inferred from direct assay Ref.3. Source: WormBase

   Molecular_functionceramide glucosyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform a (identifier: Q21054-1)

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.
Isoform b (identifier: Q21054-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MCKYGKSNLAA → MEVAKAVATNLSTAANSTVLRT
Isoform c (identifier: Q21054-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: MCKYGKSNLAA → MEVAKAVATNLSTAANSTVLRT
     361-368: DCFPSGLI → VIPKFTFF
     369-459: Missing.
Isoform d (identifier: Q21054-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 459459Ceramide glucosyltransferase 3
PRO_0000421283

Regions

Transmembrane77 – 9721Helical; Potential
Transmembrane367 – 38721Helical; Potential
Transmembrane415 – 43521Helical; Potential

Natural variations

Alternative sequence1 – 6767Missing in isoform d.
VSP_045383
Alternative sequence1 – 1111MCKYGKSNLAA → MEVAKAVATNLSTAANSTVL RT in isoform b and isoform c.
VSP_045384
Alternative sequence361 – 3688DCFPSGLI → VIPKFTFF in isoform c.
VSP_045385
Alternative sequence369 – 45991Missing in isoform c.
VSP_045386

Sequences

Sequence LengthMass (Da)Tools
Isoform a [UniParc].

Last modified March 1, 2002. Version 2.
Checksum: 55E8F89E0441281D

FASTA45951,300
        10         20         30         40         50         60 
MCKYGKSNLA AVASSTSSII GAAAAAVAEA QPSASPSTSS SFLLLEVPFR HLLRLQPPPY 

        70         80         90        100        110        120 
FIAGTRRMAA QLDVTTLIAI VGFVFVFCLY LIHIIALSYS KYRLHHKVKE DSSLPGVSII 

       130        140        150        160        170        180 
KPIVGKDNNL YENIESFFTT QYHKYELLFC FNSSDDEAVE VVKCLMKKYP KVDAKLFFGG 

       190        200        210        220        230        240 
ETVGLNPKIN NMMPAYRSAL YPLILVSDSG IFMRSDGVLD MATTMMSHEK MALVTQTPYC 

       250        260        270        280        290        300 
KDREGFDAAF EQMYFGTSHG RIYLAGNCMD FVCSTGMSSM MKKEALDECG GISNFGGYLA 

       310        320        330        340        350        360 
EDYFFGRELA NRGYKSAISS HPALQNSSSV SVSSFLDRIC RWVKLRIAML PHILLVEPLQ 

       370        380        390        400        410        420 
DCFPSGLIMA FSLNHLVGLN IMPILILHTI YWFSMDYSLM NSMQNGKLSF SPLQFMLIWL 

       430        440        450 
LRELTAPFVF IKALLQPTIQ WRNNVFHLAW GGQILPPKC 

« Hide

Isoform b [UniParc].

Checksum: 9D7F5A8FD65763F6
Show »

FASTA47052,363
Isoform c [UniParc].

Checksum: 820D79C95E28EBBD
Show »

FASTA37941,907
Isoform d [UniParc].

Checksum: FB9AA9A5AE413426
Show »

FASTA39244,354

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_495181.2. NM_062780.5.
NP_495182.2. NM_062781.4.
NP_741005.1. NM_171006.4.
NP_871996.1. NM_182196.3.
UniGeneCel.17849.
Cel.33407.

3D structure databases

ProteinModelPortalQ21054.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING6239.F59G1.1b.2.

Protein family/group databases

CAZyGT21. Glycosyltransferase Family 21.

Proteomic databases

PaxDbQ21054.
PRIDEQ21054.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF59G1.1a; F59G1.1a; F59G1.1. [Q21054-1]
F59G1.1b.1; F59G1.1b.1; F59G1.1. [Q21054-2]
F59G1.1b.2; F59G1.1b.2; F59G1.1. [Q21054-2]
F59G1.1c.1; F59G1.1c.1; F59G1.1. [Q21054-3]
F59G1.1c.2; F59G1.1c.2; F59G1.1. [Q21054-3]
F59G1.1d.1; F59G1.1d.1; F59G1.1. [Q21054-4]
F59G1.1d.2; F59G1.1d.2; F59G1.1. [Q21054-4]
F59G1.1d.3; F59G1.1d.3; F59G1.1. [Q21054-4]
F59G1.1d.4; F59G1.1d.4; F59G1.1. [Q21054-4]
F59G1.1d.5; F59G1.1d.5; F59G1.1. [Q21054-4]
GeneID174001.
KEGGcel:CELE_F59G1.1.
UCSCF59G1.1b.1. c. elegans. [Q21054-1]

Organism-specific databases

CTD174001.
WormBaseF59G1.1a; CE29810; WBGene00019127; cgt-3.
F59G1.1b; CE29811; WBGene00019127; cgt-3.
F59G1.1c; CE30378; WBGene00019127; cgt-3.
F59G1.1d; CE33409; WBGene00019127; cgt-3.

Phylogenomic databases

eggNOGCOG1215.
HOGENOMHOG000039663.
KOK00720.
OMALVWICDS.

Enzyme and pathway databases

UniPathwayUPA00222.

Family and domain databases

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

Other

NextBio882053.

Entry information

Entry nameCGT3_CAEEL
AccessionPrimary (citable) accession number: Q21054
Secondary accession number(s): G5EET1, G5EGR9, Q8T3D8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 85 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