CGT_RAT
ID CGT_RAT Reviewed; 541 AA.
AC Q09426;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=2-hydroxyacylsphingosine 1-beta-galactosyltransferase {ECO:0000305};
DE EC=2.4.1.47 {ECO:0000269|PubMed:7694285, ECO:0000269|PubMed:8713090};
DE AltName: Full=Ceramide UDP-galactosyltransferase;
DE Short=CGalT;
DE AltName: Full=Cerebroside synthase;
DE AltName: Full=UDP-galactose-ceramide galactosyltransferase;
DE Flags: Precursor;
GN Name=Ugt8 {ECO:0000312|RGD:3938}; Synonyms=Cgt, Ugt4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7694285; DOI=10.1073/pnas.90.21.10265;
RA Schulte S., Stoffel W.;
RT "Ceramide UDPgalactosyltransferase from myelinating rat brain:
RT purification, cloning, and expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10265-10269(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7521399; DOI=10.1002/jnr.490380214;
RA Stahl N., Jurevics H., Morell P., Suzuki K., Popko B.;
RT "Isolation, characterization, and expression of cDNA clones that encode rat
RT UDP-galactose: ceramide galactosyltransferase.";
RL J. Neurosci. Res. 38:234-242(1994).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION.
RX PubMed=8713090; DOI=10.1042/bj3170589;
RA van der Bijl P., Strous G.J., Lopes-Cardozo M., Thomas-Oates J.,
RA van Meer G.;
RT "Synthesis of non-hydroxy-galactosylceramides and galactosyldiglycerides by
RT hydroxy-ceramide galactosyltransferase.";
RL Biochem. J. 317:589-597(1996).
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 (PubMed:8713090). {ECO:0000269|PubMed:7694285,
CC ECO:0000269|PubMed:8713090}.
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:0000269|PubMed:7694285, ECO:0000269|PubMed:8713090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13094;
CC Evidence={ECO:0000305|PubMed:8713090};
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:0000269|PubMed:8713090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43401;
CC Evidence={ECO:0000305|PubMed:8713090};
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:0000269|PubMed:8713090};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43405;
CC Evidence={ECO:0000305|PubMed:8713090};
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:0000269|PubMed:7694285, ECO:0000269|PubMed:8713090}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:8713090}.
CC -!- TISSUE SPECIFICITY: Brain, restricted to the oligodendrocyte-containing
CC cell layers of cerebrum and cerebellum.
CC -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; L21698; AAA16108.1; -; mRNA.
DR EMBL; U07683; AAA50212.1; -; mRNA.
DR PIR; A48801; A48801.
DR RefSeq; NP_062149.1; NM_019276.3.
DR RefSeq; XP_017446541.1; XM_017591052.1.
DR AlphaFoldDB; Q09426; -.
DR SMR; Q09426; -.
DR STRING; 10116.ENSRNOP00000012676; -.
DR SwissLipids; SLP:000000910; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR GlyGen; Q09426; 3 sites.
DR iPTMnet; Q09426; -.
DR PaxDb; Q09426; -.
DR PRIDE; Q09426; -.
DR Ensembl; ENSRNOT00000012676; ENSRNOP00000012676; ENSRNOG00000009345.
DR GeneID; 50555; -.
DR KEGG; rno:50555; -.
DR UCSC; RGD:3938; rat.
DR CTD; 7368; -.
DR RGD; 3938; Ugt8.
DR eggNOG; KOG1192; Eukaryota.
DR GeneTree; ENSGT00940000156545; -.
DR HOGENOM; CLU_012949_3_1_1; -.
DR InParanoid; Q09426; -.
DR OMA; WKYEGSA; -.
DR OrthoDB; 508327at2759; -.
DR PhylomeDB; Q09426; -.
DR TreeFam; TF315472; -.
DR Reactome; R-RNO-1660662; Glycosphingolipid metabolism.
DR UniPathway; UPA00787; -.
DR PRO; PR:Q09426; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000009345; Expressed in cerebellum and 12 other tissues.
DR Genevisible; Q09426; RN.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003851; F:2-hydroxyacylsphingosine 1-beta-galactosyltransferase activity; IDA:UniProtKB.
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; IMP:RGD.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; TAS:RGD.
DR GO; GO:0042552; P:myelination; TAS:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0030913; P:paranodal junction assembly; ISO:RGD.
DR GO; GO:0002175; P:protein localization to paranode region of axon; ISO:RGD.
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_0000036066"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:7694285"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:7694285"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 541 AA; 61126 MW; 260D7603170151BB CRC64;
MKSYTPYFML LWSAVGIARA AKIIIVPPIM FESHLYIFKT LASALHERGH HTVFLLSEGR
DIDPSNHYSL QRYPGIFNST TSDAFLQSKM RNIFSGRLTA VELVDILDHY TKNCDMMVGN
QALIQGLKKE KFDLLLVDPN DMCGFVIAHL LGVKYAVFST GLWYPAEVGA PAPLAYVPEF
NSLLTDRMNF LERMKNTGVY LISRMGVSFL VLPKYERIMQ KYNLLPAKSM YDLVHGSSLW
MLCTDVALEF PRPTLPNVVY VGGILTKPAS PLPEDLQRWV DGAQEHGFVL VSFGAGVKYL
SEDIANKLAG ALGRLPQKVI WRFSGTKPKN LGNNTKLIEW LPQNDLLGHS NIRAFLSHGG
LNSIFETMYH GVPVVGIPLF GDHYDTMTRV QAKGMGILLE WNTVTEGELY DALVKVINNP
SYRQRAQKLS EIHKDQPGHP VNRTTYWIDY ILRHDGAHHL RSAVHQISFC QYFLLDIAFV
LLLGAVALYF IVSYVTKFIY RKVKSLCSRS THSTVNGHYQ NGILNGRYKG NGHIKHEKKV
K
