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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

Pathway:isphingolipid 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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Lipid 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

  • Golgi apparatus membrane Sequence AnalysisBy similarity; Multi-pass membrane protein Sequence AnalysisBy similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1010LumenalSequence Analysis
Transmembranei11 – 3222HelicalSequence AnalysisAdd
BLAST
Topological domaini33 – 195163CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei196 – 21520HelicalSequence AnalysisAdd
BLAST
Topological domaini216 – 28772LumenalSequence AnalysisAdd
BLAST
Transmembranei288 – 30417HelicalSequence AnalysisAdd
BLAST
Topological domaini305 – 3095CytoplasmicSequence Analysis
Transmembranei310 – 32819HelicalSequence AnalysisAdd
BLAST
Topological domaini329 – 34820LumenalSequence AnalysisAdd
BLAST
Transmembranei349 – 36921HelicalSequence AnalysisAdd
BLAST
Topological domaini370 – 39425CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394Ceramide glucosyltransferase-BPRO_0000376855Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ5U4S8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.
InterProiIPR025993. Ceramide_glucosylTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF13506. Glyco_transf_21. 1 hit.
[Graphical view]
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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ5U4S8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi495444.
KEGGixla:495444.

Organism-specific databases

CTDi495444.
XenbaseiXB-GENE-944700. ugcg.

Phylogenomic databases

KOiK00720.

Enzyme and pathway databases

UniPathwayiUPA00222.

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

  1. NIH - Xenopus Gene Collection (XGC) project
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.

Entry informationi

Entry nameiCEGTB_XENLA
AccessioniPrimary (citable) accession number: Q5U4S8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: December 7, 2004
Last modified: January 7, 2015
This is version 45 of the entry and version 1 of the sequence. [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

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.