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MGP001152

UniProt Annotations

Entry Information
Gene Namepolypeptide N-acetylgalactosaminyltransferase 3
Protein EntryGALT3_HUMAN
UniProt IDQ14435
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q14435-1; Sequence=Displayed; Name=2; IsoId=Q14435-2; Sequence=VSP_011202, VSP_011203; Note=No experimental confirmation available.;
Catalytic ActivityUDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. {ECO:0000269|PubMed:8663203}.
CofactorName=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
DiseaseTumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement. {ECO:0000269|PubMed:15133511, ECO:0000269|PubMed:15599692}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainThere are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding. {ECO:0000250}.
DomainThe ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity. {ECO:0000250}.
FunctionCatalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D- galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis. {ECO:0000269|PubMed:16638743, ECO:0000269|PubMed:9295285}.
MiscellaneousOverexpressed in many differentiated carcinomas, suggesting that it may serve as a marker of tumor differentiation.
PathwayProtein modification; protein glycosylation.
Sequence CautionSequence=AAH56246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
SimilarityBelongs to the glycosyltransferase 2 family. GalNAc-T subfamily. {ECO:0000305}.
SimilarityContains 1 ricin B-type lectin domain. {ECO:0000255|PROSITE-ProRule:PRU00174}.
Subcellular LocationGolgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein {ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the trans and medial parts of the Golgi stack.
Tissue SpecificityExpressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon. Also expressed in placenta and lung and fetal lung and fetal kidney. {ECO:0000269|PubMed:12708471, ECO:0000269|PubMed:8663203}.
Web ResourceName=Functional Glycomics Gateway - GTase; Note=Polypeptide N-acetylgalactosaminyltransferase 3; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_485";
Web ResourceName=GGDB; Note=GlycoGene database; URL="http://jcggdb.jp/rcmg/ggdb/Homolog?cat=symbol&symbol=GALNT3";
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