ID   CEGTA_XENLA             Reviewed;         394 AA.
AC   Q8AY29; Q5FWQ7;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Ceramide glucosyltransferase-A;
DE            Short=XLCGT {ECO:0000303|PubMed:18095347};
DE            EC=2.4.1.80 {ECO:0000269|PubMed:18095347};
DE   AltName: Full=Glycosylceramide synthase-A {ECO:0000305};
DE   AltName: Full=UDP-glucose ceramide glucosyltransferase-A;
GN   Name=ugcg-a; Synonyms=ugcg {ECO:0000312|EMBL:AAH89245.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAM49061.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=18095347; DOI=10.1002/dvdy.21406;
RA   Luque M.E., Crespo P.M., Monaco M.E., Aybar M.J., Daniotti J.L.,
RA   Sanchez S.S.;
RT   "Cloning and functional characterization of two key enzymes of
RT   glycosphingolipid biosynthesis in the amphibian Xenopus laevis.";
RL   Dev. Dyn. 237:112-123(2008).
RN   [2] {ECO:0000312|EMBL:AAH89245.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg {ECO:0000312|EMBL:AAH89245.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-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) (PubMed:18095347). Glucosylceramide is
CC       the core component of glycosphingolipids/GSLs, amphipathic molecules
CC       consisting of a ceramide lipid moiety embedded in the outer leaflet of
CC       the membrane, linked to one of hundreds of different externally
CC       oriented oligosaccharide structures. Glycosphingolipids are essential
CC       components of membrane microdomains that mediate membrane trafficking
CC       and signal transduction. They are implicated in many fundamental
CC       cellular processes, including growth, differentiation, migration,
CC       morphogenesis, cell-to-cell and cell-to-matrix interactions
CC       (PubMed:18095347). Glycosphingolipids are required for convergence
CC       extension movements during early development (PubMed:18095347).
CC       Catalyzes the synthesis of xylosylceramide/XylCer (such as beta-D-
CC       xylosyl-(1<->1')-N-acylsphing-4-enine) using UDP-Xyl as xylose donor
CC       (By similarity). {ECO:0000250|UniProtKB:Q16739,
CC       ECO:0000269|PubMed:18095347, ECO:0000303|PubMed:18095347}.
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:18095347};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089;
CC         Evidence={ECO:0000305|PubMed:18095347};
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:0000269|PubMed:18095347}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:18095347}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:Q9R0E0}.
CC   -!- TISSUE SPECIFICITY: At the late gastrula stage, weakly expressed
CC       ubiquitously. As neurulation proceeds (stages 15-16), expression moves
CC       towards the dorsal structures: involuted paraxial mesoderm and neural
CC       folds. In the tailbud embryo (stage 28), expression is restricted to
CC       the notochord. At later stages (stage 35), expression remains in the
CC       notochord and also appears weakly in the cephalic region.
CC       {ECO:0000269|PubMed:18095347}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Expressed at all stages of oogenesis except in previtellogenic oocytes.
CC       During embryogenesis, weakly expressed as early as the one-cell stage
CC       shortly after fertilization, and remains at a relatively uniform level
CC       throughout embryogenesis, persisting at least until stage 35 (early
CC       tadpole). {ECO:0000269|PubMed:18095347}.
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; AY112732; AAM49061.1; -; mRNA.
DR   EMBL; BC089245; AAH89245.1; -; mRNA.
DR   RefSeq; NP_001083944.1; NM_001090475.1.
DR   AlphaFoldDB; Q8AY29; -.
DR   SMR; Q8AY29; -.
DR   SwissLipids; SLP:000000788; -.
DR   CAZy; GT21; Glycosyltransferase Family 21.
DR   DNASU; 399204; -.
DR   GeneID; 399204; -.
DR   KEGG; xla:399204; -.
DR   AGR; Xenbase:XB-GENE-6254211; -.
DR   CTD; 399204; -.
DR   Xenbase; XB-GENE-6254211; ugcg.L.
DR   OrthoDB; 2786173at2759; -.
DR   UniPathway; UPA00222; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 399204; Expressed in intestine and 18 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008120; F:ceramide glucosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046479; P:glycosphingolipid catabolic process; IDA:UniProtKB.
DR   CDD; cd02520; Glucosylceramide_synthase; 1.
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   1: Evidence at protein 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-A"
FT                   /id="PRO_0000376854"
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"
FT   CONFLICT        108
FT                   /note="D -> V (in Ref. 2; AAH89245)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   394 AA;  44651 MW;  D25C6236C6A3388A CRC64;
     MAVLDLALQG LAIFGCVLFF VLWFMHFLSI VYTRLHLNKK ISDKQPYSKL PGVSLLKPLK
     GVDPNLINNL ETFFELDYPK FEILLCVQDL DDPAVDVCKK LLGKYPSDDA 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 PTISWRTGRF RLRCGGTAEE ILDV
//