CEGT_KOMPG
ID CEGT_KOMPG Reviewed; 509 AA.
AC C4R4B3; Q96V37;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 63.
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 OrderedLocusNames=PAS_chr3_0357;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=GS115 / ATCC 20864;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
RN [3]
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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19028992; DOI=10.1128/ec.00255-08;
RA Ramamoorthy V., Cahoon E.B., Thokala M., Kaur J., Li J., Shah D.M.;
RT "Sphingolipid C-9 methyltransferases are important for growth and virulence
RT but not for sensitivity to antifungal plant defensins in Fusarium
RT graminearum.";
RL Eukaryot. Cell 8:217-229(2009).
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). Shows increased resistance
CC to plant defensins MsDef1 and RsAFP2, and to heliomicin, a defensin-
CC like peptide from the insect Heliothis virescens (PubMed:14604982,
CC PubMed:19028992). {ECO:0000269|PubMed:11443131,
CC ECO:0000269|PubMed:14604982, ECO:0000269|PubMed:19028992}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF364403; AAK73020.1; -; Genomic_DNA.
DR EMBL; FN392321; CAY70399.1; -; Genomic_DNA.
DR RefSeq; XP_002492578.1; XM_002492533.1.
DR AlphaFoldDB; C4R4B3; -.
DR STRING; 644223.C4R4B3; -.
DR CAZy; GT21; Glycosyltransferase Family 21.
DR EnsemblFungi; CAY70399; CAY70399; PAS_chr3_0357.
DR GeneID; 8199490; -.
DR KEGG; ppa:PAS_chr3_0357; -.
DR eggNOG; KOG2547; Eukaryota.
DR HOGENOM; CLU_030898_1_0_1; -.
DR InParanoid; C4R4B3; -.
DR OMA; HGSMPFH; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000000314; Chromosome 3.
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:0008120; F:ceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006665; P:sphingolipid metabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR025993; Ceramide_glucosylTrfase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR12726; PTHR12726; 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..509
FT /note="Ceramide glucosyltransferase"
FT /id="PRO_5002942221"
FT TOPO_DOM 1..42
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..408
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..509
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 123
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 179
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 321
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 361..365
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 321
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 509 AA; 57164 MW; 08F80CB3F1B77821 CRC64;
MIMQLGLTSL AFLALKCDAY NIAPKIDTPN VEPFAPSGGL KLLAIVAIIW YVVVLLVAYY
GFFEIMQKFS KRKTLPVPPQ VEGVTILRPI KGIDPEMELC LQSAFDQDYP KFEIIICVES
ENDPGIGVAE ALIRKYPHVD ARILKGDSHN PDHFGPNPKV NNLAKGYSAG KYDIMWILDS
NVWVCSGALS RSVDALNRSL DNGRSTFDFQ TGKGRKVNLV HHVPMAISIN PQTGTNLDEM
FLFTSHSKFY ISINKAALAP CVNGKSNLYR RSELDLAVKR LGKGSEPSLD GTTGILAKDA
AYYGSKPGQG LRFFARYIGE DNMIATALWF QNGGRTGLTG DAAIQPLGGV NSTSLKNYLL
RRIRWLRVRK HMVLEATLLE PTTECLLCGT FGTFAISTLF LQSYFNWKFF IFHLLVWMVT
DYTQFHILLT NASQDTATCN VPYFAEPNFN AYGSPFESSN LRTFHRWVLY WLLREVLALP
IWISAMLGTR IIWRNRPFRI NVDLSAEEL
