ID B4GT1_BOVIN Reviewed; 402 AA. AC P08037; Q0VC05; Q8MIG0; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 16-JUN-2009, entry version 107. DE RecName: Full=Beta-1,4-galactosyltransferase 1; DE Short=Beta-1,4-GalTase 1; DE Short=Beta4Gal-T1; DE Short=b4Gal-T1; DE EC=2.4.1.-; DE AltName: Full=UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 1; DE AltName: Full=UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 1; DE Includes: DE RecName: Full=Lactose synthase A protein; DE EC=2.4.1.22; DE Includes: DE RecName: Full=N-acetyllactosamine synthase; DE EC=2.4.1.90; DE AltName: Full=Nal synthetase; DE Includes: DE RecName: Full=Beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase; DE EC=2.4.1.38; DE Includes: DE RecName: Full=Beta-N-acetylglucosaminyl-glycolipid beta-1,4-galactosyltransferase; DE EC=2.4.1.-; DE Contains: DE RecName: Full=Processed beta-1,4-galactosyltransferase 1; GN Name=B4GALT1; Synonyms=GALT, GGTB2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=89325338; PubMed=2502398; RX DOI=10.1111/j.1432-1033.1989.tb14915.x; RA D'Agostaro G., Bendiak B., Tropak M.; RT "Cloning of cDNA encoding the membrane-bound form of bovine beta 1,4- RT galactosyltransferase."; RL Eur. J. Biochem. 183:211-217(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Fetal skin; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 69-402. RX MEDLINE=86149345; PubMed=2419911; DOI=10.1073/pnas.83.6.1573; RA Shaper N.L., Shaper J.H., Meuth J.L., Fox J.L., Chang H., Kirsch I.R., RA Hollis G.F.; RT "Bovine galactosyltransferase: identification of a clone by direct RT immunological screening of a cDNA expression library."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1573-1577(1986). RN [4] RP NUCLEOTIDE SEQUENCE OF 74-402. RX MEDLINE=86259669; PubMed=3014508; DOI=10.1073/pnas.83.13.4720; RA Narimatsu H., Sinha S., Brew K., Okayama H., Qasba P.K.; RT "Cloning and sequencing of cDNA of bovine N-acetylglucosamine (beta 1- RT 4)galactosyltransferase."; RL Proc. Natl. Acad. Sci. U.S.A. 83:4720-4724(1986). RN [5] RP SEQUENCE REVISION TO 164; 256 AND 265. RA Qasba P.K., Narimatsu H., Masibay A.S.; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-77. RX MEDLINE=89345541; PubMed=2503823; DOI=10.1073/pnas.86.15.5733; RA Masibay A.S., Qasba P.K.; RT "Expression of bovine beta-1,4-galactosyltransferase cDNA in COS-7 RT cells."; RL Proc. Natl. Acad. Sci. U.S.A. 86:5733-5737(1989). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-165. RX MEDLINE=90153986; PubMed=2105947; RA Russo R.N., Shaper N.L., Shaper J.H.; RT "Bovine beta 1-->4-galactosyltransferase: two sets of mRNA transcripts RT encode two forms of the protein with different amino-terminal domains. RT In vitro translation experiments demonstrate that both the short and RT the long forms of the enzyme are type II membrane-bound RT glycoproteins."; RL J. Biol. Chem. 265:3324-3331(1990). RN [8] RP PARTIAL PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-90. RX MEDLINE=90354395; PubMed=2117606; RA Yadav S.P., Brew K.; RT "Identification of a region of UDP-galactose:N-acetylglucosamine beta RT 4-galactosyltransferase involved in UDP-galactose binding by RT differential labeling."; RL J. Biol. Chem. 265:14163-14169(1990). RN [9] RP DISULFIDE BOND. RX MEDLINE=91093259; PubMed=1898734; RA Yadav S.P., Brew K.; RT "Structure and function in galactosyltransferase. Sequence locations RT of alpha-lactalbumin binding site, thiol groups, and disulfide bond."; RL J. Biol. Chem. 266:698-703(1991). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 115-402 IN COMPLEX WITH RP SUBSTRATE, AND DISULFIDE BONDS. RX MEDLINE=99321743; PubMed=10393171; DOI=10.1093/emboj/18.13.3546; RA Gastinel L.N., Cambillau C., Bourne Y.; RT "Crystal structures of the bovine beta4galactosyltransferase catalytic RT domain and its complex with uridine diphosphogalactose."; RL EMBO J. 18:3546-3557(1999). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 117-402 IN COMPLEX WITH RP SUBSTRATE AND MANGANESE IONS. RX MEDLINE=21313625; PubMed=11419947; DOI=10.1006/jmbi.2001.4757; RA Ramakrishnan B., Qasba P.K.; RT "Crystal structure of lactose synthase reveals a large conformational RT change in its catalytic component, the beta1,4-galactosyltransferase- RT I."; RL J. Mol. Biol. 310:205-218(2001). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 117-402 IN COMPLEX WITH RP SUBSTRATE AND MANGANESE IONS. RX MEDLINE=22047859; PubMed=12051854; DOI=10.1016/S0022-2836(02)00020-7; RA Ramakrishnan B., Balaji P.V., Qasba P.K.; RT "Crystal structure of beta1,4-galactosyltransferase complex with UDP- RT Gal reveals an oligosaccharide acceptor binding site."; RL J. Mol. Biol. 318:491-502(2002). RN [13] RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 117-402 OF MUTANT THR-342 IN RP COMPLEX WITH SUBSTRATE AND MANGANESE IONS, AND MUTAGENESIS OF TRP-314. RX MEDLINE=22809472; PubMed=12927542; DOI=10.1016/S0022-2836(03)00790-3; RA Ramasamy V., Ramakrishnan B., Boeggeman E., Qasba P.K.; RT "The role of tryptophan 314 in the conformational changes of beta1,4- RT galactosyltransferase-I."; RL J. Mol. Biol. 331:1065-1076(2003). CC -!- FUNCTION: The Golgi complex form catalyzes the production of CC lactose in the lactating mammary gland and could also be CC responsible for the synthesis of complex-type N-linked CC oligosaccharides in many glycoproteins as well as the carbohydrate CC moieties of glycolipids. CC -!- FUNCTION: The cell surface form functions as a recognition CC molecule during a variety of cell to cell and cell to matrix CC interactions, as those occurring during development and egg CC fertilization, by binding to specific oligosaccharide ligands on CC opposing cells or in the extracellular matrix. CC -!- CATALYTIC ACTIVITY: UDP-galactose + D-glucose = UDP + lactose. CC -!- CATALYTIC ACTIVITY: UDP-galactose + N-acetyl-beta-D- CC glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N- CC acetyl-beta-D-glucosaminylglycopeptide. CC -!- CATALYTIC ACTIVITY: UDP-galactose + N-acetyl-D-glucosamine = UDP + CC N-acetyllactosamine. CC -!- COFACTOR: Manganese. CC -!- PATHWAY: Protein modification; protein glycosylation. CC -!- SUBUNIT: Homodimer; and heterodimer with alpha-lactabulmin to form CC lactose synthase. CC -!- SUBCELLULAR LOCATION: Isoform Long: Golgi apparatus, Golgi stack CC membrane; Single-pass type II membrane protein. Cell membrane; CC Single-pass type II membrane protein. Cell surface. Note=Found in CC trans cisternae of Golgi. CC -!- SUBCELLULAR LOCATION: Isoform Short: Golgi apparatus, Golgi stack CC membrane; Single-pass type II membrane protein. Note=Found in CC trans cisternae of Golgi. CC -!- SUBCELLULAR LOCATION: Processed beta-1,4-galactosyltransferase 1: CC Secreted. Note=Soluble form found in body fluids. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; Synonyms=Cell surface; CC IsoId=P08037-1; Sequence=Displayed; CC Name=Short; Synonyms=Golgi complex; CC IsoId=P08037-2; Sequence=VSP_018801; CC -!- PTM: The soluble form derives from the membrane forms by CC proteolytic processing. CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14558; CAA32695.1; -; mRNA. DR EMBL; BC120415; AAI20416.1; -; mRNA. DR EMBL; M13214; AAA30534.1; -; mRNA. DR EMBL; AF515786; AAM54035.2; -; mRNA. DR EMBL; M25398; AAA30533.1; -; Genomic_DNA. DR EMBL; J05217; AAA30559.1; -; mRNA. DR IPI; IPI00685910; -. DR IPI; IPI00760476; -. DR PIR; I45897; I45897. DR PIR; S05018; S05018. DR RefSeq; NP_803478.1; -. DR UniGene; Bt.5141; -. DR PDB; 1FGX; X-ray; 2.40 A; A/B=115-402. DR PDB; 1FR8; X-ray; 2.40 A; A/B=115-402. DR PDB; 1NF5; X-ray; 2.00 A; B/D=130-402. DR PDB; 1NHE; X-ray; 2.50 A; B/D=130-402. DR PDB; 1NKH; X-ray; 2.00 A; B/D=130-402. DR PDB; 1NMM; X-ray; 2.00 A; B/D=130-402. DR PDB; 1NQI; X-ray; 2.00 A; B/D=130-402. DR PDB; 1NWG; X-ray; 2.32 A; B/D=131-402. DR PDB; 1O0R; X-ray; 2.30 A; A/B=130-402. DR PDB; 1O23; X-ray; 2.32 A; B/D=130-402. DR PDB; 1OQM; X-ray; 2.10 A; B/D=130-402. DR PDB; 1PZT; X-ray; 1.92 A; A=130-402. DR PDB; 1PZY; X-ray; 2.30 A; B/D=130-402. DR PDB; 1TVY; X-ray; 2.30 A; A/B=130-402. DR PDB; 1TW1; X-ray; 2.30 A; A/B=130-402. DR PDB; 1TW5; X-ray; 2.30 A; A/B=130-402. DR PDB; 1YRO; X-ray; 1.90 A; B/D=130-402. DR PDB; 2FYC; X-ray; 2.00 A; B/D=130-402. DR PDB; 2FYD; X-ray; 2.00 A; B/D=130-400. DR PDBsum; 1FGX; -. DR PDBsum; 1FR8; -. DR PDBsum; 1NF5; -. DR PDBsum; 1NHE; -. DR PDBsum; 1NKH; -. DR PDBsum; 1NMM; -. DR PDBsum; 1NQI; -. DR PDBsum; 1NWG; -. DR PDBsum; 1O0R; -. DR PDBsum; 1O23; -. DR PDBsum; 1OQM; -. DR PDBsum; 1PZT; -. DR PDBsum; 1PZY; -. DR PDBsum; 1TVY; -. DR PDBsum; 1TW1; -. DR PDBsum; 1TW5; -. DR PDBsum; 1YRO; -. DR PDBsum; 2FYC; -. DR PDBsum; 2FYD; -. DR CAZy; GT7; Glycosyltransferase Family 7. DR Ensembl; ENSBTAG00000015249; Bos taurus. DR GeneID; 281781; -. DR KEGG; bta:281781; -. DR HOVERGEN; P08037; -. DR OMA; P08037; NAVVGRC. DR BRENDA; 2.4.1.22; 251. DR BRENDA; 2.4.1.38; 251. DR BRENDA; 2.4.1.90; 251. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB. DR GO; GO:0030057; C:desmosome; ISS:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0030112; C:glycocalyx; ISS:UniProtKB. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000138; C:Golgi trans cisterna; ISS:UniProtKB. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-...; ISS:UniProtKB. DR GO; GO:0004461; F:lactose synthase activity; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; ISS:UniProtKB. DR GO; GO:0009312; P:oligosaccharide biosynthetic process; ISS:UniProtKB. DR InterPro; IPR003859; Galactosyl_T_2. DR PANTHER; PTHR19300; Galactosyl_T_2; 1. DR Pfam; PF02709; Galactosyl_T_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Cell membrane; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Manganese; Membrane; KW Metal-binding; Secreted; Signal-anchor; Transferase; Transmembrane. FT CHAIN 1 402 Beta-1,4-galactosyltransferase 1. FT /FTId=PRO_0000012276. FT CHAIN ? 402 Processed beta-1,4-galactosyltransferase FT 1. FT /FTId=PRO_0000296228. FT TOPO_DOM 1 24 Cytoplasmic (Potential). FT TRANSMEM 25 44 Signal-anchor for type II membrane FT protein (Potential). FT TOPO_DOM 45 402 Lumenal (Potential). FT METAL 254 254 Manganese. FT METAL 347 347 Manganese. FT CARBOHYD 90 90 N-linked (GlcNAc...) (Probable). FT CARBOHYD 117 117 N-linked (GlcNAc...) (Potential). FT DISULFID 134 176 FT DISULFID 247 266 FT VAR_SEQ 1 13 Missing (in isoform Short). FT /FTId=VSP_018801. FT MUTAGEN 314 314 W->A: Reduces galactosyltransferase FT activity, lactose synthase activity and FT substrate binding by 99%. FT CONFLICT 65 66 HG -> QA (in Ref. 7). FT CONFLICT 158 158 V -> I (in Ref. 1; CAA32695). FT CONFLICT 187 187 P -> L (in Ref. 1; CAA32695). FT CONFLICT 205 206 IL -> MV (in Ref. 1; CAA32695). FT CONFLICT 282 282 F -> L (in Ref. 3; AAA30534). FT HELIX 155 161 FT TURN 167 169 FT STRAND 174 177 FT STRAND 181 190 FT HELIX 192 208 FT STRAND 212 220 FT STRAND 222 224 FT HELIX 228 239 FT TURN 240 242 FT STRAND 247 251 FT STRAND 255 259 FT HELIX 278 280 FT STRAND 292 297 FT HELIX 298 303 FT HELIX 317 327 FT TURN 337 340 FT STRAND 341 344 FT HELIX 363 369 FT TURN 370 372 FT HELIX 375 377 FT STRAND 381 387 FT STRAND 392 397 SQ SEQUENCE 402 AA; 44843 MW; FABF94E74E0C6F81 CRC64; MKFREPLLGG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLRRL PQLVGVHPPL QGSSHGAAAI GQPSGELRLR GVAPPPPLQN SSKPRSRAPS NLDAYSHPGP GPGPGSNLTS APVPSTTTRS LTACPEESPL LVGPMLIEFN IPVDLKLVEQ QNPKVKLGGR YTPMDCISPH KVAIIIPFRN RQEHLKYWLY YLHPILQRQQ LDYGIYVINQ AGESMFNRAK LLNVGFKEAL KDYDYNCFVF SDVDLIPMND HNTYRCFSQP RHISVAMDKF GFSLPYVQYF GGVSALSKQQ FLSINGFPNN YWGWGGEDDD IYNRLAFRGM SVSRPNAVIG KCRMIRHSRD KKNEPNPQRF DRIAHTKETM LSDGLNSLTY MVLEVQRYPL YTKITVDIGT PS //