CGT_MOUSE
ID CGT_MOUSE Reviewed; 541 AA.
AC Q64676; Q61634; Q91W57;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=2-hydroxyacylsphingosine 1-beta-galactosyltransferase {ECO:0000305};
DE EC=2.4.1.47 {ECO:0000250|UniProtKB:Q09426};
DE AltName: Full=Ceramide UDP-galactosyltransferase;
DE AltName: Full=Cerebroside synthase;
DE AltName: Full=UDP-galactose-ceramide galactosyltransferase;
DE Flags: Precursor;
GN Name=Ugt8 {ECO:0000312|EMBL:AAC53576.1}; Synonyms=Cgt, Ugt4, Ugt8a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8661123; DOI=10.1006/geno.1996.0341;
RA Coetzee T., Li X., Fujita N., Marcus J., Suzuki K., Francke U., Popko B.;
RT "Molecular cloning, chromosomal mapping, and characterization of the mouse
RT UDP-galactose:ceramide galactosyltransferase gene.";
RL Genomics 35:215-222(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=BALB/cJ; TISSUE=Leukocyte;
RX PubMed=8661124; DOI=10.1006/geno.1996.0342;
RA Bosio A., Binczek E., Stoffel W.;
RT "Molecular cloning and characterization of the mouse CGT gene encoding UDP-
RT galactose ceramide-galactosyltransferase (cerebroside synthetase).";
RL Genomics 35:223-226(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the transfer of galactose to ceramide, a key
CC enzymatic step in the biosynthesis of galactocerebrosides, which are
CC abundant sphingolipids of the myelin membrane of the central nervous
CC system and peripheral nervous system. Galactosylates both hydroxy- and
CC non-hydroxy fatty acid-containing ceramides and diglycerides.
CC {ECO:0000250|UniProtKB:Q09426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-
CC galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + UDP;
CC Xref=Rhea:RHEA:13093, ChEBI:CHEBI:15378, ChEBI:CHEBI:18390,
CC ChEBI:CHEBI:52639, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.47;
CC Evidence={ECO:0000250|UniProtKB:Q09426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13094;
CC Evidence={ECO:0000250|UniProtKB:Q09426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(2-hydroxy-hexanoyl)-sphing-4-enine + UDP-alpha-D-galactose
CC = H(+) + N-(2-hydroxy-hexanoyl)-beta-D-galactosyl-sphing-4-enine +
CC UDP; Xref=Rhea:RHEA:43400, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:83244, ChEBI:CHEBI:83246;
CC Evidence={ECO:0000250|UniProtKB:Q09426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43401;
CC Evidence={ECO:0000250|UniProtKB:Q09426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-(2-hydroxy-hexanoyl)-sphinganine + UDP-alpha-D-galactose =
CC H(+) + N-(2-hydroxyhexanoyl)-beta-D-galactosylsphinganine + UDP;
CC Xref=Rhea:RHEA:43404, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:83248, ChEBI:CHEBI:83257;
CC Evidence={ECO:0000250|UniProtKB:Q09426};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43405;
CC Evidence={ECO:0000250|UniProtKB:Q09426};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-sphingoid base + UDP-alpha-D-galactose = a D-
CC galactosylceramide + H(+) + UDP; Xref=Rhea:RHEA:48344,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36498, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:83273;
CC Evidence={ECO:0000250|UniProtKB:Q16880};
CC -!- PATHWAY: Sphingolipid metabolism; galactosylceramide biosynthesis.
CC {ECO:0000250|UniProtKB:Q09426}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q09426}; Single-
CC pass membrane protein {ECO:0000250|UniProtKB:Q09426}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:Q09426}.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; U48896; AAC53576.1; -; Genomic_DNA.
DR EMBL; U48892; AAC53576.1; JOINED; Genomic_DNA.
DR EMBL; U48893; AAC53576.1; JOINED; Genomic_DNA.
DR EMBL; U48894; AAC53576.1; JOINED; Genomic_DNA.
DR EMBL; X92122; CAA63090.1; -; mRNA.
DR EMBL; X92123; CAA63091.1; -; Genomic_DNA.
DR EMBL; X92124; CAA63091.1; JOINED; Genomic_DNA.
DR EMBL; X92125; CAA63091.1; JOINED; Genomic_DNA.
DR EMBL; X92126; CAA63091.1; JOINED; Genomic_DNA.
DR EMBL; X92177; CAA63091.1; JOINED; Genomic_DNA.
DR EMBL; AK137364; BAE23325.1; -; mRNA.
DR EMBL; BC016885; AAH16885.1; -; mRNA.
DR CCDS; CCDS17821.1; -.
DR RefSeq; NP_035804.2; NM_011674.4.
DR RefSeq; XP_006501372.2; XM_006501309.3.
DR RefSeq; XP_006501373.1; XM_006501310.3.
DR AlphaFoldDB; Q64676; -.
DR SMR; Q64676; -.
DR STRING; 10090.ENSMUSP00000050852; -.
DR BindingDB; Q64676; -.
DR ChEMBL; CHEMBL4739858; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyConnect; 2096; 10 N-Linked glycans (1 site).
DR GlyGen; Q64676; 3 sites, 10 N-linked glycans (1 site).
DR iPTMnet; Q64676; -.
DR PhosphoSitePlus; Q64676; -.
DR SwissPalm; Q64676; -.
DR jPOST; Q64676; -.
DR MaxQB; Q64676; -.
DR PaxDb; Q64676; -.
DR PeptideAtlas; Q64676; -.
DR PRIDE; Q64676; -.
DR ProteomicsDB; 283900; -.
DR Antibodypedia; 2809; 218 antibodies from 31 providers.
DR DNASU; 22239; -.
DR Ensembl; ENSMUST00000057944; ENSMUSP00000050852; ENSMUSG00000032854.
DR Ensembl; ENSMUST00000198610; ENSMUSP00000143605; ENSMUSG00000032854.
DR GeneID; 22239; -.
DR KEGG; mmu:22239; -.
DR UCSC; uc008rfy.1; mouse.
DR CTD; 22239; -.
DR MGI; MGI:109522; Ugt8a.
DR VEuPathDB; HostDB:ENSMUSG00000032854; -.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000156545; -.
DR HOGENOM; CLU_012949_3_1_1; -.
DR InParanoid; Q64676; -.
DR OMA; WKYEGSA; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q64676; -.
DR TreeFam; TF315472; -.
DR Reactome; R-MMU-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00787; -.
DR BioGRID-ORCS; 22239; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Ugt8a; mouse.
DR PRO; PR:Q64676; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q64676; protein.
DR Bgee; ENSMUSG00000032854; Expressed in cerebellar nuclear complex and 157 other tissues.
DR Genevisible; Q64676; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003851; F:2-hydroxyacylsphingosine 1-beta-galactosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008120; F:ceramide glucosyltransferase activity; TAS:MGI.
DR GO; GO:0047263; F:N-acylsphingosine galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; IMP:BHF-UCL.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009247; P:glycolipid biosynthetic process; TAS:MGI.
DR GO; GO:0042552; P:myelination; TAS:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030913; P:paranodal junction assembly; IMP:BHF-UCL.
DR GO; GO:0002175; P:protein localization to paranode region of axon; IMP:BHF-UCL.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR InterPro; IPR035595; UDP_glycos_trans_CS.
DR Pfam; PF00201; UDPGT; 1.
DR PROSITE; PS00375; UDPGT; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Lipid metabolism;
KW Membrane; Reference proteome; Signal; Sphingolipid metabolism; Transferase;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..541
FT /note="2-hydroxyacylsphingosine 1-beta-
FT galactosyltransferase"
FT /id="PRO_0000036065"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 518..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 335
FT /note="T -> S (in Ref. 1; AAC53576)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="R -> H (in Ref. 2; CAA63090/CAA63091)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="E -> K (in Ref. 2; CAA63090/CAA63091)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="R -> P (in Ref. 2; CAA63090/CAA63091)"
FT /evidence="ECO:0000305"
FT CONFLICT 533..534
FT /note="RV -> HI (in Ref. 2; CAA63090/CAA63091)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="R -> K (in Ref. 2; CAA63090/CAA63091)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 61249 MW; 0E3436597F8810D0 CRC64;
MKSYTPYFML LWSAVGIARA AKIIIVPPIM FESHLYIFKT LASALHERGH HTVLLLSEGR
DIAPSNHYSL QRYPGIFNST TSDAFLQSKM RNIFSGRLTA VELVDILDHY TKNCDMMVGN
QALIQGLKKE KFDLLLVDPN DMCGFVIAHL LGVKYAVFST GLWYPAEVGA PAPLAYVPEF
NSLLTDRMNF LERMKNTGVY LISRIGVSFL VLPKYERIMQ KYNLLPAKSM YDLVHGSSLW
MLCTDVALEF PRPTLPNVVY VGGILTKPAS PLPEDLQRWV SGAQEHGFVL VSFGAGVKYL
SEDIANKLAG ALGRLPQKVI WRFSGTKPKN LGNNTKLIEW LPQNDLLGHS NIRAFLSHGG
LNSIFETMYH GVPVVGIPLF GDHYDTMTRV QAKGMGILLE WNTVTEGELY DALVKVINNP
SYRQRAQKLS EIHKDQPGHP VNRTTYWIDY ILRHDGARHL RSAVHQISFC QYFLLDIAFV
LLLGAVLLYF ILSYVTKFIY RKIKSLWSKN EHSTVNGHYQ NGIRNGKYKG NGRVKHEKKV
R
