Search by BoMiProt ID - Bomi8143


Primary Information

BoMiProt ID Bomi8143
Protein Name Polypeptide N-acetylgalactosaminyltransferase 1/Polypeptide GalNAc transferase 1/Protein-UDP acetylgalactosaminyltransferase 1/UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Organism Bos taurus
Uniprot IDQ07537
Milk FractionWhey,MFGM
Ref Sequence ID NP_803485.1
Aminoacid Length 559
Molecular Weight 64192
FASTA Sequence Download
Gene Name GALNT1
Gene ID 282241
Protein Existence Status reviewed

Secondary Information

Protein Function Mucin-type O-glycan biosynthesis is regulated by the family of UDP-GalNAc polypeptide:N-acetylgalactosaminlytransfersases (ppGalNAcTs) that catalyzes the first step in the pathway by transferring GalNAc to Ser or Thr residues in a protein from the sugar donor UDP-GalNAc. 
Biochemical Properties Twenty distinct ppGalNAcT isoforms have been detected in humans and all but 4 have demonstrable catalytic activity.A corresponding set of 18 distinct ppGalNAcTs is expressed in mice.
PTMs Disulfide bond formation,N-Linked Glycosylation at Asn
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q07537|GALT1_BOVIN Polypeptide N-acetylgalactosaminyltransferase 1 OS=Bos taurus OX=9913 GN=GALNT1 PE=1 SV=1 MRKFAYCKVVLATSLIWVLLDMFLLLYFSECNKCDEKKERGLPAGDVLEPVQKPHEGPGE MGKPVVIPKEDQEKMKEMFKINQFNLMASEMIALN*95RSLPDVRLEGCKTKVYPDNLPTTSV VIVFHNEAWSTLLRTVHSVINRSPRHMLEEIVLVDDASERDFLKRPLESYVKKLKVPVHV IRMEQRSGLIRARLKGAAVSKGQVITFLDAHCECTVGWLEPLLARIKHDRKTVVCPIIDV ISDDTFEYMAGSDMTYGGFNWKLNFRWYPVPQREMDRRKGDRTLPVRTPTMAGGLFSIDR DYFQEIGTYDAGMDIWGGENLEISFRIWQCGGTLEIVTCSHVGHVFRKATPYTFPGGTGQ IINKNNRRLAEVWMDEFKNFFYIISPGVTKVDYGDISSRLGLRHKLQCRPFSWYLENIYP DSQIPRHYFSLGEIRNVETNQCLDNMARKENEKVGIFNCHGMGGNQVFSYTANKEIRTDD LCLDVSKLNGPVTMLKCHHLKGNQLWEYDPVKLTLQHVNSNQCLDKATDEDSQVPSIRDC SGSRSQQWLLRN*552VTLPEIF
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction 1TMH; (7-29)
Significance of PTMs N-glycosylated, contains two N-linked oligosaccharides.
Additional Comments ppGalNAcT-1 is highly expressed in bone, the hypothesis is that it might be involved in bone protein glycosylation and that a lack of ppGalNAcT-1 activity might result in underglycosylation of several glycoproteins expressed in the skeleton.
Bibliography 1.Miwa HE, Gerken TA, Jamison O, Tabak LA. Isoform-specific O-glycosylation of osteopontin and bone sialoprotein by polypeptide N-acetylgalactosaminyltransferase-1. J Biol Chem. 2010 Jan 8;285(2):1208-19. doi: 10.1074/jbc.M109.035436. Epub 2009 Oct 30. PMID: 19880513; PMCID: PMC2801249. 2. Tenno, M., Ohtsubo, K., Hagen, F. K., Ditto, D., Zarbock, A., Schaerli, P., von Andrian, U. H., Ley, K., Le, D., Tabak, L. A., and Marth, J. D. (2007) Mol. Cell. Biol. 27, 8783–8796. 3.