Q16739 (CEGT_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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". Ref.1
Catalytic activity	UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. Ref.1
Pathway	Lipid metabolism; sphingolipid metabolism.
Subcellular location	Golgi apparatus membrane; Multi-pass membrane protein By similarity.
Tissue specificity	Found in all tissues examined. Ref.1
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	epidermis development Traceable author statement PubMed 9545298. Source: ProtInc glucosylceramide biosynthetic process Traceable author statement Ref.1. Source: ProtInc phospholipid metabolic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ceramide glucosyltransferase activity Traceable author statement Ref.1. Source: ProtInc
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_0000059176
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)
	Q16739 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 3B998569F8A96449	FASTA	394	44,854
	10 20 30 40 50 60 MALLDLALEG MAVFGFVLFL VLWLMHFMAI IYTRLHLNKK ATDKQPYSKL PGVSLLKPLK 70 80 90 100 110 120 GVDPNLINNL ETFFELDYPK YEVLLCVQDH DDPAIDVCKK LLGKYPNVDA RLFIGGKKVG 130 140 150 160 170 180 INPKINNLMP GYEVAKYDLI WICDSGIRVI PDTLTDMVNQ MTEKVGLVHG LPYVADRQGF 190 200 210 220 230 240 AATLEQVYFG TSHPRYYISA NVTGFKCVTG MSCLMRKDVL DQAGGLIAFA QYIAEDYFMA 250 260 270 280 290 300 KAIADRGWRF AMSTQVAMQN 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]	"Expression cloning of a cDNA for human ceramide glucosyltransferase that catalyzes the first glycosylation step of glycosphingolipid synthesis." Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y. Proc. Natl. Acad. Sci. U.S.A. 93:4638-4643(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Melanoma.
[2]	Erratum Ichikawa S., Sakiyama H., Suzuki G., Hidari K.I.-P., Hirabayashi Y. Proc. Natl. Acad. Sci. U.S.A. 93:12654-12654(1996) [PubMed] [Europe PMC] [Abstract]
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[4]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: Testis.
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases
EMBL GenBank DDBJ	D50840 mRNA. Translation: BAA09451.1. AK314847 mRNA. Translation: BAG37364.1. AL442066 Genomic DNA. Translation: CAI15902.1. CH471105 Genomic DNA. Translation: EAW59091.1. BC038711 mRNA. Translation: AAH38711.1.
IPI	IPI00003861.
RefSeq	NP_003349.1. NM_003358.1.
UniGene	Hs.304249. Hs.593014.
3D structure databases
ProteinModelPortal	Q16739.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000363397.
Protein family/group databases
CAZy	GT21. Glycosyltransferase Family 21.
PTM databases
PhosphoSite	Q16739.
Polymorphism databases
DMDM	2498228.
Proteomic databases
PaxDb	Q16739.
PRIDE	Q16739.
Protocols and materials databases
DNASU	7357.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000374279; ENSP00000363397; ENSG00000148154.
GeneID	7357.
KEGG	hsa:7357.
UCSC	uc004bft.3. human.
Organism-specific databases
CTD	7357.
GeneCards	GC09P114659.
HGNC	HGNC:12524. UGCG.
HPA	HPA024124.
MIM	602874. gene.
neXtProt	NX_Q16739.
PharmGKB	PA37169.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1215.
HOGENOM	HOG000039663.
HOVERGEN	HBG003997.
InParanoid	Q16739.
KO	K00720.
OMA	GIKCVTG.
OrthoDB	EOG43TZVM.
PhylomeDB	Q16739.
Enzyme and pathway databases
BRENDA	2.4.1.80. 2681.
Pathway_Interaction_DB	il2_pi3kpathway. IL2 signaling events mediated by PI3K.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00222.
Gene expression databases
Bgee	Q16739.
CleanEx	HS_UGCG.
Genevestigator	Q16739.
GermOnline	ENSG00000148154. Homo sapiens.
Family and domain databases
InterPro	IPR025993. Ceramide_glucosylTrfase. [Graphical view]
Pfam	PF13506. Glyco_transf_21. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q16739.
ChEMBL	CHEMBL2063.
DrugBank	DB00419. Miglustat.
GenomeRNAi	7357.
NextBio	28808.
SOURCE	Search...

Entry information

Entry name

CEGT_HUMAN

Accession

Primary (citable) accession number: Q16739
Secondary accession number(s): Q5T258

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.