CEGT_XENTR
ID CEGT_XENTR Reviewed; 394 AA.
AC Q5BL38;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ceramide glucosyltransferase {ECO:0000250|UniProtKB:Q16739};
DE EC=2.4.1.80 {ECO:0000250|UniProtKB:Q8AY29};
DE AltName: Full=Glycosylceramide synthase;
DE AltName: Full=UDP-glucose ceramide glucosyltransferase {ECO:0000312|EMBL:AAH90614.1};
GN Name=ugcg; ORFNames=TEgg030g03.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ81500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg {ECO:0000312|EMBL:CAJ81500.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:CAJ81500.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud {ECO:0000312|EMBL:AAH90614.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in the initial step of the glucosylceramide-
CC based glycosphingolipid/GSL synthetic pathway at the cytosolic surface
CC of the Golgi. Catalyzes the transfer of glucose from UDP-glucose to
CC ceramide to produce glucosylceramide/GlcCer (such as beta-D-glucosyl-
CC (1<->1')-N-acylsphing-4-enine). Glucosylceramide is the core component
CC of glycosphingolipids/GSLs, amphipathic molecules consisting of a
CC ceramide lipid moiety embedded in the outer leaflet of the membrane,
CC linked to one of hundreds of different externally oriented
CC oligosaccharide structures. Glycosphingolipids are essential components
CC of membrane microdomains that mediate membrane trafficking and signal
CC transduction. They are implicated in many fundamental cellular
CC processes, including growth, differentiation, migration, morphogenesis,
CC cell-to-cell and cell-to-matrix interactions (By similarity). Catalyzes
CC the synthesis of xylosylceramide/XylCer (such as beta-D-xylosyl-
CC (1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor (By
CC similarity). {ECO:0000250|UniProtKB:Q16739,
CC ECO:0000250|UniProtKB:Q8AY29}.
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:0000250|UniProtKB:Q8AY29};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-xylose = a beta-D-
CC xylosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC Xref=Rhea:RHEA:70243, ChEBI:CHEBI:15378, ChEBI:CHEBI:52639,
CC ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:189068;
CC Evidence={ECO:0000250|UniProtKB:Q16739};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70244;
CC Evidence={ECO:0000250|UniProtKB:Q16739};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(9Z-octadecenoyl)-sphing-4-enine + UDP-alpha-D-xylose =
CC beta-D-xylosyl-(1<->1')-N-(9Z-octadecenoyl)-sphing-4-enine + H(+) +
CC UDP; Xref=Rhea:RHEA:70247, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:77996, ChEBI:CHEBI:189081;
CC Evidence={ECO:0000250|UniProtKB:Q16739};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70248;
CC Evidence={ECO:0000250|UniProtKB:Q16739};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000250|UniProtKB:Q8AY29}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8AY29, ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000250|UniProtKB:Q8AY29, 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 -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000255}.
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DR EMBL; CR762041; CAJ81500.1; -; mRNA.
DR EMBL; BC090614; AAH90614.1; -; mRNA.
DR RefSeq; NP_001016133.1; NM_001016133.2.
DR AlphaFoldDB; Q5BL38; -.
DR SMR; Q5BL38; -.
DR STRING; 8364.ENSXETP00000005911; -.
DR CAZy; GT21; Glycosyltransferase Family 21.
DR PaxDb; Q5BL38; -.
DR DNASU; 548887; -.
DR Ensembl; ENSXETT00000084396; ENSXETP00000100363; ENSXETG00000010219.
DR GeneID; 548887; -.
DR KEGG; xtr:548887; -.
DR CTD; 7357; -.
DR Xenbase; XB-GENE-944694; ugcg.
DR eggNOG; KOG2547; Eukaryota.
DR HOGENOM; CLU_030898_0_0_1; -.
DR InParanoid; Q5BL38; -.
DR OMA; TCLYHGV; -.
DR OrthoDB; 793389at2759; -.
DR PhylomeDB; Q5BL38; -.
DR TreeFam; TF314564; -.
DR Reactome; R-XTR-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000010219; Expressed in neurula embryo and 20 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
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; ISS:UniProtKB.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IBA:GO_Central.
DR GO; GO:0046479; P:glycosphingolipid catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Developmental protein; Glycosyltransferase; Golgi apparatus;
KW Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome;
KW Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..394
FT /note="Ceramide glucosyltransferase"
FT /id="PRO_0000376856"
FT TOPO_DOM 1..10
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..215
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 216..287
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..348
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 92
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 144
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 236
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 272..276
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 236
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 394 AA; 44638 MW; 1CF7077F02358BD0 CRC64;
MAVLDLALQG LAIFGCVLFF VLWFMHFLSI VYTRLHLNKK VSDKQPYSKL PGVSLLKPLK
GVDPNLINNL ETFFELDYPK FEILLCVQDL DDPAVDVCKK LLGKYPSVDA KLFIGGKKVG
INPKINNLMP GYEVAKYDLI WICDSGIKVK PDTLTDMANQ MTEKVGLVHG LPYVADRQGF
AATLEQVYFG TSHPRSYISA NVTGFKCVTG MSCLMRKEVL DQAGGLIAFA QYIAEDYFMA
KAIADRGWKF SMATQVAMQN SGCYSISQFQ SRMIRWAKLR INMLPATIIC EPISECFVAS
LIIGWAAHHI FRWDIMVFFM CHCLAWFIFD YIQLRGVQGG PLNFSKLDYA VAWFIRESMT
IYIFLSALWD PTISWRTGRY RLRCGGTAEE ILDV
