ID D6RK12_COPC7 Unreviewed; 431 AA.
AC D6RK12;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=CC1G_13695 {ECO:0000313|EMBL:EFI28669.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EFI28669.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EFI28669.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFI28669.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AACS02000001; EFI28669.1; -; Genomic_DNA.
DR RefSeq; XP_002912163.1; XM_002912117.1.
DR AlphaFoldDB; D6RK12; -.
DR STRING; 240176.D6RK12; -.
DR GeneID; 6018151; -.
DR KEGG; cci:CC1G_13695; -.
DR VEuPathDB; FungiDB:CC1G_13695; -.
DR eggNOG; KOG2547; Eukaryota.
DR HOGENOM; CLU_030898_1_0_1; -.
DR InParanoid; D6RK12; -.
DR OMA; HGSMPFH; -.
DR OrthoDB; 2786173at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000001861; 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; 1.
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:UP000001861};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..411
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 431 AA; 48942 MW; 1D66F9E195D40594 CRC64;
MPSLEVDDDL RNTLSFGFAI AGLVWYSVLW CIGLLGAVAA YRRYRNRPIY VDYTPAREAP
GVSILRPLKG LDPNLYTNLE STFRQNYPNF EILFSVADAK DQAIPVVQEL LQLYPDVKAQ
IVVGEEVVGV NPKVNNLVRP YRMAAHDIVW VLDSNVSTDP GTLSRAVEAL TSPRNTSKRR
IGVVHHIPFV ESTTAYWGSR IEAAFLNTFH AKMYIAINTV AIESCVVGKS NLYRRSDVDR
VNGTLKPIDP MDLDEGRVKR GFPSFGRFLA EDNMIASALW HELGLRHDLS TDVAYNVVGN
MTIWDYVWRR VRWLRVRKRM VLAANLVEPF TESIMLSIIG SSSGKYLFGI PRVLFMAVHF
VLWFLVDISV YKSLADRVPV VIDRYFVVAW LLREVASLPI WIFGFFGNTV VWRGQRYRML
RNGEVALASS K
//