ID CGT2_CAEEL Reviewed; 443 AA.
AC G5EC84;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Ceramide glucosyltransferase 2;
DE Short=CGT-2 {ECO:0000303|PubMed:19240113, ECO:0000303|PubMed:21325339};
DE EC=2.4.1.80 {ECO:0000269|PubMed:21325339};
GN Name=cgt-2; ORFNames=F20B4.6;
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 [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11443131; DOI=10.1074/jbc.m104952200;
RA Leipelt M., Warnecke D., Zahringer U., Ott C., Muller F., Hube B.,
RA Heinz E.;
RT "Glucosylceramide synthases, a gene family responsible for the biosynthesis
RT of glucosphingolipids in animals, plants, and fungi.";
RL J. Biol. Chem. 276:33621-33629(2001).
RN [2]
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 [3]
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 [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND 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 [5]
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).
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:11443131, PubMed:19240113,
CC PubMed:21325339). Only branched-chain sphingoid bases like 15-
CC methylhexadecasphing-4-enine are used for generating complex
CC sphingolipids in Caenorhabditis elegans (PubMed:7651085).
CC {ECO:0000269|PubMed:11443131, ECO:0000269|PubMed:19240113,
CC ECO:0000269|PubMed:21325339, 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:11443131, ECO:0000269|PubMed:21325339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12089;
CC Evidence={ECO:0000269|PubMed:11443131, 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:11443131, ECO:0000305|PubMed:19240113,
CC ECO:0000305|PubMed:21325339};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34612;
CC Evidence={ECO:0000305|PubMed:11443131, ECO:0000305|PubMed:19240113,
CC ECO:0000305|PubMed:21325339};
CC -!- PATHWAY: Lipid metabolism; sphingolipid metabolism.
CC {ECO:0000269|PubMed:19240113, ECO:0000269|PubMed:21325339,
CC ECO:0000305|PubMed:11443131}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed mostly in intestine and vulva.
CC {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: Reduced brood size.
CC {ECO:0000269|PubMed:21325339}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; AF364401; AAK73018.1; -; mRNA.
DR EMBL; FO081185; CCD69753.1; -; Genomic_DNA.
DR PIR; T28827; T28827.
DR RefSeq; NP_510857.2; NM_078456.4.
DR AlphaFoldDB; G5EC84; -.
DR BioGRID; 46661; 2.
DR STRING; 6239.F20B4.6.1; -.
DR SwissLipids; SLP:000000022; -.
DR CAZy; GT21; Glycosyltransferase Family 21.
DR PaxDb; 6239-F20B4-6; -.
DR PeptideAtlas; G5EC84; -.
DR EnsemblMetazoa; F20B4.6.1; F20B4.6.1; WBGene00017625.
DR EnsemblMetazoa; F20B4.6.2; F20B4.6.2; WBGene00017625.
DR GeneID; 181790; -.
DR KEGG; cel:CELE_F20B4.6; -.
DR AGR; WB:WBGene00017625; -.
DR WormBase; F20B4.6; CE30960; WBGene00017625; cgt-2.
DR eggNOG; KOG2547; Eukaryota.
DR GeneTree; ENSGT00390000012898; -.
DR HOGENOM; CLU_030898_0_0_1; -.
DR InParanoid; G5EC84; -.
DR OrthoDB; 2786173at2759; -.
DR PhylomeDB; G5EC84; -.
DR Reactome; R-CEL-9840309; Glycosphingolipid biosynthesis.
DR UniPathway; UPA00222; -.
DR PRO; PR:G5EC84; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017625; Expressed in adult organism and 2 other cell types or tissues.
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; IBA:GO_Central.
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 Glycosyltransferase; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..443
FT /note="Ceramide glucosyltransferase 2"
FT /id="PRO_0000421282"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 139
FT /note="D1"
FT /evidence="ECO:0000305"
FT MOTIF 191
FT /note="D2"
FT /evidence="ECO:0000305"
FT MOTIF 285
FT /note="D3"
FT /evidence="ECO:0000305"
FT MOTIF 321..325
FT /note="(Q/R)XXRW"
FT /evidence="ECO:0000305"
FT ACT_SITE 285
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9R0E0"
SQ SEQUENCE 443 AA; 50121 MW; 2690419210CA6C93 CRC64;
MGDKITGLEV EIIPEISEVQ PESLQEQNAS SLYYPLFSQY IPLLLTGTKK ILEDIDYCTC
FAVFGVVFVS ALYFLHIVGL CYGKYRLHRP TKPNPSLPGV SIIKPIIGAD ANLYTNLETF
FTTQYHKFEL LFCFDRSDDP AVKVVESLVK KYPSVDSTMF FGGEKIGLNP KINNMMPAYR
IAKYQLIMIS DSGIFMKSDA VLDMASTMMS HETMALVTQT PYCKDRKGFA SVFEQIYFGT
SHARIYLAGN CLQFNCPTGM SSMMKKEALD ECGGFAAFSG YLAEDYFFGK KLASRGYKSG
ISTHPALQNS AAVTMTSFTD RVCRWVKLRM AMMPQIIFVE PLQDCFPSAL IISFSLNYIA
NIDMLTTIML HVVFWITMDC MVMCKMQNKK MSFSPLKFLL IWLLRELFAP LVFIKAALDP
SIRWRDNVFH LAWGGKIRSQ TSI
//
