O88693 (CEGT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ceramide glucosyltransferase
EC=2.4.1.80

Alternative name(s):
GLCT-1
Glucosylceramide synthase
Short name=GCS
UDP-glucose ceramide glucosyltransferase
UDP-glucose:N-acylsphingosine D-glucosyltransferase

Gene names

Name:

Ugcg

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the first glycosylation step in glycosphingolipid biosynthesis, the transfer of glucose to ceramide. May also serve as a "flippase" By similarity.
Catalytic activity	UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. UniProtKB Q16739
Pathway	Lipid metabolism; sphingolipid metabolism.
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 2 family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Sphingolipid metabolism
Cellular component	Golgi apparatus Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	sphingolipid metabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ceramide glucosyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	Ceramide glucosyltransferase		PRO_0000059177
Regions
	Topological domain	1 – 10	10	Lumenal Potential
	Transmembrane	11 – 32	22	Helical; Potential
	Topological domain	33 – 195	163	Cytoplasmic Potential
	Transmembrane	196 – 215	20	Helical; Potential
	Topological domain	216 – 287	72	Lumenal Potential
	Transmembrane	288 – 304	17	Helical; Potential
	Topological domain	305 – 309	5	Cytoplasmic Potential
	Transmembrane	310 – 328	19	Helical; Potential
	Topological domain	329 – 348	20	Lumenal Potential
	Transmembrane	349 – 369	21	Helical; Potential
	Topological domain	370 – 394	25	Cytoplasmic Potential
Sites
	Site	193	1	May play an important role in binding to the inhibitors DEPC and PDMP By similarity

Sequences

	Sequence		Length	Mass (Da)
	O88693 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 8B18D09437CACE0E	FASTA	394	44,839
	10 20 30 40 50 60 MALLDLAQEG MALFGFVLFV VLWLMHFMSI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK 70 80 90 100 110 120 GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG 130 140 150 160 170 180 INPKINNLMP AYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF 190 200 210 220 230 240 AATLEQVYFG TSHPRSYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA 250 260 270 280 290 300 KAIADRGWRF SMSTQVAMQN SGSYSISQFQ SRMIRWTKLR INMLPATIIC EPISECFVAS 310 320 330 340 350 360 LIIGWAAHHV FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG TLCFSKLDYA VAWFIRESMT 370 380 390 IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of the mouse ceramide glucosyltransferase gene." Ichikawa S., Ozawa K., Hirabayashi Y. Biochem. Biophys. Res. Commun. 253:707-711(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129/SvJ.
[2]	"Molecular cloning and expression of mouse ceramide glucosyltransferase." Ichikawa S., Ozawa K., Hirabayashi Y. Biochem. Mol. Biol. Int. 44:1193-1202(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6J. Tissue: Brain.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Limb.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB012807 Genomic DNA. Translation: BAA33558.1. D89866 mRNA. Translation: BAA28782.1. AL808112 Genomic DNA. Translation: CAM26180.1. CH466565 Genomic DNA. Translation: EDL02214.1. BC050828 mRNA. Translation: AAH50828.1.
IPI	IPI00133265.
RefSeq	NP_035803.1. NM_011673.3.
UniGene	Mm.198803.
3D structure databases
ProteinModelPortal	O88693.
ModBase	Search...
Protein family/group databases
CAZy	GT21. Glycosyltransferase Family 21.
PTM databases
PhosphoSite	O88693.
Proteomic databases
PRIDE	O88693.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000030074; ENSMUSP00000030074; ENSMUSG00000028381.
GeneID	22234.
KEGG	mmu:22234.
UCSC	uc008szr.1. mouse.
Organism-specific databases
CTD	7357.
MGI	MGI:1332243. Ugcg.
Phylogenomic databases
eggNOG	COG1215.
GeneTree	ENSGT00390000012898.
HOGENOM	HOG000039663.
HOVERGEN	HBG003997.
InParanoid	A2AN90.
KO	K00720.
OMA	GIKCVTG.
OrthoDB	EOG43TZVM.
Enzyme and pathway databases
UniPathway	UPA00222.
Gene expression databases
Bgee	O88693.
CleanEx	MM_UGCG.
Genevestigator	O88693.
GermOnline	ENSMUSG00000028381. Mus musculus.
Family and domain databases
InterPro	IPR025993. Ceramide_glucosylTrfase. [Graphical view]
Pfam	PF13506. Glyco_transf_21. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O88693.
ChEMBL	CHEMBL6013.
ChiTaRS	UGCG. mouse.
NextBio	302281.
SOURCE	Search...

Entry information

Entry name

CEGT_MOUSE

Accession

Primary (citable) accession number: O88693
Secondary accession number(s): A2AN90

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	November 1, 1998
Last modified:	April 3, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program