CGT1_CAEEL
ID CGT1_CAEEL Reviewed; 466 AA.
AC O18037;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ceramide glucosyltransferase 1;
DE Short=CGT-1 {ECO:0000303|PubMed:19240113, ECO:0000303|PubMed:21325339};
DE EC=2.4.1.80 {ECO:0000269|PubMed:21325339};
GN Name=cgt-1 {ECO:0000312|WormBase:T06C12.10};
GN Synonyms=tag-217 {ECO:0000312|WormBase:T06C12.10};
GN ORFNames=T06C12.10 {ECO:0000312|WormBase:T06C12.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION.
RX PubMed=7651085; DOI=10.1007/bf02537032;
RA Chitwood D.J., Lusby W.R., Thompson M.J., Kochansky J.P., Howarth O.W.;
RT "The glycosylceramides of the nematode Caenorhabditis elegans contain an
RT unusual, branched-chain sphingoid base.";
RL Lipids 30:567-573(1995).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP PATHWAY.
RX PubMed=19240113; DOI=10.1242/jcs.042754;
RA Marza E., Simonsen K.T., Faergeman N.J., Lesa G.M.;
RT "Expression of ceramide glucosyltransferases, which are essential for
RT glycosphingolipid synthesis, is only required in a small subset of C.
RT elegans cells.";
RL J. Cell Sci. 122:822-833(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=21325339; DOI=10.1093/glycob/cwr019;
RA Nomura K.H., Murata D., Hayashi Y., Dejima K., Mizuguchi S.,
RA Kage-Nakadai E., Gengyo-Ando K., Mitani S., Hirabayashi Y., Ito M.,
RA Nomura K.;
RT "Ceramide glucosyltransferase of the nematode Caenorhabditis elegans is
RT involved in oocyte formation and in early embryonic cell division.";
RL Glycobiology 21:834-848(2011).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26115433; DOI=10.1371/journal.pone.0130778;
RA Zhu M., Wu G., Li Y.X., Stevens J.K., Fan C.X., Spang A., Dong M.Q.;
RT "Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a Role in
RT Membrane Trafficking in Caenorhabditis elegans.";
RL PLoS ONE 10:e0130778-e0130778(2015).
RN [6]
RP ERRATUM.
RX PubMed=27631731; DOI=10.1371/journal.pone.0163398;
RA Zhu M., Wu G., Li Y.X., Stevens J.K., Fan C.X., Spang A., Dong M.Q.;
RT "Correction: Serum- and Glucocorticoid-Inducible Kinase-1 (SGK-1) Plays a
RT Role in Membrane Trafficking in Caenorhabditis elegans.";
RL PLoS ONE 11:e0163398-e0163398(2016).
CC -!- FUNCTION: Catalyzes the first glycosylation step in glycosphingolipid
CC biosynthesis, the transfer of glucose to ceramide to produce
CC glucosylceramides (GlcCer). GlcCer are known to contribute to the
CC physical properties and physiological functions of membranes and may
CC regulate signal transduction (PubMed:19240113, PubMed:21325339). Only
CC branched-chain sphingoid bases like 15-methylhexadecasphing-4-enine are
CC used for generating complex sphingolipids in Caenorhabditis elegans
CC (PubMed:7651085). Together with cgt-3, plays a role in the trafficking
CC of proteins such as mig-14 to the cell membrane in intestinal cells
CC (PubMed:26115433). {ECO:0000269|PubMed:19240113,
CC ECO:0000269|PubMed:21325339, ECO:0000269|PubMed:26115433,
CC ECO:0000269|PubMed:7651085}.
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:21325339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089;
CC Evidence={ECO:0000269|PubMed:21325339};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acyl-15-methylhexadecasphing-4-enine + UDP-alpha-D-glucose =
CC H(+) + N-acyl-1-beta-D-glucosyl-15-methylhexadecasphing-4-enine +
CC UDP; Xref=Rhea:RHEA:34611, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:70815, ChEBI:CHEBI:70846;
CC Evidence={ECO:0000305|PubMed:19240113, ECO:0000305|PubMed:21325339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34612;
CC Evidence={ECO:0000305|PubMed:19240113, ECO:0000305|PubMed:21325339};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:19240113, ECO:0000269|PubMed:21325339}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in excretory canals, pharyngeal
CC intestinal valve, intestine and intestinal rectal valve.
CC {ECO:0000305|PubMed:19240113, ECO:0000305|PubMed:21325339}.
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 -!- DISRUPTION PHENOTYPE: Knockdown of cgt-1 alone reduces brood size,
CC while simultaneous knockdown of cgt-3 and cgt-1 results in a larval
CC stage death (L1 lethal) phenotype (PubMed:19240113, PubMed:21325339).
CC Double RNAi-mediated knockdown together with cgt-3 reduces the rate of
CC development and restores the basolateral cell membrane localization of
CC mig-14 in intestinal cells in a sgk-1 ok538 mutant background
CC (PubMed:26115433). {ECO:0000269|PubMed:19240113,
CC ECO:0000269|PubMed:21325339, ECO:0000269|PubMed:26115433}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; BX284605; CAB03296.2; -; Genomic_DNA.
DR PIR; T24561; T24561.
DR RefSeq; NP_506971.2; NM_074570.4.
DR AlphaFoldDB; O18037; -.
DR STRING; 6239.T06C12.10; -.
DR SwissLipids; SLP:000000021; -.
DR CAZy; GT21; Glycosyltransferase Family 21.
DR PaxDb; O18037; -.
DR PRIDE; O18037; -.
DR EnsemblMetazoa; T06C12.10.1; T06C12.10.1; WBGene00011517.
DR GeneID; 188169; -.
DR KEGG; cel:CELE_T06C12.10; -.
DR UCSC; T06C12.10.1; c. elegans.
DR CTD; 188169; -.
DR WormBase; T06C12.10; CE31986; WBGene00011517; cgt-1.
DR eggNOG; KOG2547; Eukaryota.
DR GeneTree; ENSGT00390000012898; -.
DR HOGENOM; CLU_030898_0_0_1; -.
DR InParanoid; O18037; -.
DR OrthoDB; 793389at2759; -.
DR PhylomeDB; O18037; -.
DR UniPathway; UPA00222; -.
DR PRO; PR:O18037; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00011517; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
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; IBA:GO_Central.
DR GO; GO:0102769; F:dihydroceramide glucosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006679; P:glucosylceramide biosynthetic process; IGI:WormBase.
DR GO; GO:0002119; P:nematode larval development; IGI:WormBase.
DR GO; GO:1904508; P:regulation of protein localization to basolateral plasma membrane; IGI:WormBase.
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 Glycosyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..466
FT /note="Ceramide glucosyltransferase 1"
FT /id="PRO_0000421281"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 148
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 200
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 294
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 330..334
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 466 AA; 52416 MW; EBC36C0EF42C5831 CRC64;
MEAANEVVNL FASQATTPSS LDAVTTLETV STPTFIFPEV SDSQILQLMP ATLYSGMNWL
RDHLDGFSLL ALSGCIFVSV LYLVHIIAFF YSIYRLHHKV EPDPTLPGVS VIKPIVGTDK
NLYQNLESFF TSQYHSFELL FCFHSEEDEA IEVVRSLIKK HPNIEAKILF EGEPVGMNPK
VNNMMPAYRA ARYPLVLISD SAIFMRPDGI LDMATTMMSH EKMASVTQIP YCKDRQGFHA
AFEQIFFGTS HARLYLVGNF LGVVCSSGMS SMMKKSALDE CGGMEKFGEY LAEDYFFAKA
LTSRGCKAAI STHPALQNSA SVTVLSFFNR IGRWIKLRIA MMPHLMVVEP LQDCVTSGLI
MAFGLNYLGG YSVYKTFGLH LFYWIVMDFS LMTSMQNGKF NFTPFLFVFI WLFREFTSPF
IFIKAVLAPT IVWRNNKFKL SWGGRIRTSK NSQKVPEAVS LSKGAV
