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Protein

Ceramide glucosyltransferase-B

Gene

ugcg-b

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

Catalytic activityi

UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine.By similarity

Pathwayi: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.By similarity
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

Keywordsi

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

Enzyme and pathway databases

UniPathwayiUPA00222.

Names & Taxonomyi

Protein namesi
Recommended name:
Ceramide glucosyltransferase-B (EC:2.4.1.80)
Alternative name(s):
UDP-glucose ceramide glucosyltransferaseBy similarity
Gene namesi
Name:ugcg-b
Synonyms:ugcg
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-944700. 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_00003768551 – 394Ceramide glucosyltransferase-BAdd BLAST394

Structurei

3D structure databases

ProteinModelPortaliQ5U4S8.
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.

Q5U4S8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVLDLALQG LAIFGCILFF VLWFMHFLSI VYTRLHLNKK VSDKQPYSKL
60 70 80 90 100
PGVSLLKPLK GVDSNLINNL ETFFELDYPK FEILLCVQDL DDPAVDVCKK
110 120 130 140 150
LLGKYPSVDA KLFIGGKKVG INPKINNLMP GYEVAKYDLI WICDSGIKVK
160 170 180 190 200
PDTLTDMANQ MTEKVGLVHG LPYVADRQGF AATLEQVYFG TSHPRSYISA
210 220 230 240 250
NVTGIKCVTG 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 PTISWRTGRY RLRCGGTAEE ILDV
Length:394
Mass (Da):44,607
Last modified:December 7, 2004 - v1
Checksum:iFDA06E33F49749B3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC084966 mRNA. Translation: AAH84966.1.
RefSeqiNP_001088566.1. NM_001095097.1.
UniGeneiXl.21133.

Genome annotation databases

GeneIDi495444.
KEGGixla:495444.

Similar proteinsi

Entry informationi

Entry nameiCEGTB_XENLA
AccessioniPrimary (citable) accession number: Q5U4S8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: December 7, 2004
Last modified: September 27, 2017
This is version 48 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