ID M3YS48_MUSPF Unreviewed; 396 AA.
AC M3YS48;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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};
GN Name=B4GALT3 {ECO:0000313|Ensembl:ENSMPUP00000014158.1,
GN ECO:0000313|RefSeq:XP_012902969.1, ECO:0000313|RefSeq:XP_012902973.1,
GN ECO:0000313|RefSeq:XP_012902974.1, ECO:0000313|RefSeq:XP_012902976.1,
GN ECO:0000313|RefSeq:XP_044942503.1, ECO:0000313|RefSeq:XP_044942504.1,
GN ECO:0000313|RefSeq:XP_044942505.1, ECO:0000313|RefSeq:XP_044942506.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000014158.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000014158.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_012902969.1, ECO:0000313|RefSeq:XP_012902973.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_012902969.1,
RC ECO:0000313|RefSeq:XP_012902973.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00037536,
CC ECO:0000256|RuleBase:RU368121}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-D-glucosamine + UDP-alpha-D-galactose = beta-D-
CC galactosyl-(1->4)-N-acetyl-D-glucosamine + H(+) + UDP;
CC Xref=Rhea:RHEA:17745, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:60152, ChEBI:CHEBI:66914, ChEBI:CHEBI:506227;
CC EC=2.4.1.90; Evidence={ECO:0000256|ARBA:ARBA00036701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000256|ARBA:ARBA00036701};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-
CC Cer(d18:1(4E)) + UDP-alpha-D-galactose = a neolactoside
CC nLc4Cer(d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:31499,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17006, ChEBI:CHEBI:17103,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.275;
CC Evidence={ECO:0000256|ARBA:ARBA00035795};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000256|ARBA:ARBA00035795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-
CC galactose = beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-
CC beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + H(+)
CC + UDP; Xref=Rhea:RHEA:62548, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:90357, ChEBI:CHEBI:144378;
CC Evidence={ECO:0000256|ARBA:ARBA00036434};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC Evidence={ECO:0000256|ARBA:ARBA00036434};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl
CC derivative + H(+) + UDP; Xref=Rhea:RHEA:22932, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:61631, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:133507; EC=2.4.1.38;
CC Evidence={ECO:0000256|ARBA:ARBA00035817};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000256|ARBA:ARBA00035817};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = a beta-D-
CC galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(+) + UDP;
CC Xref=Rhea:RHEA:62552, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:79208, ChEBI:CHEBI:83264;
CC Evidence={ECO:0000256|ARBA:ARBA00043774};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC Evidence={ECO:0000256|ARBA:ARBA00043774};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|RuleBase:RU368121};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR EMBL; AEYP01088008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004775973.1; XM_004775916.2.
DR RefSeq; XP_004775979.1; XM_004775922.2.
DR RefSeq; XP_012902969.1; XM_013047515.2.
DR RefSeq; XP_012902970.1; XM_013047516.1.
DR RefSeq; XP_012902971.1; XM_013047517.1.
DR RefSeq; XP_012902972.1; XM_013047518.1.
DR RefSeq; XP_012902973.1; XM_013047519.2.
DR RefSeq; XP_012902974.1; XM_013047520.2.
DR RefSeq; XP_012902975.1; XM_013047521.1.
DR RefSeq; XP_012902976.1; XM_013047522.2.
DR RefSeq; XP_044942503.1; XM_045086568.1.
DR RefSeq; XP_044942504.1; XM_045086569.1.
DR RefSeq; XP_044942505.1; XM_045086570.1.
DR RefSeq; XP_044942506.1; XM_045086571.1.
DR STRING; 9669.ENSMPUP00000014158; -.
DR Ensembl; ENSMPUT00000014384.1; ENSMPUP00000014158.1; ENSMPUG00000014266.1.
DR GeneID; 101673173; -.
DR KEGG; mpuf:101673173; -.
DR CTD; 8703; -.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000158549; -.
DR HOGENOM; CLU_044391_1_2_1; -.
DR OMA; CDPGGPR; -.
DR OrthoDB; 306273at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008378; F:galactosyltransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006682; P:galactosylceramide biosynthetic process; IEA:Ensembl.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
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:SF33; BETA-1,4-GALACTOSYLTRANSFERASE 3; 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 3: Inferred from homology;
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 metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Manganese {ECO:0000256|RuleBase:RU368121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|RuleBase:RU368121};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW ECO:0000256|RuleBase:RU368121};
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 80..213
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 218..295
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
FT REGION 341..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 396 AA; 44170 MW; 01473AD6EE156060 CRC64;
MLRRLLERPC TLALLVGSQL AVMMYLSLGG FRSLSALFGR EQGPTFDYSH PHDVYSNLSH
LPGAPVAPGA PPAPQGLPYC PERSPLLVGP VSVSFSPVPS LAEIAERNPR VEPGGRYRPA
GCEPRSRTAI IVPHRAREHH LRLLLYHLHP FLQRQQLAYG IYVIHQAGNG TFNRAKLLNV
GVREALRDEE WDCLFLHDVD LLPENDHNLY VCDPRGPRHV AVAMNKFGYS LPYPQYFGGV
SALTPDQYLK MNGFPNEYWG WGGEDDDIAT RVRLAGMKIS RPPTSVGHYK MVKHRGDKGN
EENPHRFDLL VRTQNSWTQD GMNSLTYRLL ARELGPLYTN ITADIGTDPR GPRTPSGPRY
PPGSSQAFRQ EMLQRRPPAR PGPPPTANHT APNGSH
//
