B4GT1_RAT
ID B4GT1_RAT Reviewed; 32 AA.
AC P80225;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 23-FEB-2022, entry version 92.
DE RecName: Full=Beta-1,4-galactosyltransferase 1 {ECO:0000305};
DE Short=Beta-1,4-GalTase 1;
DE Short=Beta4Gal-T1;
DE Short=b4Gal-T1;
DE EC=2.4.1.-;
DE AltName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase;
DE AltName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase;
DE EC=2.4.1.38;
DE AltName: Full=Lactose synthase A protein;
DE EC=2.4.1.22;
DE AltName: Full=N-acetyllactosamine synthase;
DE EC=2.4.1.90;
DE AltName: Full=Nal synthase;
DE AltName: Full=Neolactotriaosylceramide beta-1,4-galactosyltransferase;
DE EC=2.4.1.275 {ECO:0000250|UniProtKB:P08037};
DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1;
DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1;
DE Flags: Fragments;
GN Name=B4galt1 {ECO:0000312|RGD:620900}; Synonyms=Ggtb2;
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 PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=8375379; DOI=10.1111/j.1432-1033.1993.tb18158.x;
RA Bendiak B., Ward L.D., Simpson R.J.;
RT "Proteins of the Golgi apparatus. Purification to homogeneity, N-terminal
RT sequence, and unusually large Stokes radius of the membrane-bound form of
RT UDP-galactose:N-acetylglucosamine beta 1-4galactosyltransferase from rat
RT liver.";
RL Eur. J. Biochem. 216:405-417(1993).
CC -!- FUNCTION: This protein is responsible for the synthesis of complex-type
CC N-linked oligosaccharides in many glycoproteins as well as the
CC carbohydrate moieties of glycolipids. {ECO:0000250|UniProtKB:P08037}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP;
CC Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405;
CC Evidence={ECO:0000250|UniProtKB:P08037};
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:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933;
CC Evidence={ECO:0000250|UniProtKB:P08037};
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:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746;
CC Evidence={ECO:0000250|UniProtKB:P08037};
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:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31500;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucosylceramide + UDP-alpha-D-galactose = 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:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62553;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a neolactoside IV(3)-beta-GlcNAc-nLc4Cer + UDP-alpha-D-
CC galactose = beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-
CC (1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-
CC beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1')-ceramide + 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:0000250|UniProtKB:P08037};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62549;
CC Evidence={ECO:0000250|UniProtKB:P08037};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P15291};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250|UniProtKB:P15535}; Single-pass type II membrane protein.
CC Secreted {ECO:0000250|UniProtKB:P08037}. Cell membrane
CC {ECO:0000250|UniProtKB:P08037}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:P08037}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:P15535}. Note=Membrane-bound form in trans
CC cisternae of Golgi. Secreted into the body fluid.
CC {ECO:0000250|UniProtKB:P15535}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S36825; S36825.
DR UCSC; RGD:620900; rat.
DR RGD; 620900; B4galt1.
DR BRENDA; 2.4.1.133; 5301.
DR BRENDA; 2.4.1.38; 5301.
DR SABIO-RK; P80225; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0030057; C:desmosome; ISO:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000138; C:Golgi trans cisterna; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
DR GO; GO:0008378; F:galactosyltransferase activity; ISO:RGD.
DR GO; GO:0004461; F:lactose synthase activity; ISO:RGD.
DR GO; GO:0030145; F:manganese ion binding; ISO:RGD.
DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISO:RGD.
DR GO; GO:0035250; F:UDP-galactosyltransferase activity; ISO:RGD.
DR GO; GO:0002526; P:acute inflammatory response; ISO:RGD.
DR GO; GO:0060055; P:angiogenesis involved in wound healing; ISO:RGD.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR GO; GO:0045136; P:development of secondary sexual characteristics; ISO:RGD.
DR GO; GO:0002064; P:epithelial cell development; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0006012; P:galactose metabolic process; ISO:RGD.
DR GO; GO:0009101; P:glycoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0005989; P:lactose biosynthetic process; ISO:RGD.
DR GO; GO:0050900; P:leukocyte migration; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISO:RGD.
DR GO; GO:0007341; P:penetration of zona pellucida; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; ISO:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISO:RGD.
DR GO; GO:0006487; P:protein N-linked glycosylation; ISO:RGD.
DR GO; GO:0060046; P:regulation of acrosome reaction; ISO:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0042060; P:wound healing; ISO:RGD.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Direct protein sequencing;
KW Glycosyltransferase; Golgi apparatus; Lipid metabolism; Manganese;
KW Membrane; Metal-binding; Reference proteome; Secreted; Transferase.
FT CHAIN 1..>32
FT /note="Beta-1,4-galactosyltransferase 1"
FT /id="PRO_0000080531"
FT NON_CONS 15..16
FT /evidence="ECO:0000305"
FT NON_TER 32
SQ SEQUENCE 32 AA; 3137 MW; F58B846F5DCB297F CRC64;
PGATLQXAXX LLVAVXAXPP PPLGVXPKPX PG
