B4GT6_RAT
ID B4GT6_RAT Reviewed; 382 AA.
AC O88419;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Beta-1,4-galactosyltransferase 6 {ECO:0000305};
DE Short=Beta-1,4-GalTase 6;
DE Short=Beta4Gal-T6;
DE Short=b4Gal-T6;
DE EC=2.4.1.-;
DE AltName: Full=Glucosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.274 {ECO:0000269|PubMed:9593693};
DE AltName: Full=Lactosylceramide synthase {ECO:0000303|PubMed:9593693};
DE Short=LacCer synthase {ECO:0000303|PubMed:9593693};
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 6;
DE AltName: Full=UDP-Gal:glucosylceramide beta-1,4-galactosyltransferase {ECO:0000250|UniProtKB:Q9UBX8};
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 6;
GN Name=B4galt6 {ECO:0000312|RGD:71046};
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], PROTEIN SEQUENCE OF 256-279; 318-336 AND
RP 343-358, FUNCTION AS GLUCOSYLCERAMIDE BETA-1,4-GALACTOSYLTRANSFERASE,
RP CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9593693; DOI=10.1074/jbc.273.22.13570;
RA Nomura T., Takizawa M., Aoki J., Arai H., Inoue K., Wakisaka E.,
RA Yoshizuka N., Imokawa G., Dohmae N., Takio K., Hattori M., Matsuo N.;
RT "Purification, cDNA cloning, and expression of UDP-Gal: glucosylceramide
RT beta-1,4-galactosyltransferase from rat brain.";
RL J. Biol. Chem. 273:13570-13577(1998).
CC -!- FUNCTION: Catalyzes the synthesis of lactosylceramide (LacCer) via the
CC transfer of galactose from UDP-galactose to glucosylceramide (GlcCer)
CC (PubMed:9593693). LacCer is the starting point in the biosynthesis of
CC all gangliosides (membrane-bound glycosphingolipids) which play pivotal
CC roles in the CNS including neuronal maturation and axonal and myelin
CC formation (By similarity). {ECO:0000250|UniProtKB:Q9WVK5,
CC ECO:0000269|PubMed:9593693}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-
CC galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) +
CC H(+) + UDP; Xref=Rhea:RHEA:31495, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17950, ChEBI:CHEBI:22801, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914; EC=2.4.1.274;
CC Evidence={ECO:0000269|PubMed:9593693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496;
CC Evidence={ECO:0000269|PubMed:9593693};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:9593693};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9593693};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:9593693};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:9593693}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2. {ECO:0000269|PubMed:9593693};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- PATHWAY: Sphingolipid metabolism.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein.
CC Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
CC -!- TISSUE SPECIFICITY: Highest expression in brain with lower levels found
CC in lungs, heart, skeletal muscle and kidney. Lowest expression in
CC testis, liver and spleen. {ECO:0000269|PubMed:9593693}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
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DR EMBL; AF048687; AAC24515.1; -; mRNA.
DR RefSeq; NP_113928.1; NM_031740.1.
DR AlphaFoldDB; O88419; -.
DR SMR; O88419; -.
DR STRING; 10116.ENSRNOP00000021764; -.
DR SwissLipids; SLP:000000764; -.
DR CAZy; GT7; Glycosyltransferase Family 7.
DR GlyGen; O88419; 8 sites.
DR PaxDb; O88419; -.
DR PRIDE; O88419; -.
DR Ensembl; ENSRNOT00000111678; ENSRNOP00000082568; ENSRNOG00000015895.
DR GeneID; 65196; -.
DR KEGG; rno:65196; -.
DR CTD; 9331; -.
DR RGD; 71046; B4galt6.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158138; -.
DR InParanoid; O88419; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; O88419; -.
DR TreeFam; TF312834; -.
DR Reactome; R-RNO-2022854; Keratan sulfate biosynthesis.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR Reactome; R-RNO-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR PRO; PR:O88419; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008378; F:galactosyltransferase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; IDA:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0022010; P:central nervous system myelination; ISS:UniProtKB.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISS:UniProtKB.
DR GO; GO:0010706; P:ganglioside biosynthetic process via lactosylceramide; ISS:UniProtKB.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:RGD.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0001572; P:lactosylceramide biosynthetic process; ISO:RGD.
DR GO; GO:0042551; P:neuron maturation; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Sphingolipid metabolism; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..382
FT /note="Beta-1,4-galactosyltransferase 6"
FT /id="PRO_0000080549"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT TRANSMEM 16..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..382
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 163..167
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 202..204
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 229..230
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 230
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 258
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 290
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 292..295
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 323..324
FT /ligand="UDP-alpha-D-galactose"
FT /ligand_id="ChEBI:CHEBI:66914"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 323
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT BINDING 334
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000250|UniProtKB:Q9UBV7"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..152
FT /evidence="ECO:0000250|UniProtKB:P15291"
FT DISULFID 223..242
FT /evidence="ECO:0000250|UniProtKB:P15291"
SQ SEQUENCE 382 AA; 44778 MW; 37C2A32B32D10D51 CRC64;
MSALKRMMRV SNRSLIAFIF FFSLSTSCLY FIYVAPGIAN TYLFMVQARG IMLRENVKTI
GHMIRLYTNK NTTLNGTDYP EGNNTSDYLV QTTTYLPQNF TYSPHLPCPE KLPYMRGFLS
VNVSEISFDE VHQLFSKDSE IEPGGHWRPQ DCKPRWKVAV LIPFRNRHEH LPIFFLHLIP
MLQKQRLEFA FYVIEQTGTQ PFNRAMLFNV GFKEAMKDRA WDCVIFHDVD HLPENDRNYY
GCGEMPRHFA AKLDKYMYIL PYKEFFGGVS GLTVEQFRKI NGFPNAFWGW GGEDDDLWNR
VHYSGYNVTR PEGDLGKYTS IPHHHRGEVQ FLGRYKLLRY SKERQFIDGL NNLLYTPKIL
VDRLYTNISV NLMPELAPVE DY
