ID:GLTL2_HUMAN DESCRIPTION: RecName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 2; EC=2.4.1.41; AltName: Full=Polypeptide GalNAc transferase-like protein 2; Short=GalNAc-T-like protein 2; Short=pp-GaNTase-like protein 2; AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 2; AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2; 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate. 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 membrane; Single-pass type II membrane protein (By similarity). TISSUE SPECIFICITY: Widely expressed. Highly expressed in small intestine, placenta, spleen, cerebral cortex and ovary. Expressed at intermediate level in uterus, mammary gland, stomach, cerebellum and whole brain. Weakly expressed in fetal brain, bone marrow, thyroid gland, thymus, heart, skeletal muscle, lung, liver, colon, pancreas, kidney and testis. Not expressed in leukocyte. Expressed in both normal and osteoarthritic cartilage. Expressed at low level in chondrocytes in all zones of both normal and osteoarthritic cartilage. 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. CAUTION: Was originally (PubMed:15147861) termed Galnt15/pp- GaNTase 15. SEQUENCE CAUTION: Sequence=CAD89983.1; Type=Frameshift; Positions=169, 192, 206, 222, 270; 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-like protein 2; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_501";
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 Q8N3T1
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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.
Protein Q8N3T1 (Reactome details) participates in the following event(s):
R-HSA-913675 GALNTs transfer GalNAc from UDP-GalNAc to mucins to form Tn antigens R-HSA-913709 O-linked glycosylation of mucins R-HSA-5173105 O-linked glycosylation R-HSA-597592 Post-translational protein modification R-HSA-392499 Metabolism of proteins
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Sequence and Links to Tools and Databases 
Common Gene Haplotype Alleles 
