ID   Q80WN6_CRIGR            Unreviewed;       388 AA.
AC   Q80WN6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   04-NOV-2026, entry version 82.
DE   RecName: Full=Beta-1,4-galactosyltransferase {ECO:0000256|RuleBase:RU368121};
DE            Short=Beta-1,4-GalTase {ECO:0000256|RuleBase:RU368121};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:AAM77198.1};
RN   [1] {ECO:0000313|EMBL:AAM77198.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Ovary {ECO:0000313|EMBL:AAM77198.1};
RA   Lee J., Park S.-H., Sundaram S., Shaper N.L., Raju T.S., stanley P.;
RT   "Consequences of the lower expression level of six beta-1,4-
RT   galactosyltransferase transcripts in Lec19 CHO glycosylation mutants.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC       oligosaccharides in many glycoproteins as well as the carbohydrate
CC       moieties of glycolipids. {ECO:0000256|RuleBase:RU368121}.
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         UDP + H(+); 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:0000256|ARBA:ARBA00052889};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31496;
CC         Evidence={ECO:0000256|ARBA:ARBA00052889};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936,
CC         ECO:0000256|RuleBase:RU368121};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC   -!- PATHWAY: Sphingolipid metabolism. {ECO:0000256|ARBA:ARBA00004991}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC       {ECO:0000256|RuleBase:RU368121}. Golgi apparatus, Golgi stack membrane
CC       {ECO:0000256|ARBA:ARBA00004447}; Single-pass type II membrane protein
CC       {ECO:0000256|ARBA:ARBA00004447}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC       {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR   EMBL; AY117539; AAM77198.1; -; mRNA.
DR   RefSeq; NP_001233707.1; NM_001246778.1.
DR   AlphaFoldDB; Q80WN6; -.
DR   SMR; Q80WN6; -.
DR   GeneID; 100689347; -.
DR   KEGG; cge:100689347; -.
DR   CTD; 9334; -.
DR   OrthoDB; 10038994at2759; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008489; F:UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0022010; P:central nervous system myelination; IEA:Ensembl.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IEA:Ensembl.
DR   GO; GO:0001574; P:ganglioside biosynthetic process; IEA:Ensembl.
DR   GO; GO:0009101; P:glycoprotein biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0042551; P:neuron maturation; IEA:Ensembl.
DR   GO; GO:0040019; P:positive regulation of embryonic development; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   CDD; cd00899; b4GalT; 1.
DR   FunFam; 3.90.550.10:FF:000037; Beta-1,4-galactosyltransferase 6; 1.
DR   Gene3D; 3.90.550.10; Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A; 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:SF45; BETA-1,4-GALACTOSYLTRANSFERASE 5; 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   2: Evidence at transcript level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368121};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU368121};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW   ECO:0000256|RuleBase:RU368121};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|RuleBase:RU368121};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368121};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   ECO:0000256|RuleBase:RU368121};
KW   Sphingolipid metabolism {ECO:0000256|ARBA:ARBA00022919};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          114..248
FT                   /note="Galactosyltransferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13733"
FT   DOMAIN          253..330
FT                   /note="Galactosyltransferase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02709"
SQ   SEQUENCE   388 AA;  44932 MW;  60F8FD7754F50ED1 CRC64;
     MRARRGLLRL PRRSLLAALF FFSLSSSLLY FVYVAPGIVN TYLFMVQAQS ILLRDNVRTI
     GAQVYEQVVR SAYAKRNSSL NDSDYPLDLN HSEAFPPTTT FLPEDFTYFA NHPCPERLPS
     MKGPIDINMS EIRMDDIHEL FSRDPAIKLG GHWKPSDCVP RWKVAILIPF RNRHEHLPVL
     LRHLIPMLQR QRLQFAFYVV EQVGTQPFNR AMLFNVGFLE AMKDLDWDCL IFHDVDHIPE
     SDRNYYGCGQ MPRHFATKLD KYMYLLPYAE FFGGVSGLTV EQFQKINGFP NAFWGWGGED
     DDLWNRVQNA GYSVSRPEGD TGKYKSIPHH HRGEVQFLGR YALLRKSKER QGLDGLNNLN
     YFANITYDAL YKNITVNLTP ELAQVTEY
//