Human Gene GALNT7 (uc003isz.4) Description and Page Index
Description: Homo sapiens UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 7 (GalNAc-T7) (GALNT7), mRNA. RefSeq Summary (NM_017423): This gene encodes GalNAc transferase 7, a member of the GalNAc-transferase family. The enzyme encoded by this gene controls the initiation step of mucin-type O-linked protein glycosylation and transfer of N-acetylgalactosamine to serine and threonine amino acid residues. This enzyme is a type II transmembrane protein and shares common sequence motifs with other family members. Unlike other family members, this enzyme shows exclusive specificity for partially GalNAc-glycosylated acceptor substrates and shows no activity with non-glycosylated peptides. This protein may function as a follow-up enzyme in the initiation step of O-glycosylation. [provided by RefSeq, Jul 2008]. ##Evidence-Data-START## Transcript exon combination :: AJ002744.1, BC047468.1 [ECO:0000332] RNAseq introns :: single sample supports all introns SAMEA1965299, SAMEA1966682 [ECO:0000348] ##Evidence-Data-END## ##RefSeq-Attributes-START## MANE Ensembl match :: ENST00000265000.9/ ENSP00000265000.4 RefSeq Select criteria :: based on conservation, expression, longest protein ##RefSeq-Attributes-END## Transcript (Including UTRs) Position: hg19 chr4:174,089,904-174,245,118 Size: 155,215 Total Exon Count: 12 Strand: + Coding Region Position: hg19 chr4:174,089,987-174,242,868 Size: 152,882 Coding Exon Count: 12
ID:GALT7_HUMAN DESCRIPTION: RecName: Full=N-acetylgalactosaminyltransferase 7; EC=2.4.1.-; AltName: Full=Polypeptide GalNAc transferase 7; Short=GalNAc-T7; Short=pp-GaNTase 7; AltName: Full=Protein-UDP acetylgalactosaminyltransferase 7; AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7; FUNCTION: Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. 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. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS. 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=N- acetylgalactosaminyltransferase 7; URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_489";
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 Q86SF2
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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.