CEGTA_XENLA
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 03-AUG-2022, entry version 64.
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 CTD; 399204; -.
DR Xenbase; XB-GENE-6254211; ugcg.L.
DR OrthoDB; 793389at2759; -.
DR UniPathway; UPA00222; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 399204; Expressed in intestine and 18 other tissues.
DR GO; GO:0005794; C:Golgi apparatus; IDA: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: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 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 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
