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Database: UniProt
Entry: W7I386_9PEZI
LinkDB: W7I386_9PEZI
Original site: W7I386_9PEZI 
ID   W7I386_9PEZI            Unreviewed;       486 AA.
AC   W7I386;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00019988};
DE            EC=2.4.1.80 {ECO:0000256|ARBA:ARBA00012699};
DE   AltName: Full=Glucosylceramide synthase {ECO:0000256|ARBA:ARBA00031543};
DE   AltName: Full=UDP-glucose ceramide glucosyltransferase {ECO:0000256|ARBA:ARBA00032575};
DE   AltName: Full=UDP-glucose:N-acylsphingosine D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031017};
GN   ORFNames=DRE_03864 {ECO:0000313|EMBL:EWC46852.1};
OS   Drechslerella stenobrocha 248.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Drechslerella.
OX   NCBI_TaxID=1043628 {ECO:0000313|EMBL:EWC46852.1, ECO:0000313|Proteomes:UP000024837};
RN   [1] {ECO:0000313|EMBL:EWC46852.1, ECO:0000313|Proteomes:UP000024837}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=248 {ECO:0000313|EMBL:EWC46852.1,
RC   ECO:0000313|Proteomes:UP000024837};
RA   Liu X., Zhang W., Liu K.;
RT   "Drechslerella stenobrocha genome reveals carnivorous origination and
RT   mechanical trapping mechanism of predatory fungi.";
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC       {ECO:0000256|ARBA:ARBA00004760}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000256|ARBA:ARBA00006739}.
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DR   EMBL; KI966414; EWC46852.1; -; Genomic_DNA.
DR   AlphaFoldDB; W7I386; -.
DR   HOGENOM; CLU_030898_1_0_1; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000024837; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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   InterPro; IPR025993; Ceramide_glucosylTrfase.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR12726; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR12726:SF0; CERAMIDE GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF13506; Glyco_transf_21; 2.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024837};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   486 AA;  54709 MW;  3D28DAB3CA4A36E1 CRC64;
     MSDQEPFPYA HLAAQAAAIV AVIWYVAIWL IGLLGHIRIR ATISRKLVAG APRAESVSST
     LSPSNAPGVT IIRPIKSPGP FQTEPHLAEC LLSSVRQRYP RFELILTVAD HDDPAIHCIR
     QIIRENPDHD VSLVIGDEKI GINPKINNLI RGWRKAKYDI VWVIDCNIWL DPGAMGRAVD
     VLLGHPWDED LRQKPSRRPA KFVHHLPICV NTTGTDEFLK PWTSRFDSSG CALEESFLSS
     SHAKFYTAIN TVAIAPCIIG KSNMFRKSHL MELCPKTPYT EGGIATFSSK LCEDHLIAEQ
     LWKYTVKDDV KYNNENGTSA GLIKHALLNE PCFQPMSGMT IRDYWARRSR WLQVRKFAVF
     AATIVEPGTE SFLASYIGGV GLKYLGLLPA DWTVLYFWLA SVGAWCLGDW LLYREIHKYE
     TVNKSDPDCP VWLKVGRKRS IPAWFLQWLG REALALPVWF NGMFRGDVNW RGNEFSVGIG
     GIRQAN
//
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