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MGP004437

UniProt Annotations

Entry Information
Gene Namebeta-1,4-glucuronyltransferase 1
Protein EntryB4GA1_HUMAN
UniProt IDO43505
SpeciesHuman
Comments
Comment typeDescription
Biophysicochemical PropertiespH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:25279699};
CautionWas initially characterized as a beta-1,3-N- acetylglucosaminyltransferase involved in the synthesis of poly-N- acetyllactosamine, able to initiate the synthesis or the elongation of the linear poly-N-acetyllactosaminoglycans (PubMed:9405606). However, it was later shown that it acts as a beta-1,4-glucuronyltransferase (PubMed:25279699, PubMed:25279697). {ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000305|PubMed:9405606}.
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25279699};
DiseaseMuscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A13 (MDDGA13) [MIM:615287]: An autosomal recessive disorder characterized by congenital muscular dystrophy associated with cobblestone lissencephaly and other brain anomalies, eye malformations, profound mental retardation, and death usually in the first years of life. Included diseases are the more severe Walker-Warburg syndrome and the slightly less severe muscle-eye-brain disease. {ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:23877401}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionBeta-1,4-glucuronyltransferase involved in O- mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE, during synthesis of phosphorylated O- mannosyl glycan (PubMed:25279699, PubMed:25279697). Phosphorylated O-mannosyl glycan is a carbohydrate is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity (PubMed:25279699, PubMed:25279697). Required for axon guidance; via its function in O-mannosylation of alpha- dystroglycan (DAG1) (By similarity). {ECO:0000250|UniProtKB:Q8BWP8, ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}.
PathwayProtein modification; protein glycosylation. {ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:9405606}.
SimilarityBelongs to the glycosyltransferase 49 family. {ECO:0000305}.
Subcellular LocationGolgi apparatus membrane {ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:23359570}. Note=Localizes near the trans-Golgi apparatus. {ECO:0000269|PubMed:25279699}.
SubunitInteracts with LARGE and GYLTL1B/LARGE2. {ECO:0000269|PubMed:19587235}.
Tissue SpecificityIn the adult, highly expressed in heart, brain, skeletal muscle and kidney and to a lesser extent in placenta, pancreas, spleen, prostate, testis, ovary, small intestine and colon. Very weak expression in lung, liver, thymus and peripheral blood leukocytes. In fetal highly expressed in brain and kidney and to a lesser extent in lung and liver. {ECO:0000269|PubMed:9405606}.
Web ResourceName=Functional Glycomics Gateway - GTase; Note=N- acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_547";
Web ResourceName=GGDB; Note=GlycoGene database; URL="http://jcggdb.jp/rcmg/ggdb/Homolog?cat=symbol&symbol=B3GNT1";
Web ResourceName=SeattleSNPs; URL="http://pga.gs.washington.edu/data/b3gnt6/";
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