CEGT_CANAL
ID CEGT_CANAL Reviewed; 544 AA.
AC Q5AMQ4; A0A1D8PLE8;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Ceramide glucosyltransferase {ECO:0000250|UniProtKB:Q16739};
DE EC=2.4.1.80 {ECO:0000269|PubMed:11443131};
DE AltName: Full=GLCT-1;
DE AltName: Full=Glucosylceramide synthase {ECO:0000303|PubMed:11443131};
DE Short=GCS;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase {ECO:0000303|PubMed:14604982};
DE AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase;
GN Name=HSX11 {ECO:0000303|PubMed:11443131}; Synonyms=CGT1;
GN OrderedLocusNames=CAALFM_C402010CA; ORFNames=CaO19.12061, CaO19.4592;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND DISRUPTION PHENOTYPE.
RX PubMed=11443131; DOI=10.1074/jbc.m104952200;
RA Leipelt M., Warnecke D., Zahringer U., Ott C., Muller F., Hube B.,
RA Heinz E.;
RT "Glucosylceramide synthases, a gene family responsible for the biosynthesis
RT of glucosphingolipids in animals, plants, and fungi.";
RL J. Biol. Chem. 276:33621-33629(2001).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=14604982; DOI=10.1074/jbc.m311165200;
RA Thevissen K., Warnecke D.C., Francois I.E., Leipelt M., Heinz E., Ott C.,
RA Zaehringer U., Thomma B.P., Ferket K.K., Cammue B.P.;
RT "Defensins from insects and plants interact with fungal
RT glucosylceramides.";
RL J. Biol. Chem. 279:3900-3905(2004).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=20019081; DOI=10.1099/mic.0.033985-0;
RA Oura T., Kajiwara S.;
RT "Candida albicans sphingolipid C9-methyltransferase is involved in hyphal
RT elongation.";
RL Microbiology 156:1234-1243(2010).
CC -!- FUNCTION: Catalyzes the final step in the biosynthesis of the membrane
CC lipid glucosylceramide (GluCer), the transfer of glucose to ceramide.
CC Glucosylceramides play important roles in growth, differentiation and
CC pathogenicity. {ECO:0000269|PubMed:11443131}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-glucose = a beta-D-
CC glucosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC Xref=Rhea:RHEA:12088, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.80;
CC Evidence={ECO:0000269|PubMed:11443131};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000305|PubMed:11443131}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9R0E0}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DOMAIN: The D1, D2, D3, (Q/R)XXRW motif is a critical part of the GCS
CC active site, involved in catalysis and UDP-sugar binding.
CC {ECO:0000250|UniProtKB:Q9R0E0}.
CC -!- DISRUPTION PHENOTYPE: Results in complete loss of glucosylceramides
CC (GluCers) in mutant cells (PubMed:11443131). Has a decreased hyphal
CC growth rate and increased susceptibility to SDS and fluconazole,
CC suggesting defects in the cell membrane structure (PubMed:20019081).
CC Shows increased resistance to plant defensin RsAFP2, and to heliomicin,
CC a defensin-like peptide from the insect Heliothis virescens
CC (PubMed:14604982). {ECO:0000269|PubMed:11443131,
CC ECO:0000269|PubMed:14604982, ECO:0000269|PubMed:20019081}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; CP017626; AOW28972.1; -; Genomic_DNA.
DR RefSeq; XP_722664.1; XM_717571.1.
DR AlphaFoldDB; Q5AMQ4; -.
DR STRING; 237561.Q5AMQ4; -.
DR EnsemblFungi; KHC77503; KHC77503; W5Q_03501.
DR EnsemblFungi; KHC86755; KHC86755; I503_03493.
DR GeneID; 3635660; -.
DR KEGG; cal:CAALFM_C402010CA; -.
DR CGD; CAL0000175173; HSX11.
DR VEuPathDB; FungiDB:C4_02010C_A; -.
DR eggNOG; KOG2547; Eukaryota.
DR HOGENOM; CLU_030898_1_0_1; -.
DR InParanoid; Q5AMQ4; -.
DR OMA; HGSMPFH; -.
DR OrthoDB; 793389at2759; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:Q5AMQ4; -.
DR Proteomes; UP000000559; Chromosome 4.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008120; F:ceramide glucosyltransferase activity; IDA:CGD.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IMP:CGD.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; PTHR12726; 1.
DR Pfam; PF13506; Glyco_transf_21; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Golgi apparatus; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..544
FT /note="Ceramide glucosyltransferase"
FT /id="PRO_0000434806"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..451
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 502..522
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..544
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 109
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 171
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 364
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 404..408
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 364
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 544 AA; 62451 MW; C97BAD8D51725D95 CRC64;
MVQEELSLFR ITTGYFFLLW YIIILVAAYS GFFEILFNFR NRPILHTKQQ ANHQNDPESD
DEEIYEGVTI IRPIKGIDPE LTSCLESSFC QNYPRSKLQI LFCVDDPNDP SIPIIQKLIA
KYPTVDAQIL TSESYNSQTK TSDDHYGPNP KVNNLAKGFV HAKYDILWVM DSNVWASSNI
LKNSVISLNG NLNMSRKMGQ SRPVKLVHHV PLALSINNTT RSDDFIGGQD LEITAMTPVP
SSESLNSQLV KRKSSPKSNN SLNVHPGFTY SKFSKKLGAE LDEMFLHTSH SKFYVSLNNL
AVAPCVNGKS NIYRRSDLDQ SVRLIPHKDS PFFKDPKVKQ DAGYYTSLGV GHAIKFFARY
IGEDNMIGIA LWENTQGRTG LTGDVVVQPY SGSENNAVKD YIQRRVRWLR VRKYMVLLAT
LIEPTTESII CGIYGTYAIS TVFFGTWFNK YWFVMHMLIW MLTDYVQYHT LINHTLDVKN
ITYLPNWLNE SIPPKQRNCL QWGYIWILRE LLALPIWIIA MIGHEIDWRG RPFRIKKDLT
AEEM
