B4GT1_HUMAN
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 03-AUG-2022, entry version 228.
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 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 [21]
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 [22]
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).
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:16157350}.
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 = 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: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}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,4-
CC galactosyltransferase 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_436";
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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; 94.
DR IntAct; P15291; 18.
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 GlyGen; P15291; 5 sites, 1 O-linked glycan (4 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; P15291; -.
DR PeptideAtlas; P15291; -.
DR PRIDE; P15291; -.
DR ProteomicsDB; 53124; -. [P15291-1]
DR ProteomicsDB; 53125; -. [P15291-2]
DR Antibodypedia; 2256; 181 antibodies from 27 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 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 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; KDCISSH; -.
DR OrthoDB; 1201618at2759; -.
DR PhylomeDB; P15291; -.
DR TreeFam; TF312834; -.
DR BioCyc; MetaCyc:HS01519-MON; -.
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; 11 hits in 1078 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 187 other tissues.
DR ExpressionAtlas; P15291; baseline and differential.
DR Genevisible; P15291; HS.
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:UniProtKB.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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:0070085; P:glycosylation; IBA:GO_Central.
DR GO; GO:0005989; P:lactose biosynthetic process; TAS:Reactome.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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: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 Gene3D; 3.90.550.10; -; 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; PTHR19300; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; Cell membrane; Cell projection;
KW Congenital disorder of glycosylation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Lipid metabolism; Manganese; Membrane; Metal-binding; Reference proteome;
KW Secreted; Signal-anchor; Transferase; Transmembrane; 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 dbSNP:rs1065764)"
FT /id="VAR_054019"
FT VARIANT 257
FT /note="H -> R (in dbSNP:rs9169)"
FT /id="VAR_054020"
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 UDP-
FT 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
