ID:GALT2_HUMAN DESCRIPTION: RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2; EC=2.4.1.41; AltName: Full=Polypeptide GalNAc transferase 2; Short=GalNAc-T2; Short=pp-GaNTase 2; AltName: Full=Protein-UDP acetylgalactosaminyltransferase 2; AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2; Contains: RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2 soluble form; FUNCTION: Catalyzes 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 a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region. CATALYTIC ACTIVITY: UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. COFACTOR: Manganese (By similarity). COFACTOR: Calcium (By similarity). PATHWAY: Protein modification; protein glycosylation. SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note=Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists. TISSUE SPECIFICITY: Widely expressed. DOMAIN: There 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 (By similarity). DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity (By similarity). SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. SIMILARITY: Contains 1 ricin B-type lectin domain. WEB RESOURCE: Name=GGDB; Note=GlycoGene database; URL="http://riodb.ibase.aist.go.jp/rcmg/ggdb/"; WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Polypeptide N-acetylgalactosaminyltransferase 2; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_484";
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q10471
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0004653 polypeptide N-acetylgalactosaminyltransferase activity GO:0005515 protein binding GO:0016740 transferase activity GO:0016757 transferase activity, transferring glycosyl groups GO:0030145 manganese ion binding GO:0030246 carbohydrate binding GO:0046872 metal ion binding
Biological Process: GO:0002378 immunoglobulin biosynthetic process GO:0006486 protein glycosylation GO:0006493 protein O-linked glycosylation GO:0016266 O-glycan processing GO:0018242 protein O-linked glycosylation via serine GO:0018243 protein O-linked glycosylation via threonine