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Protein

Ceramide glucosyltransferase-A

Gene

ugcg-a

Organism
Xenopus laevis (African clawed frog)
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. Glycosphingolipids are required for convergence extension movements during early development.1 Publication

Catalytic activityi

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

Pathwayi: 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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei236Proton acceptorBy similarity1

GO - Molecular functioni

GO - Biological processi

  • glycosphingolipid catabolic process Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW

Keywordsi

Molecular functionDevelopmental protein, Glycosyltransferase, Transferase
Biological processLipid biosynthesis, Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00222.

Protein family/group databases

CAZyiGT21. Glycosyltransferase Family 21.

Chemistry databases

SwissLipidsiSLP:000000788.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide glucosyltransferase-A (EC:2.4.1.80)
Short name:
XLCGT1 Publication
Alternative name(s):
UDP-glucose ceramide glucosyltransferaseImported
Gene namesi
Name:ugcg-a
Synonyms:ugcgImported
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-6254211. ugcg.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10LumenalSequence analysis10
Transmembranei11 – 32HelicalSequence analysisAdd BLAST22
Topological domaini33 – 195CytoplasmicSequence analysisAdd BLAST163
Transmembranei196 – 215HelicalSequence analysisAdd BLAST20
Topological domaini216 – 287LumenalSequence analysisAdd BLAST72
Transmembranei288 – 304HelicalSequence analysisAdd BLAST17
Topological domaini305 – 309CytoplasmicSequence analysis5
Transmembranei310 – 328HelicalSequence analysisAdd BLAST19
Topological domaini329 – 348LumenalSequence analysisAdd BLAST20
Transmembranei349 – 369HelicalSequence analysisAdd BLAST21
Topological domaini370 – 394CytoplasmicSequence analysisAdd BLAST25

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003768541 – 394Ceramide glucosyltransferase-AAdd BLAST394

Expressioni

Tissue specificityi

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.1 Publication

Developmental stagei

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).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8AY29.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi92D1Curated1
Motifi144D2Curated1
Motifi236D3Curated1
Motifi272 – 276(Q/R)XXRWCurated5

Domaini

The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS active site, involved in catalysis and UDP-sugar binding.By similarity

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Sequence analysis

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

KOiK00720.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiView protein in InterPro
IPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
PfamiView protein in Pfam
PF13506. Glyco_transf_21. 1 hit.
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8AY29-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLDLALQG LAIFGCVLFF VLWFMHFLSI VYTRLHLNKK ISDKQPYSKL
60 70 80 90 100
PGVSLLKPLK GVDPNLINNL ETFFELDYPK FEILLCVQDL DDPAVDVCKK
110 120 130 140 150
LLGKYPSDDA KLFIGGKKVG INPKINNLMP GYEVAKYDLI WICDSGIKVK
160 170 180 190 200
PDTLTDMANQ MTEKVGLVHG LPYVADRQGF AATLEQVYFG TSHPRSYISA
210 220 230 240 250
NVTGFKCVTG MSCLMRKEVL DQAGGLIAFA QYIAEDYFMA KAIADRGWKF
260 270 280 290 300
SMATQVAMQN SGCYSISQFQ SRMIRWAKLR INMLPATIIC EPISECFVAS
310 320 330 340 350
LIIGWAAHHI FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG PLNFSKLDYA
360 370 380 390
VAWFIRESMT IYIFLSALWD PTISWRTGRF RLRCGGTAEE ILDV
Length:394
Mass (Da):44,651
Last modified:March 1, 2003 - v1
Checksum:iD25C6236C6A3388A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti108D → V in AAH89245 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY112732 mRNA. Translation: AAM49061.1.
BC089245 mRNA. Translation: AAH89245.1.
RefSeqiNP_001083944.1. NM_001090475.1.
UniGeneiXl.21362.

Genome annotation databases

GeneIDi399204.
KEGGixla:399204.

Similar proteinsi

Entry informationi

Entry nameiCEGTA_XENLA
AccessioniPrimary (citable) accession number: Q8AY29
Secondary accession number(s): Q5FWQ7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: March 1, 2003
Last modified: September 27, 2017
This is version 50 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families