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Q09426 (CGT_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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:
2-hydroxyacylsphingosine 1-beta-galactosyltransferase

EC=2.4.1.45
Alternative name(s):
Ceramide UDP-galactosyltransferase
Cerebroside synthase
UDP-galactose-ceramide galactosyltransferase
Gene names
Name:Ugt8
Synonyms:Cgt, Ugt4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.

Catalytic activity

UDP-alpha-D-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D-galactosyl)-2-(2-hydroxyacyl)sphingosine.

Pathway

Sphingolipid metabolism; galactosylceramide biosynthesis.

Subcellular location

Membrane; Single-pass membrane protein Potential.

Tissue specificity

Brain, restricted to the oligodendrocyte-containing cell layers of cerebrum and cerebellum.

Sequence similarities

Belongs to the UDP-glycosyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 5415212-hydroxyacylsphingosine 1-beta-galactosyltransferase
PRO_0000036066

Regions

Transmembrane472 – 49221Helical; Potential

Amino acid modifications

Glycosylation781N-linked (GlcNAc...) Potential Ref.1
Glycosylation3331N-linked (GlcNAc...) Potential Ref.1
Glycosylation4421N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q09426 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 260D7603170151BB

FASTA54161,126
        10         20         30         40         50         60 
MKSYTPYFML LWSAVGIARA AKIIIVPPIM FESHLYIFKT LASALHERGH HTVFLLSEGR 

        70         80         90        100        110        120 
DIDPSNHYSL QRYPGIFNST TSDAFLQSKM RNIFSGRLTA VELVDILDHY TKNCDMMVGN 

       130        140        150        160        170        180 
QALIQGLKKE KFDLLLVDPN DMCGFVIAHL LGVKYAVFST GLWYPAEVGA PAPLAYVPEF 

       190        200        210        220        230        240 
NSLLTDRMNF LERMKNTGVY LISRMGVSFL VLPKYERIMQ KYNLLPAKSM YDLVHGSSLW 

       250        260        270        280        290        300 
MLCTDVALEF PRPTLPNVVY VGGILTKPAS PLPEDLQRWV DGAQEHGFVL VSFGAGVKYL 

       310        320        330        340        350        360 
SEDIANKLAG ALGRLPQKVI WRFSGTKPKN LGNNTKLIEW LPQNDLLGHS NIRAFLSHGG 

       370        380        390        400        410        420 
LNSIFETMYH GVPVVGIPLF GDHYDTMTRV QAKGMGILLE WNTVTEGELY DALVKVINNP 

       430        440        450        460        470        480 
SYRQRAQKLS EIHKDQPGHP VNRTTYWIDY ILRHDGAHHL RSAVHQISFC QYFLLDIAFV 

       490        500        510        520        530        540 
LLLGAVALYF IVSYVTKFIY RKVKSLCSRS THSTVNGHYQ NGILNGRYKG NGHIKHEKKV 


K 

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References

[1]"Ceramide UDPgalactosyltransferase from myelinating rat brain: purification, cloning, and expression."
Schulte S., Stoffel W.
Proc. Natl. Acad. Sci. U.S.A. 90:10265-10269(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Brain.
[2]"Isolation, characterization, and expression of cDNA clones that encode rat UDP-galactose: ceramide galactosyltransferase."
Stahl N., Jurevics H., Morell P., Suzuki K., Popko B.
J. Neurosci. Res. 38:234-242(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L21698 mRNA. Translation: AAA16108.1.
U07683 mRNA. Translation: AAA50212.1.
PIRA48801.
RefSeqNP_062149.1. NM_019276.3.
UniGeneRn.9744.

3D structure databases

ProteinModelPortalQ09426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000012676.

Protein family/group databases

CAZyGT1. Glycosyltransferase Family 1.

Proteomic databases

PaxDbQ09426.
PRIDEQ09426.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012676; ENSRNOP00000012676; ENSRNOG00000009345.
GeneID50555.
KEGGrno:50555.
UCSCRGD:3938. rat.

Organism-specific databases

CTD7368.
RGD3938. Ugt8.

Phylogenomic databases

eggNOGCOG1819.
GeneTreeENSGT00560000076760.
HOGENOMHOG000220831.
HOVERGENHBG098341.
InParanoidQ09426.
KOK04628.
OMASNHYSLQ.
OrthoDBEOG7GBFWS.
PhylomeDBQ09426.
TreeFamTF315472.

Enzyme and pathway databases

UniPathwayUPA00787.

Gene expression databases

GenevestigatorQ09426.

Family and domain databases

InterProIPR002213. UDP_glucos_trans.
[Graphical view]
PANTHERPTHR11926. PTHR11926. 1 hit.
PfamPF00201. UDPGT. 1 hit.
[Graphical view]
PROSITEPS00375. UDPGT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio610356.
PROQ09426.

Entry information

Entry nameCGT_RAT
AccessionPrimary (citable) accession number: Q09426
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 102 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