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Q21054

- CGT3_CAEEL

UniProt

Q21054 - CGT3_CAEEL

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Protein
Ceramide glucosyltransferase 3
Gene
cgt-3, F59G1.1
Organism
Caenorhabditis elegans
Status
Reviewed - 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

Pathwayi

GO - Molecular functioni

  1. ceramide glucosyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. sphingolipid metabolic process Source: UniProtKB-UniPathway
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.

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: 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 – 9721Helical; Reviewed prediction
Add
BLAST
Transmembranei367 – 38721Helical; Reviewed prediction
Add
BLAST
Transmembranei415 – 43521Helical; Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. 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 3
PRO_0000421283Add
BLAST

Proteomic databases

PaxDbiQ21054.
PRIDEiQ21054.

Interactioni

Protein-protein interaction databases

STRINGi6239.F59G1.1b.2.

Structurei

3D structure databases

ProteinModelPortaliQ21054.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000012898.
HOGENOMiHOG000039663.
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. Align

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

MCKYGKSNLA AVASSTSSII GAAAAAVAEA QPSASPSTSS SFLLLEVPFR    50
HLLRLQPPPY FIAGTRRMAA QLDVTTLIAI VGFVFVFCLY LIHIIALSYS 100
KYRLHHKVKE DSSLPGVSII KPIVGKDNNL YENIESFFTT QYHKYELLFC 150
FNSSDDEAVE VVKCLMKKYP KVDAKLFFGG ETVGLNPKIN NMMPAYRSAL 200
YPLILVSDSG IFMRSDGVLD MATTMMSHEK MALVTQTPYC KDREGFDAAF 250
EQMYFGTSHG RIYLAGNCMD FVCSTGMSSM MKKEALDECG GISNFGGYLA 300
EDYFFGRELA NRGYKSAISS HPALQNSSSV SVSSFLDRIC RWVKLRIAML 350
PHILLVEPLQ DCFPSGLIMA FSLNHLVGLN IMPILILHTI YWFSMDYSLM 400
NSMQNGKLSF SPLQFMLIWL LRELTAPFVF IKALLQPTIQ WRNNVFHLAW 450
GGQILPPKC 459
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.
VSP_045383Add
BLAST
Alternative sequencei1 – 1111MCKYGKSNLAA → MEVAKAVATNLSTAANSTVL RT in isoform b and isoform c.
VSP_045384Add
BLAST
Alternative sequencei361 – 3688DCFPSGLI → VIPKFTFF in isoform c.
VSP_045385
Alternative sequencei369 – 45991Missing in isoform c.
VSP_045386Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
RefSeqi NP_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 ]
UniGenei Cel.17849.
Cel.33407.

3D structure databases

ProteinModelPortali Q21054.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 6239.F59G1.1b.2.

Protein family/group databases

CAZyi GT21. Glycosyltransferase Family 21.

Proteomic databases

PaxDbi Q21054.
PRIDEi Q21054.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai F59G1.1a ; F59G1.1a ; WBGene00019127 . [Q21054-1 ]
GeneIDi 174001.
KEGGi cel:CELE_F59G1.1.
UCSCi F59G1.1b.1. c. elegans. [Q21054-1 ]

Organism-specific databases

CTDi 174001.
WormBasei F59G1.1a ; CE29810 ; WBGene00019127 ; cgt-3.
F59G1.1b ; CE29811 ; WBGene00019127 ; cgt-3.
F59G1.1c ; CE30378 ; WBGene00019127 ; cgt-3.
F59G1.1d ; CE33409 ; WBGene00019127 ; cgt-3.

Phylogenomic databases

eggNOGi COG1215.
GeneTreei ENSGT00390000012898.
HOGENOMi HOG000039663.
KOi K00720.
OMAi LVWICDS.

Enzyme and pathway databases

UniPathwayi UPA00222 .
Reactomei REACT_197713. Glycosphingolipid metabolism.

Miscellaneous databases

NextBioi 882053.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF13506. Glyco_transf_21. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 88 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

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