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   24-JAN-2024, entry version 140.
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.ENSRNOP00000075106; -.
DR   SwissLipids; SLP:000000764; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyCosmos; O88419; 8 sites, No reported glycans.
DR   GlyGen; O88419; 8 sites.
DR   PhosphoSitePlus; O88419; -.
DR   PaxDb; 10116-ENSRNOP00000021764; -.
DR   Ensembl; ENSRNOT00000111678.1; ENSRNOP00000082568.1; ENSRNOG00000015895.8.
DR   Ensembl; ENSRNOT00055031163; ENSRNOP00055025125; ENSRNOG00055018341.
DR   Ensembl; ENSRNOT00060021366; ENSRNOP00060016865; ENSRNOG00060012590.
DR   Ensembl; ENSRNOT00065025162; ENSRNOP00065019702; ENSRNOG00065015185.
DR   GeneID; 65196; -.
DR   KEGG; rno:65196; -.
DR   AGR; RGD:71046; -.
DR   CTD; 9331; -.
DR   RGD; 71046; B4galt6.
DR   eggNOG; KOG3916; Eukaryota.
DR   GeneTree; ENSGT00940000158138; -.
DR   InParanoid; O88419; -.
DR   OMA; VVWDCII; -.
DR   OrthoDB; 306273at2759; -.
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: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   CDD; cd00899; b4GalT; 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; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR19300:SF47; BETA-1,4-GALACTOSYLTRANSFERASE 6; 1.
DR   Pfam; PF02709; Glyco_transf_7C; 1.
DR   Pfam; PF13733; Glyco_transf_7N; 1.
DR   PRINTS; PR02050; B14GALTRFASE.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 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
//