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{{Underlinked|date=May 2016}}
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{{Infobox_gene}}
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'''Beta-1,4-galactosyltransferase 1''' is an [[enzyme]] that in humans is encoded by the ''B4GALT1'' [[gene]].<ref name="pmid9597550">{{cite journal | vauthors = Lo NW, Shaper JH, Pevsner J, Shaper NL | title = The expanding beta 4-galactosyltransferase gene family: messages from the databanks | journal = Glycobiology | volume = 8 | issue = 5 | pages = 517–26 |date=Aug 1998 | pmid = 9597550 | pmc =  | doi =10.1093/glycob/8.5.517 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2683| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_B4GALT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nf5.
| PDB = {{PDB2|1nf5}}, {{PDB2|1nhe}}, {{PDB2|1nkh}}, {{PDB2|1nmm}}, {{PDB2|1nqi}}, {{PDB2|1nwg}}, {{PDB2|1o0r}}, {{PDB2|1o23}}, {{PDB2|1oqm}}, {{PDB2|2ae7}}, {{PDB2|2aec}}, {{PDB2|2aes}}, {{PDB2|2agd}}, {{PDB2|2ah9}}, {{PDB2|2fy7}}, {{PDB2|2fya}}, {{PDB2|2fyb}}
| Name = UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1
| HGNCid = 924
| Symbol = B4GALT1
| AltSymbols =; GTB; B4GAL-T1; DKFZp686N19253; GGTB2; GT1; MGC50983; beta4Gal-T1
| OMIM = 137060
| ECnumber =
| Homologene = 20378
| MGIid = 95705
  | GeneAtlas_image1 = PBB_GE_B4GALT1_201883_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_B4GALT1_201882_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_B4GALT1_211631_x_at_tn.png
  | Function = {{GNF_GO|id=GO:0003831 |text = beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity}} {{GNF_GO|id=GO:0003945 |text = N-acetyllactosamine synthase activity}} {{GNF_GO|id=GO:0004461 |text = lactose synthase activity}} {{GNF_GO|id=GO:0008378 |text = galactosyltransferase activity}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006012 |text = galactose metabolic process}} {{GNF_GO|id=GO:0009312 |text = oligosaccharide biosynthetic process}} {{GNF_GO|id=GO:0030198 |text = extracellular matrix organization and biogenesis}} {{GNF_GO|id=GO:0045136 |text = development of secondary sexual characteristics}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2683
    | Hs_Ensembl = ENSG00000086062
    | Hs_RefseqProtein = NP_001488
    | Hs_RefseqmRNA = NM_001497
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 33100635
    | Hs_GenLoc_end = 33157354
    | Hs_Uniprot = P15291
    | Mm_EntrezGene = 14595
    | Mm_Ensembl = ENSMUSG00000028413
    | Mm_RefseqmRNA = NM_022305
    | Mm_RefseqProtein = NP_071641
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 40993273
    | Mm_GenLoc_end = 41042669
    | Mm_Uniprot = Q05CE5
  }}
}}
'''UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1''', also known as '''B4GALT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2683| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose &lt;=&gt; UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5' end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase.<ref name="entrez">{{cite web | title = Entrez Gene: B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2683| accessdate = }}</ref>
| summary_text = This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose &lt;=&gt; UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5' end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Amado M, Almeida R, Schwientek T, Clausen H |title=Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. |journal=Biochim. Biophys. Acta |volume=1473 |issue= 1 |pages= 35-53 |year= 2000 |pmid= 10580128 |doi=  }}
*{{cite journal  | vauthors=Amado M, Almeida R, Schwientek T, Clausen H |title=Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. |journal=Biochim. Biophys. Acta |volume=1473 |issue= 1 |pages= 35–53 |year= 2000 |pmid= 10580128 |doi=  10.1016/S0304-4165(99)00168-3}}
*{{cite journal  | author=Gerber AC, Kozdrowski I, Wyss SR, Berger EG |title=The charge heterogeneity of soluble human galactosyltransferases isolated from milk, amniotic fluid and malignant ascites. |journal=Eur. J. Biochem. |volume=93 |issue= 3 |pages= 453-60 |year= 1979 |pmid= 33805 |doi=  }}
*{{cite journal  | vauthors=Gerber AC, Kozdrowski I, Wyss SR, Berger EG |title=The charge heterogeneity of soluble human galactosyltransferases isolated from milk, amniotic fluid and malignant ascites. |journal=Eur. J. Biochem. |volume=93 |issue= 3 |pages= 453–60 |year= 1979 |pmid= 33805 |doi=10.1111/j.1432-1033.1979.tb12843.x }}
*{{cite journal  | author=Uejima T, Uemura M, Nozawa S, Narimatsu H |title=Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. |journal=Cancer Res. |volume=52 |issue= 22 |pages= 6158-63 |year= 1992 |pmid= 1384956 |doi=  }}
*{{cite journal  | vauthors=Uejima T, Uemura M, Nozawa S, Narimatsu H |title=Complementary DNA cloning for galactosyltransferase associated with tumor and determination of antigenic epitopes recognized by specific monoclonal antibodies. |journal=Cancer Res. |volume=52 |issue= 22 |pages= 6158–63 |year= 1992 |pmid= 1384956 |doi=  }}
*{{cite journal  | author=Lopez LC, Youakim A, Evans SC, Shur BD |title=Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. |journal=J. Biol. Chem. |volume=266 |issue= 24 |pages= 15984-91 |year= 1991 |pmid= 1714903 |doi=  }}
*{{cite journal  | vauthors=Lopez LC, Youakim A, Evans SC, Shur BD |title=Evidence for a molecular distinction between Golgi and cell surface forms of beta 1,4-galactosyltransferase. |journal=J. Biol. Chem. |volume=266 |issue= 24 |pages= 15984–91 |year= 1991 |pmid= 1714903 |doi=  }}
*{{cite journal  | author=Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC |title=Genomic structure and expression of human beta-1,4-galactosyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1269-76 |year= 1991 |pmid= 1903938 |doi= }}
*{{cite journal  | vauthors=Mengle-Gaw L, McCoy-Haman MF, Tiemeier DC |title=Genomic structure and expression of human beta-1,4-galactosyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=176 |issue= 3 |pages= 1269–76 |year= 1991 |pmid= 1903938 |doi=10.1016/0006-291X(91)90423-5  }}
*{{cite journal  | author=Aoki D, Appert HE, Johnson D, ''et al.'' |title=Analysis of the substrate binding sites of human galactosyltransferase by protein engineering. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3171-8 |year= 1990 |pmid= 2120039 |doi=  }}
*{{cite journal  | vauthors=Aoki D, Appert HE, Johnson D |title=Analysis of the substrate binding sites of human galactosyltransferase by protein engineering |journal=EMBO J. |volume=9 |issue= 10 |pages= 3171–8 |year= 1990 |pmid= 2120039 |doi=  | pmc=552046  |display-authors=etal}}
*{{cite journal  | author=Watzele G, Berger EG |title=Near identity of HeLa cell galactosyltransferase with the human placental enzyme. |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7174 |year= 1991 |pmid= 2124683 |doi= }}
*{{cite journal  | vauthors=Watzele G, Berger EG |title=Near identity of HeLa cell galactosyltransferase with the human placental enzyme |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7174 |year= 1991 |pmid= 2124683 |doi=10.1093/nar/18.23.7174  | pmc=332820  }}
*{{cite journal  | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi=  }}
*{{cite journal  | vauthors=Kalyanaraman VS, Rodriguez V, Veronese F |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1 |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371–80 |year= 1990 |pmid= 2187500 |doi=10.1089/aid.1990.6.371 |display-authors=etal}}
*{{cite journal  | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi=  }}
*{{cite journal  | vauthors=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384–8 |year= 1989 |pmid= 2541446 |doi=10.1073/pnas.86.9.3384  | pmc=287137 }}
*{{cite journal  | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi=  }}
*{{cite journal  | vauthors=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452–6 |year= 1989 |pmid= 2542563 |doi= | pmc=250699 }}
*{{cite journal  | author=Kozarsky K, Penman M, Basiripour L, ''et al.'' |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein. |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163-9 |year= 1989 |pmid= 2649653 |doi=  }}
*{{cite journal  | vauthors=Kozarsky K, Penman M, Basiripour L |title=Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein |journal=J. Acquir. Immune Defic. Syndr. |volume=2 |issue= 2 |pages= 163–9 |year= 1989 |pmid= 2649653 |doi=  |display-authors=etal}}
*{{cite journal  | author=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis. |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265-82 |year= 1988 |pmid= 2829950 |doi=  }}
*{{cite journal  | vauthors=Robinson WE, Montefiori DC, Mitchell WM |title=Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis |journal=AIDS Res. Hum. Retroviruses |volume=3 |issue= 3 |pages= 265–82 |year= 1988 |pmid= 2829950 |doi=10.1089/aid.1987.3.265 }}
*{{cite journal  | author=Appert HE, Rutherford TJ, Tarr GE, ''et al.'' |title=Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence. |journal=Biochem. Biophys. Res. Commun. |volume=138 |issue= 1 |pages= 224-9 |year= 1986 |pmid= 3091013 |doi=  }}
*{{cite journal  | vauthors=Appert HE, Rutherford TJ, Tarr GE |title=Isolation of galactosyltransferase from human milk and the determination of its N-terminal amino acid sequence |journal=Biochem. Biophys. Res. Commun. |volume=138 |issue= 1 |pages= 224–9 |year= 1986 |pmid= 3091013 |doi=10.1016/0006-291X(86)90269-X |display-authors=etal}}
*{{cite journal  | author=Appert HE, Rutherford TJ, Tarr GE, ''et al.'' |title=Isolation of a cDNA coding for human galactosyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=139 |issue= 1 |pages= 163-8 |year= 1986 |pmid= 3094506 |doi=  }}
*{{cite journal  | vauthors=Appert HE, Rutherford TJ, Tarr GE |title=Isolation of a cDNA coding for human galactosyltransferase |journal=Biochem. Biophys. Res. Commun. |volume=139 |issue= 1 |pages= 163–8 |year= 1986 |pmid= 3094506 |doi=10.1016/S0006-291X(86)80094-8 |display-authors=etal}}
*{{cite journal  | author=Furukawa K, Roth S, Sawicki J |title=Several galactosyltransferase activities are associated with mouse chromosome 17. |journal=Genetics |volume=114 |issue= 3 |pages= 983-91 |year= 1987 |pmid= 3098628 |doi=  }}
*{{cite journal  | vauthors=Furukawa K, Roth S, Sawicki J |title=Several Galactosyltransferase Activities Are Associated with Mouse Chromosome 17 |journal=Genetics |volume=114 |issue= 3 |pages= 983–91 |year= 1987 |pmid= 3098628 |doi= | pmc=1203025 }}
*{{cite journal  | author=Masri KA, Appert HE, Fukuda MN |title=Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase). |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 2 |pages= 657-63 |year= 1989 |pmid= 3144273 |doi=  }}
*{{cite journal  | vauthors=Masri KA, Appert HE, Fukuda MN |title=Identification of the full-length coding sequence for human galactosyltransferase (beta-N-acetylglucosaminide: beta 1,4-galactosyltransferase) |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 2 |pages= 657–63 |year= 1989 |pmid= 3144273 |doi=10.1016/S0006-291X(88)80300-0 }}
*{{cite journal  | author=Roth J, Lentze MJ, Berger EG |title=Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells. |journal=J. Cell Biol. |volume=100 |issue= 1 |pages= 118-25 |year= 1985 |pmid= 3917437 |doi=  }}
*{{cite journal  | vauthors=Roth J, Lentze MJ, Berger EG |title=Immunocytochemical demonstration of ecto-galactosyltransferase in absorptive intestinal cells |journal=J. Cell Biol. |volume=100 |issue= 1 |pages= 118–25 |year= 1985 |pmid= 3917437 |doi=10.1083/jcb.100.1.118  | pmc=2113462 }}
*{{cite journal  | author=Roth J, Berger EG |title=Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae. |journal=J. Cell Biol. |volume=93 |issue= 1 |pages= 223-9 |year= 1982 |pmid= 6121819 |doi=  }}
*{{cite journal  | vauthors=Roth J, Berger EG |title=Immunocytochemical localization of galactosyltransferase in HeLa cells: codistribution with thiamine pyrophosphatase in trans-Golgi cisternae |journal=J. Cell Biol. |volume=93 |issue= 1 |pages= 223–9 |year= 1982 |pmid= 6121819 |doi=10.1083/jcb.93.1.223  | pmc=2112114 }}
*{{cite journal  | author=Chatterjee SK, Mukerjee S, Tripathi PK |title=Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones. |journal=Int. J. Biochem. Cell Biol. |volume=27 |issue= 3 |pages= 329-36 |year= 1995 |pmid= 7540104 |doi=  }}
*{{cite journal  | vauthors=Chatterjee SK, Mukerjee S, Tripathi PK |title=Analysis of the sequences of human beta-1,4-galactosyltransferase cDNA clones |journal=Int. J. Biochem. Cell Biol. |volume=27 |issue= 3 |pages= 329–36 |year= 1995 |pmid= 7540104 |doi=10.1016/1357-2725(94)00062-G }}
*{{cite journal  | author=Kudo T, Narimatsu H |title=The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells. |journal=Glycobiology |volume=5 |issue= 4 |pages= 397-403 |year= 1995 |pmid= 7579794 |doi=  }}
*{{cite journal  | vauthors=Kudo T, Narimatsu H |title=The beta 1,4-galactosyltransferase gene is post-transcriptionally regulated during differentiation of mouse F9 teratocarcinoma cells |journal=Glycobiology |volume=5 |issue= 4 |pages= 397–403 |year= 1995 |pmid= 7579794 |doi=10.1093/glycob/5.4.397 }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* [https://www.ncbi.nlm.nih.gov/books/NBK1332/  GeneReviews/NCBI/NIH/UW entry on Congenital Disorders of Glycosylation Overview]
* {{UCSC gene info|B4GALT1}}
 
{{PDB Gallery|geneid=2683}}
 
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Revision as of 02:24, 30 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Beta-1,4-galactosyltransferase 1 is an enzyme that in humans is encoded by the B4GALT1 gene.[1][2]

This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene is unique among the beta4GalT genes because it encodes an enzyme that participates both in glycoconjugate and lactose biosynthesis. For the first activity, the enzyme adds galactose to N-acetylglucosamine residues that are either monosaccharides or the nonreducing ends of glycoprotein carbohydrate chains. The second activity is restricted to lactating mammary tissues where the enzyme forms a heterodimer with alpha-lactalbumin to catalyze UDP-galactose + D-glucose <=> UDP + lactose. The two enzymatic forms result from alternate transcription initiation sites and post-translational processing. Two transcripts, which differ only at the 5' end, with approximate lengths of 4.1 kb and 3.9 kb encode the same protein. The longer transcript encodes the type II membrane-bound, trans-Golgi resident protein involved in glycoconjugate biosynthesis. The shorter transcript encodes a protein which is cleaved to form the soluble lactose synthase.[2]

References

  1. ↑ Lo NW, Shaper JH, Pevsner J, Shaper NL (Aug 1998). "The expanding beta 4-galactosyltransferase gene family: messages from the databanks". Glycobiology. 8 (5): 517–26. doi:10.1093/glycob/8.5.517. PMID 9597550.
  2. ↑ 2.0 2.1 "Entrez Gene: B4GALT1 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1".

Further reading

External links



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