ID B4GT1_HUMAN Reviewed; 398 AA. AC P15291; B2R710; D3DRL2; Q12909; Q12910; Q12911; Q14456; Q14509; Q14523; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 5. DT 27-MAR-2024, entry version 237. 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.- {ECO:0000269|PubMed:16157350}; 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 {ECO:0000269|PubMed:16157350}; DE AltName: Full=Lactose synthase A protein; DE EC=2.4.1.22 {ECO:0000269|PubMed:16157350}; DE AltName: Full=N-acetyllactosamine synthase; DE EC=2.4.1.90 {ECO:0000269|PubMed:16157350}; 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 Contains: DE RecName: Full=Processed beta-1,4-galactosyltransferase 1 {ECO:0000305}; GN Name=B4GALT1 {ECO:0000312|HGNC:HGNC:924}; Synonyms=GGTB2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3144273; DOI=10.1016/s0006-291x(88)80300-0; RA Masri K.A., Appert H.E., Fukuda M.N.; RT "Identification of the full-length coding sequence for human RT galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4- RT galactosyltransferase)."; RL Biochem. Biophys. Res. Commun. 157:657-663(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2124683; DOI=10.1093/nar/18.23.7174; RA Watzele G., Berger E.G.; RT "Near identity of HeLa cell galactosyltransferase with the human placental RT enzyme."; RL Nucleic Acids Res. 18:7174-7174(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1903938; DOI=10.1016/0006-291x(91)90423-5; RA Mengle-Gaw L., McCoy-Haman M.F., Tiemeier D.C.; RT "Genomic structure and expression of human beta-1,4- RT galactosyltransferase."; RL Biochem. Biophys. Res. Commun. 176:1269-1276(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=1384956; RA Uejima T., Uemura M., Nozawa S., Narimatsu H.; RT "Complementary DNA cloning for galactosyltransferase associated with tumor RT and determination of antigenic epitopes recognized by specific monoclonal RT antibodies."; RL Cancer Res. 52:6158-6163(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=7579794; DOI=10.1093/glycob/5.4.397; RA Kudo T., Narimatsu H.; RT "The beta 1, 4-galactosyltransferase gene is post-transcriptionally RT regulated during differentiation of mouse F9 teratocarcinoma cells."; RL Glycobiology 5:397-403(1995). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Fetal liver; RX PubMed=7540104; DOI=10.1016/1357-2725(94)00062-g; RA Chatterjee S.K., Mukerjee S., Tripathi P.K.; RT "Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA RT clones."; RL Int. J. Biochem. Cell Biol. 27:329-336(1995). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 138-398, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=3094506; DOI=10.1016/s0006-291x(86)80094-8; RA Appert H.E., Rutherford T.J., Tarr G.E., Wiest J.S., Thomford N.R., RA McCorquodale D.J.; RT "Isolation of a cDNA coding for human galactosyltransferase."; RL Biochem. Biophys. Res. Commun. 139:163-168(1986). RN [11] RP PROTEIN SEQUENCE OF 78-94. RX PubMed=3091013; DOI=10.1016/0006-291x(86)90269-x; RA Appert H.E., Rutherford T.J., Tarr G.E., Thomford N.R., McCorquodale D.J.; RT "Isolation of galactosyltransferase from human milk and the determination RT of its N-terminal amino acid sequence."; RL Biochem. Biophys. Res. Commun. 138:224-229(1986). RN [12] RP PROTEIN SEQUENCE OF 274-326, CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS RP OF TYR-282; TYR-285; TYR-307; TRP-308 AND TRP-310. RX PubMed=2120039; DOI=10.1002/j.1460-2075.1990.tb07515.x; RA Aoki D., Appert H.E., Johnson D., Wong S.S., Fukuda M.N.; RT "Analysis of the substrate binding sites of human galactosyltransferase by RT protein engineering."; RL EMBO J. 9:3171-3178(1990). RN [13] RP ALTERNATIVE INITIATION, AND SUBCELLULAR LOCATION. RX PubMed=1714903; DOI=10.1016/s0021-9258(18)98505-4; RA Lopez L.C., Youakim A., Evans S.C., Shur B.D.; RT "Evidence for a molecular distinction between Golgi and cell surface forms RT of beta 1,4-galactosyltransferase."; RL J. Biol. Chem. 266:15984-15991(1991). RN [14] RP SUBUNIT. RX PubMed=7744867; DOI=10.1074/jbc.270.20.12170; RA Yamaguchi N., Fukuda M.N.; RT "Golgi retention mechanism of beta-1,4-galactosyltransferase. Membrane- RT spanning domain-dependent homodimerization and association with alpha- and RT beta-tubulins."; RL J. Biol. Chem. 270:12170-12176(1995). RN [15] RP REVIEW. RX PubMed=10580128; DOI=10.1016/s0304-4165(99)00168-3; RA Amado M., Almeida R., Schwientek T., Clausen H.; RT "Identification and characterization of large galactosyltransferase gene RT families: galactosyltransferases for all functions."; RL Biochim. Biophys. Acta 1473:35-53(1999). RN [16] RP INVOLVEMENT IN CDG2D. RX PubMed=11901181; DOI=10.1172/jci14010; RA Hansske B., Thiel C., Luebke T., Hasilik M., Hoening S., Peters V., RA Heidemann P.H., Hoffmann G.F., Berger E.G., von Figura K., Koerner C.; RT "Deficiency of UDP-galactose:N-acetylglucosamine beta-1,4- RT galactosyltransferase I causes the congenital disorder of glycosylation RT type IId."; RL J. Clin. Invest. 109:725-733(2002). RN [17] RP SUBCELLULAR LOCATION. RX PubMed=20378551; DOI=10.1074/jbc.m110.103184; RA Hassinen A., Rivinoja A., Kauppila A., Kellokumpu S.; RT "Golgi N-glycosyltransferases form both homo- and heterodimeric enzyme RT complexes in live cells."; RL J. Biol. Chem. 285:17771-17777(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [20] RP INVOLVEMENT IN CLDLFIB, VARIANT SER-352, AND CHARACTERIZATION OF VARIANT RP SER-352. RX PubMed=34855475; DOI=10.1126/science.abe0348; RG Regeneron Genetics Center Collaboration; RA Montasser M.E., Van Hout C.V., Miloscio L., Howard A.D., Rosenberg A., RA Callaway M., Shen B., Li N., Locke A.E., Verweij N., De T., Ferreira M.A., RA Lotta L.A., Baras A., Daly T.J., Hartford S.A., Lin W., Mao Y., Ye B., RA White D., Gong G., Perry J.A., Ryan K.A., Fang Q., Tzoneva G., Pefanis E., RA Hunt C., Tang Y., Lee L., Sztalryd-Woodle C., Mitchell B.D., Healy M., RA Streeten E.A., Taylor S.I., O'Connell J.R., Economides A.N., RA Della Gatta G., Shuldiner A.R.; RT "Genetic and functional evidence links a missense variant in B4GALT1 to RT lower LDL and fibrinogen."; RL Science 374:1221-1227(2021). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN RP COMPLEX WITH MANGANESE IONS AND N-ACETYL-D-GLUCOSAMINE, CATALYTIC ACTIVITY, RP FUNCTION, COFACTOR, MUTAGENESIS OF MET-340, AND DISULFIDE BONDS. RX PubMed=16157350; DOI=10.1016/j.jmb.2005.07.050; RA Ramasamy V., Ramakrishnan B., Boeggeman E., Ratner D.M., Seeberger P.H., RA Qasba P.K.; RT "Oligosaccharide preferences of beta1,4-galactosyltransferase-I: crystal RT structures of Met340His mutant of human beta1,4-galactosyltransferase-I RT with a pentasaccharide and trisaccharides of the N-glycan moiety."; RL J. Mol. Biol. 353:53-67(2005). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 126-397 OF MUTANT HIS-340 IN RP COMPLEX WITH MANGANESE IONS AND UDP, COFACTOR, AND DISULFIDE BONDS. RX PubMed=16497331; DOI=10.1016/j.jmb.2006.01.088; RA Ramakrishnan B., Ramasamy V., Qasba P.K.; RT "Structural snapshots of beta-1,4-galactosyltransferase-I along the kinetic RT pathway."; RL J. Mol. Biol. 357:1619-1633(2006). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 126-398 IN COMPLEX WITH MANGANESE RP IONS AND N-ACETYL-D-GLUCOSAMINE, AND COFACTOR. RX PubMed=19106107; DOI=10.1074/jbc.m805782200; RA Brown J.R., Yang F., Sinha A., Ramakrishnan B., Tor Y., Qasba P.K., RA Esko J.D.; RT "Deoxygenated disaccharide analogs as specific inhibitors of beta1-4- RT galactosyltransferase 1 and selectin-mediated tumor metastasis."; RL J. Biol. Chem. 284:4952-4959(2009). RN [24] RP VARIANT CDG2D 193-TYR--SER-398 DEL. RX PubMed=30653653; DOI=10.1111/cge.13508; RA Medrano C., Vega A., Navarrete R., Ecay M.J., Calvo R., Pascual S.I., RA Ruiz-Pons M., Toledo L., Garcia-Jimenez I., Arroyo I., Campo A., RA Couce M.L., Domingo-Jimenez M.R., Garcia-Silva M.T., RA Gonzalez-Gutierrez-Solana L., Hierro L., Martin-Hernandez E., RA Martinez-Pardo M., Roldan S., Tomas M., Cabrera J.C., Martinez-Bugallo F., RA Martin-Viota L., Vitoria-Minana I., Lefeber D.J., Giros M.L., RA Serrano Gimare M., Ugarte M., Perez B., Perez-Cerda C.; RT "Clinical and molecular diagnosis of non-phosphomannomutase 2 N-linked RT congenital disorders of glycosylation in Spain."; RL Clin. Genet. 95:615-626(2019). RN [25] RP VARIANT CDG2D TRP-21. RX PubMed=32157688; DOI=10.1111/cge.13735; RA Staretz-Chacham O., Noyman I., Wormser O., Abu Quider A., Hazan G., RA Morag I., Hadar N., Raymond K., Birk O.S., Ferreira C.R., Koifman A.; RT "B4GALT1-congenital disorders of glycosylation: Expansion of the phenotypic RT and molecular spectrum and review of the literature."; RL Clin. Genet. 97:920-926(2020). CC -!- FUNCTION: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form CC catalyzes the production of lactose in the lactating mammary gland and CC could also be responsible for the synthesis of complex-type N-linked CC oligosaccharides in many glycoproteins as well as the carbohydrate CC moieties of glycolipids. {ECO:0000269|PubMed:34855475}. CC -!- FUNCTION: [Processed beta-1,4-galactosyltransferase 1]: The cell CC surface form functions as a recognition molecule during a variety of CC cell to cell and cell to matrix interactions, as those occurring during CC development and egg fertilization, by binding to specific CC oligosaccharide ligands on opposing cells or in the extracellular CC matrix. {ECO:0000269|PubMed:16157350}. 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:0000269|PubMed:16157350}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405; CC Evidence={ECO:0000269|PubMed:16157350}; 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:0000269|PubMed:16157350}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22933; CC Evidence={ECO:0000269|PubMed:16157350}; 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:0000269|PubMed:16157350}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17746; CC Evidence={ECO:0000269|PubMed:16157350}; 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 = 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: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-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: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:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331, CC ECO:0000269|PubMed:19106107}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:16157350}. CC -!- SUBUNIT: Homodimer; and heterodimer with alpha-lactalbumin to form CC lactose synthase. Interacts (via N-terminal cytoplasmic domain) with CC UBE2Q1 (via N-terminus); the interaction is direct (By similarity). CC {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:16157350, CC ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107, CC ECO:0000269|PubMed:7744867}. CC -!- SUBCELLULAR LOCATION: [Isoform Long]: Golgi apparatus, Golgi stack CC membrane {ECO:0000269|PubMed:1714903, ECO:0000269|PubMed:20378551}; CC Single-pass type II membrane protein. Cell membrane CC {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. CC Cell surface {ECO:0000269|PubMed:1714903}. Cell projection, filopodium CC {ECO:0000250|UniProtKB:P15535}. Note=Found in trans cisternae of Golgi CC but is mainly localized at the plasma membrane (PubMed:1714903). CC B4GALT1 cell surface expression is regulated by UBE2Q1 (By similarity). CC {ECO:0000250|UniProtKB:P15535, ECO:0000269|PubMed:1714903}. CC -!- SUBCELLULAR LOCATION: [Isoform Short]: Golgi apparatus, Golgi stack CC membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane CC protein. Note=Found in trans cisternae of Golgi. CC {ECO:0000269|PubMed:1714903}. CC -!- SUBCELLULAR LOCATION: [Processed beta-1,4-galactosyltransferase 1]: CC Secreted {ECO:0000303|PubMed:2120039}. Note=Soluble form found in body CC fluids. {ECO:0000303|PubMed:2120039}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Long; Synonyms=Cell surface; CC IsoId=P15291-1; Sequence=Displayed; CC Name=Short; Synonyms=Golgi complex; CC IsoId=P15291-2; Sequence=VSP_018802; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, but at very low levels in CC fetal and adult brain. CC -!- PTM: The soluble form derives from the membrane forms by proteolytic CC processing. CC -!- DISEASE: Congenital disorder of glycosylation 2D (CDG2D) [MIM:607091]: CC A multisystem disorder caused by a defect in glycoprotein biosynthesis CC and characterized by under-glycosylated serum glycoproteins. Congenital CC disorders of glycosylation result in a wide variety of clinical CC features, such as defects in the nervous system development, CC psychomotor retardation, dysmorphic features, hypotonia, coagulation CC disorders, and immunodeficiency. The broad spectrum of features CC reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CC {ECO:0000269|PubMed:11901181, ECO:0000269|PubMed:30653653, CC ECO:0000269|PubMed:32157688}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Combined low LDL and fibrinogen (CLDLFIB) [MIM:620364]: An CC autosomal recessive condition characterized by low plasma LDL- CC cholesterol and fibrinogen levels, and associated with a decreased risk CC of coronary artery disease. {ECO:0000269|PubMed:34855475}. Note=Disease CC susceptibility may be associated with variants affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; CC Note=Beta-1,4-galactosyltransferase 1; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_436"; 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 EMBL; X14085; CAA32247.1; -; mRNA. DR EMBL; M22921; AAA35936.1; -; mRNA. DR EMBL; M22921; AAA35937.1; -; mRNA. DR EMBL; X55415; CAA39073.1; -; mRNA. DR EMBL; X55415; CAA39074.1; -; mRNA. DR EMBL; M70432; AAB00776.1; -; Genomic_DNA. DR EMBL; M70427; AAB00776.1; JOINED; Genomic_DNA. DR EMBL; M70428; AAB00776.1; JOINED; Genomic_DNA. DR EMBL; M70429; AAB00776.1; JOINED; Genomic_DNA. DR EMBL; M70430; AAB00776.1; JOINED; Genomic_DNA. DR EMBL; M70431; AAB00776.1; JOINED; Genomic_DNA. DR EMBL; X13223; CAA31611.1; -; mRNA. DR EMBL; D29805; BAA06188.1; -; mRNA. DR EMBL; U10472; AAA68218.1; -; mRNA. DR EMBL; U10473; AAA68219.1; -; mRNA. DR EMBL; U10474; AAA68220.1; -; mRNA. DR EMBL; CH471071; EAW58520.1; -; Genomic_DNA. DR EMBL; CH471071; EAW58521.1; -; Genomic_DNA. DR EMBL; AK312797; BAG35657.1; -; mRNA. DR EMBL; AL161445; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M13701; AAA35935.1; -; mRNA. DR CCDS; CCDS6535.1; -. [P15291-1] DR PIR; JQ1030; JQ1030. DR RefSeq; NP_001488.2; NM_001497.3. [P15291-1] DR PDB; 2AE7; X-ray; 2.00 A; A/B/C=126-398. DR PDB; 2AEC; X-ray; 2.00 A; A/B/C=126-398. DR PDB; 2AES; X-ray; 2.00 A; A/B/C=126-398. DR PDB; 2AGD; X-ray; 1.90 A; A/B/C=126-398. DR PDB; 2AH9; X-ray; 2.00 A; A/B/C=126-398. DR PDB; 2FY7; X-ray; 1.70 A; A=126-398. DR PDB; 2FYA; X-ray; 1.90 A; A=126-398. DR PDB; 2FYB; X-ray; 1.90 A; A=126-398. DR PDB; 3EE5; X-ray; 2.20 A; A/B/C=126-398. DR PDB; 4EE3; X-ray; 2.30 A; A/B/C=126-398. DR PDB; 4EE4; X-ray; 1.95 A; A/B/C=126-398. DR PDB; 4EE5; X-ray; 2.20 A; A/B/C=126-398. DR PDB; 4EEA; X-ray; 2.00 A; A/B/C=126-398. DR PDB; 4EEG; X-ray; 2.20 A; A/B/C=126-398. DR PDB; 4EEM; X-ray; 2.20 A; A/B/C=126-398. DR PDB; 4EEO; X-ray; 2.30 A; A/B/C=126-398. DR PDB; 4L41; X-ray; 2.70 A; C=126-398. DR PDB; 6FWT; X-ray; 1.84 A; A=122-398. DR PDB; 6FWU; X-ray; 2.35 A; A/B=126-398. DR PDBsum; 2AE7; -. DR PDBsum; 2AEC; -. DR PDBsum; 2AES; -. DR PDBsum; 2AGD; -. DR PDBsum; 2AH9; -. DR PDBsum; 2FY7; -. DR PDBsum; 2FYA; -. DR PDBsum; 2FYB; -. DR PDBsum; 3EE5; -. DR PDBsum; 4EE3; -. DR PDBsum; 4EE4; -. DR PDBsum; 4EE5; -. DR PDBsum; 4EEA; -. DR PDBsum; 4EEG; -. DR PDBsum; 4EEM; -. DR PDBsum; 4EEO; -. DR PDBsum; 4L41; -. DR PDBsum; 6FWT; -. DR PDBsum; 6FWU; -. DR AlphaFoldDB; P15291; -. DR SMR; P15291; -. DR BioGRID; 108950; 98. DR IntAct; P15291; 19. DR MINT; P15291; -. DR STRING; 9606.ENSP00000369055; -. DR BindingDB; P15291; -. DR ChEMBL; CHEMBL4384; -. DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid. DR DrugBank; DB02696; 6-Aminohexyl-uridine-C1,5'-diphosphate. DR DrugBank; DB03501; Galactose-uridine-5'-diphosphate. DR DrugBank; DB03013; N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosamine. DR DrugBank; DB00141; N-Acetylglucosamine. DR DrugBank; DB03685; Uridine monophosphate. DR CAZy; GT7; Glycosyltransferase Family 7. DR MoonProt; P15291; -. DR GlyCosmos; P15291; 5 sites, 1 glycan. DR GlyGen; P15291; 10 sites, 3 O-linked glycans (9 sites). DR iPTMnet; P15291; -. DR PhosphoSitePlus; P15291; -. DR SwissPalm; P15291; -. DR BioMuta; B4GALT1; -. DR DMDM; 116241264; -. DR EPD; P15291; -. DR jPOST; P15291; -. DR MassIVE; P15291; -. DR MaxQB; P15291; -. DR PaxDb; 9606-ENSP00000369055; -. DR PeptideAtlas; P15291; -. DR ProteomicsDB; 53124; -. [P15291-1] DR ProteomicsDB; 53125; -. [P15291-2] DR Pumba; P15291; -. DR Antibodypedia; 2256; 197 antibodies from 28 providers. DR DNASU; 2683; -. DR Ensembl; ENST00000379731.5; ENSP00000369055.4; ENSG00000086062.13. [P15291-1] DR GeneID; 2683; -. DR KEGG; hsa:2683; -. DR MANE-Select; ENST00000379731.5; ENSP00000369055.4; NM_001497.4; NP_001488.2. DR UCSC; uc003zsg.3; human. [P15291-1] DR AGR; HGNC:924; -. DR CTD; 2683; -. DR DisGeNET; 2683; -. DR GeneCards; B4GALT1; -. DR GeneReviews; B4GALT1; -. DR HGNC; HGNC:924; B4GALT1. DR HPA; ENSG00000086062; Low tissue specificity. DR MalaCards; B4GALT1; -. DR MIM; 137060; gene. DR MIM; 607091; phenotype. DR MIM; 620364; phenotype. DR neXtProt; NX_P15291; -. DR OpenTargets; ENSG00000086062; -. DR Orphanet; 79332; B4GALT1-CDG. DR PharmGKB; PA25223; -. DR VEuPathDB; HostDB:ENSG00000086062; -. DR eggNOG; KOG3916; Eukaryota. DR GeneTree; ENSGT00940000155244; -. DR HOGENOM; CLU_044391_0_0_1; -. DR InParanoid; P15291; -. DR OMA; NAMVGKC; -. DR OrthoDB; 306273at2759; -. DR PhylomeDB; P15291; -. DR TreeFam; TF312834; -. DR BioCyc; MetaCyc:HS01519-MONOMER; -. DR BRENDA; 2.4.1.133; 2681. DR BRENDA; 2.4.1.22; 2681. DR BRENDA; 2.4.1.38; 2681. DR BRENDA; 2.4.1.90; 2681. DR PathwayCommons; P15291; -. DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi. DR Reactome; R-HSA-2022854; Keratan sulfate biosynthesis. DR Reactome; R-HSA-2534343; Interaction With Cumulus Cells And The Zona Pellucida. DR Reactome; R-HSA-3656244; Defective B4GALT1 causes B4GALT1-CDG (CDG-2d). DR Reactome; R-HSA-4793953; Defective B4GALT1 causes CDG-2d. DR Reactome; R-HSA-5653890; Lactose synthesis. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-975577; N-Glycan antennae elongation. DR SignaLink; P15291; -. DR SIGNOR; P15291; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 2683; 12 hits in 1156 CRISPR screens. DR ChiTaRS; B4GALT1; human. DR EvolutionaryTrace; P15291; -. DR GeneWiki; B4GALT1; -. DR GenomeRNAi; 2683; -. DR Pharos; P15291; Tbio. DR PRO; PR:P15291; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P15291; Protein. DR Bgee; ENSG00000086062; Expressed in buccal mucosa cell and 189 other cell types or tissues. DR ExpressionAtlas; P15291; baseline and differential. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB. DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB. DR GO; GO:0030057; C:desmosome; IDA:UniProtKB. DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0000138; C:Golgi trans cisterna; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB. DR GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; IPI:UniProtKB. DR GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central. DR GO; GO:0008378; F:galactosyltransferase activity; NAS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0004461; F:lactose synthase activity; IDA:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB. DR GO; GO:0003945; F:N-acetyllactosamine synthase activity; IDA:UniProtKB. DR GO; GO:0035250; F:UDP-galactosyltransferase activity; IDA:UniProtKB. DR GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl. DR GO; GO:0060055; P:angiogenesis involved in wound healing; IEA:Ensembl. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl. DR GO; GO:0045136; P:development of secondary sexual characteristics; IEA:Ensembl. DR GO; GO:0002064; P:epithelial cell development; IEA:Ensembl. DR GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl. DR GO; GO:0006012; P:galactose metabolic process; IEA:Ensembl. DR GO; GO:0005989; P:lactose biosynthetic process; TAS:Reactome. DR GO; GO:0006629; P:lipid metabolic process; IMP:UniProtKB. DR GO; GO:1905517; P:macrophage migration; IEA:Ensembl. DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl. DR GO; GO:0009312; P:oligosaccharide biosynthetic process; IDA:UniProtKB. DR GO; GO:0007341; P:penetration of zona pellucida; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl. DR GO; GO:0061755; P:positive regulation of circulating fibrinogen levels; IMP:UniProtKB. DR GO; GO:0060054; P:positive regulation of epithelial cell proliferation involved in wound healing; IEA:Ensembl. DR GO; GO:0006487; P:protein N-linked glycosylation; IDA:UniProtKB. DR GO; GO:0060046; P:regulation of acrosome reaction; IEA:Ensembl. 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:SF5; BETA-1,4-GALACTOSYLTRANSFERASE 1; 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. DR Genevisible; P15291; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Cell membrane; Cell projection; KW Congenital disorder of glycosylation; Direct protein sequencing; KW Disease variant; Disulfide bond; Glycoprotein; Glycosyltransferase; KW Golgi apparatus; Lipid metabolism; Manganese; Membrane; Metal-binding; KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1..398 FT /note="Beta-1,4-galactosyltransferase 1" FT /id="PRO_0000012278" FT CHAIN ?..398 FT /note="Processed beta-1,4-galactosyltransferase 1" FT /id="PRO_0000296229" FT TOPO_DOM 1..24 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 25..44 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 45..398 FT /note="Lumenal" FT /evidence="ECO:0000255" FT REGION 61..117 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 183..187 FT /ligand="UDP-alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:66914" FT BINDING 222..224 FT /ligand="UDP-alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:66914" FT /evidence="ECO:0000250" FT BINDING 249..250 FT /ligand="UDP-alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:66914" FT BINDING 250 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 310 FT /ligand="UDP-alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:66914" FT /evidence="ECO:0000269|PubMed:16497331" FT BINDING 312..315 FT /ligand="N-acetyl-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:506227" FT BINDING 343..346 FT /ligand="UDP-alpha-D-galactose" FT /ligand_id="ChEBI:CHEBI:66914" FT BINDING 343 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT BINDING 355 FT /ligand="N-acetyl-D-glucosamine" FT /ligand_id="ChEBI:CHEBI:506227" FT /evidence="ECO:0000269|PubMed:16157350, FT ECO:0000269|PubMed:19106107" FT SITE 77..78 FT /note="Cleavage; to produce soluble form" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 130..172 FT /evidence="ECO:0000269|PubMed:16157350, FT ECO:0000269|PubMed:16497331, ECO:0007744|PDB:2AE7, FT ECO:0007744|PDB:2AEC, ECO:0007744|PDB:2AES, FT ECO:0007744|PDB:2AGD, ECO:0007744|PDB:2AH9, FT ECO:0007744|PDB:2FY7, ECO:0007744|PDB:2FYA, FT ECO:0007744|PDB:2FYB, ECO:0007744|PDB:3EE5, FT ECO:0007744|PDB:4EE3, ECO:0007744|PDB:4EE4, FT ECO:0007744|PDB:4EE5, ECO:0007744|PDB:4EEA, FT ECO:0007744|PDB:4EEG, ECO:0007744|PDB:4EEM, FT ECO:0007744|PDB:4EEO, ECO:0007744|PDB:4L41" FT DISULFID 243..262 FT /evidence="ECO:0000269|PubMed:16157350, FT ECO:0000269|PubMed:16497331, ECO:0007744|PDB:2AE7, FT ECO:0007744|PDB:2AEC, ECO:0007744|PDB:2AES, FT ECO:0007744|PDB:2AGD, ECO:0007744|PDB:2AH9, FT ECO:0007744|PDB:2FY7, ECO:0007744|PDB:2FYA, FT ECO:0007744|PDB:2FYB, ECO:0007744|PDB:3EE5, FT ECO:0007744|PDB:4EE3, ECO:0007744|PDB:4EE4, FT ECO:0007744|PDB:4EE5, ECO:0007744|PDB:4EEA, FT ECO:0007744|PDB:4EEG, ECO:0007744|PDB:4EEM, FT ECO:0007744|PDB:4EEO, ECO:0007744|PDB:4L41" FT VAR_SEQ 1..13 FT /note="Missing (in isoform Short)" FT /evidence="ECO:0000305" FT /id="VSP_018802" FT VARIANT 21 FT /note="R -> W (in CDG2D; uncertain significance; FT dbSNP:rs1065764)" FT /evidence="ECO:0000269|PubMed:32157688" FT /id="VAR_054019" FT VARIANT 193..398 FT /note="Missing (in CDG2D; likely pathogenic)" FT /evidence="ECO:0000269|PubMed:30653653" FT /id="VAR_088575" FT VARIANT 257 FT /note="H -> R (in dbSNP:rs9169)" FT /id="VAR_054020" FT VARIANT 352 FT /note="N -> S (protective factor against coronary artery FT disease; strongly correlated with low plasma FT LDL-cholesterol and fibrinogen levels; decreased FT UDP-galactosyltransferase activity; dbSNP:rs551564683)" FT /evidence="ECO:0000269|PubMed:34855475" FT /id="VAR_088576" FT MUTAGEN 282 FT /note="Y->G: Reduction in N-acetylglucosamine binding." FT /evidence="ECO:0000269|PubMed:2120039" FT MUTAGEN 285 FT /note="Y->F: No change in enzymatic activity." FT /evidence="ECO:0000269|PubMed:2120039" FT MUTAGEN 307 FT /note="Y->G: Reduction in N-acetylglucosamine and FT UDP-galactose binding." FT /evidence="ECO:0000269|PubMed:2120039" FT MUTAGEN 308 FT /note="W->G: Reduction in N-acetylglucosamine binding." FT /evidence="ECO:0000269|PubMed:2120039" FT MUTAGEN 310 FT /note="W->G: Reduction in N-acetylglucosamine binding." FT /evidence="ECO:0000269|PubMed:2120039" FT MUTAGEN 340 FT /note="M->H: Favors the closed conformation of the enzyme." FT /evidence="ECO:0000269|PubMed:16157350" FT CONFLICT 10 FT /note="G -> R (in Ref. 4; CAA31611 and 5; BAA06188)" FT /evidence="ECO:0000305" FT CONFLICT 11 FT /note="Missing (in Ref. 1; AAA35936, 3; AAB00776 and 6; FT AAA68220)" FT /evidence="ECO:0000305" FT CONFLICT 31..32 FT /note="AL -> VW (in Ref. 1; AAA35936/AAA35937 and 6; FT AAA68220)" FT /evidence="ECO:0000305" FT CONFLICT 35 FT /note="G -> R (in Ref. 4; CAA31611)" FT /evidence="ECO:0000305" FT CONFLICT 76 FT /note="E -> D (in Ref. 5; BAA06188)" FT /evidence="ECO:0000305" FT CONFLICT 91..115 FT /note="SSQPRPGGDSSPVVDSGPGPASNLT -> GKHAKSSFKQFLLQIKELSNPID FT LD (in Ref. 6; AAA68219)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="Y -> YGIY (in Ref. 1; CAA32247 and 3; AAB00776)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="Y -> D (in Ref. 6; AAA68218)" FT /evidence="ECO:0000305" FT CONFLICT 292 FT /note="L -> S (in Ref. 5; BAA06188)" FT /evidence="ECO:0000305" FT CONFLICT 337 FT /note="R -> T (in Ref. 5; BAA06188)" FT /evidence="ECO:0000305" FT CONFLICT 340..341 FT /note="MI -> PA (in Ref. 6; AAA68220)" FT /evidence="ECO:0000305" FT HELIX 151..157 FT /evidence="ECO:0007829|PDB:2FY7" FT TURN 163..165 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 177..186 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 188..204 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 208..216 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 218..220 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 224..238 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 243..247 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 251..255 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:6FWU" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:6FWU" FT STRAND 288..293 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 294..299 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 309..312 FT /evidence="ECO:0007829|PDB:2AGD" FT HELIX 313..323 FT /evidence="ECO:0007829|PDB:2FY7" FT TURN 333..335 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 337..340 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 344..346 FT /evidence="ECO:0007829|PDB:6FWT" FT HELIX 347..349 FT /evidence="ECO:0007829|PDB:4L41" FT HELIX 359..365 FT /evidence="ECO:0007829|PDB:2FY7" FT TURN 366..368 FT /evidence="ECO:0007829|PDB:2FY7" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 377..384 FT /evidence="ECO:0007829|PDB:2FY7" FT STRAND 387..393 FT /evidence="ECO:0007829|PDB:2FY7" SQ SEQUENCE 398 AA; 43920 MW; 29B224C83C61E165 CRC64; MRLREPLLSG SAAMPGASLQ RACRLLVAVC ALHLGVTLVY YLAGRDLSRL PQLVGVSTPL QGGSNSAAAI GQSSGELRTG GARPPPPLGA SSQPRPGGDS SPVVDSGPGP ASNLTSVPVP HTTALSLPAC PEESPLLVGP MLIEFNMPVD LELVAKQNPN VKMGGRYAPR DCVSPHKVAI IIPFRNRQEH LKYWLYYLHP VLQRQQLDYG IYVINQAGDT IFNRAKLLNV GFQEALKDYD YTCFVFSDVD LIPMNDHNAY RCFSQPRHIS VAMDKFGFSL PYVQYFGGVS ALSKQQFLTI NGFPNNYWGW GGEDDDIFNR LVFRGMSISR PNAVVGRCRM IRHSRDKKNE PNPQRFDRIA HTKETMLSDG LNSLTYQVLD VQRYPLYTQI TVDIGTPS //