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Protein

Ceramide glucosyltransferase 3

Gene

cgt-3

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Pathway: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

ReactomeiREACT_310934. 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 Componenti: 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

Topology

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

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: WormBase
Complete GO annotation...

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...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
InParanoidiQ21054.
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. AlignAdd to basket

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

        10         20         30         40         50
MCKYGKSNLA AVASSTSSII GAAAAAVAEA QPSASPSTSS SFLLLEVPFR
60 70 80 90 100
HLLRLQPPPY FIAGTRRMAA QLDVTTLIAI VGFVFVFCLY LIHIIALSYS
110 120 130 140 150
KYRLHHKVKE DSSLPGVSII KPIVGKDNNL YENIESFFTT QYHKYELLFC
160 170 180 190 200
FNSSDDEAVE VVKCLMKKYP KVDAKLFFGG ETVGLNPKIN NMMPAYRSAL
210 220 230 240 250
YPLILVSDSG IFMRSDGVLD MATTMMSHEK MALVTQTPYC KDREGFDAAF
260 270 280 290 300
EQMYFGTSHG RIYLAGNCMD FVCSTGMSSM MKKEALDECG GISNFGGYLA
310 320 330 340 350
EDYFFGRELA NRGYKSAISS HPALQNSSSV SVSSFLDRIC RWVKLRIAML
360 370 380 390 400
PHILLVEPLQ DCFPSGLIMA FSLNHLVGLN IMPILILHTI YWFSMDYSLM
410 420 430 440 450
NSMQNGKLSF SPLQFMLIWL LRELTAPFVF IKALLQPTIQ WRNNVFHLAW

GGQILPPKC
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ21054.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F59G1.1b.2.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

Proteomic databases

PaxDbiQ21054.
PRIDEiQ21054.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi174001.
WormBaseiF59G1.1a; CE29810; WBGene00019127; cgt-3.
F59G1.1b; CE29811; WBGene00019127; cgt-3.
F59G1.1c; CE30378; WBGene00019127; cgt-3.
F59G1.1d; CE33409; WBGene00019127; cgt-3.

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
InParanoidiQ21054.
KOiK00720.
OMAiLVWICDS.

Enzyme and pathway databases

UniPathwayiUPA00222.
ReactomeiREACT_310934. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi882053.
PROiQ21054.

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. "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: June 24, 2015
This is version 95 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

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.