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Q8AY29 (CEGTA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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-A

Short name=XLCGT
EC=2.4.1.80
Alternative name(s):
UDP-glucose ceramide glucosyltransferase
Gene names
Name:ugcg-a
Synonyms:ugcg
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length394 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. Glycosphingolipids are required for convergence extension movements during early development. Ref.1

Catalytic activity

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

Pathway

Lipid metabolism; sphingolipid metabolism. Ref.1

Subcellular location

Golgi apparatus membrane; Multi-pass membrane protein Potential Ref.1.

Tissue specificity

At the late gastrula stage, weakly expressed ubiquitously. As neurulation proceeds (stages 15-16), expression moves towards the dorsal structures: involuted paraxial mesoderm and neural folds. In the tailbud embryo (stage 28), expression is restricted to the notochord. At later stages (stage 35), expression remains in the notochord and also appears weakly in the cephalic region. Ref.1

Developmental stage

Expressed both maternally and zygotically. Expressed at all stages of oogenesis except in previtellogenic oocytes. During embryogenesis, weakly expressed as early as the one-cell stage shortly after fertilization, and remains at a relatively uniform level throughout embryogenesis, persisting at least until stage 35 (early tadpole). Ref.1

Sequence similarities

Belongs to the glycosyltransferase 2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Ceramide glucosyltransferase-A
PRO_0000376854

Regions

Topological domain1 – 1010Lumenal Potential
Transmembrane11 – 3222Helical; Potential
Topological domain33 – 195163Cytoplasmic Potential
Transmembrane196 – 21520Helical; Potential
Topological domain216 – 28772Lumenal Potential
Transmembrane288 – 30417Helical; Potential
Topological domain305 – 3095Cytoplasmic Potential
Transmembrane310 – 32819Helical; Potential
Topological domain329 – 34820Lumenal Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 39425Cytoplasmic Potential

Experimental info

Sequence conflict1081D → V in AAH89245. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8AY29 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: D25C6236C6A3388A

FASTA39444,651
        10         20         30         40         50         60 
MAVLDLALQG LAIFGCVLFF VLWFMHFLSI VYTRLHLNKK ISDKQPYSKL PGVSLLKPLK 

        70         80         90        100        110        120 
GVDPNLINNL ETFFELDYPK FEILLCVQDL DDPAVDVCKK LLGKYPSDDA KLFIGGKKVG 

       130        140        150        160        170        180 
INPKINNLMP GYEVAKYDLI WICDSGIKVK PDTLTDMANQ MTEKVGLVHG LPYVADRQGF 

       190        200        210        220        230        240 
AATLEQVYFG TSHPRSYISA NVTGFKCVTG MSCLMRKEVL DQAGGLIAFA QYIAEDYFMA 

       250        260        270        280        290        300 
KAIADRGWKF SMATQVAMQN SGCYSISQFQ SRMIRWAKLR INMLPATIIC EPISECFVAS 

       310        320        330        340        350        360 
LIIGWAAHHI FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG PLNFSKLDYA VAWFIRESMT 

       370        380        390 
IYIFLSALWD PTISWRTGRF RLRCGGTAEE ILDV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and functional characterization of two key enzymes of glycosphingolipid biosynthesis in the amphibian Xenopus laevis."
Luque M.E., Crespo P.M., Monaco M.E., Aybar M.J., Daniotti J.L., Sanchez S.S.
Dev. Dyn. 237:112-123(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]NIH - Xenopus Gene Collection (XGC) project
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Egg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY112732 mRNA. Translation: AAM49061.1.
BC089245 mRNA. Translation: AAH89245.1.
RefSeqNP_001083944.1. NM_001090475.1.
UniGeneXl.21362.

3D structure databases

ProteinModelPortalQ8AY29.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGT21. Glycosyltransferase Family 21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID399204.
KEGGxla:399204.

Organism-specific databases

CTD399204.
XenbaseXB-GENE-6254211. ugcg.

Phylogenomic databases

KOK00720.

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...

Entry information

Entry nameCEGTA_XENLA
AccessionPrimary (citable) accession number: Q8AY29
Secondary accession number(s): Q5FWQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: March 1, 2003
Last modified: June 11, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways