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Identification
HMDB Protein ID HMDBP00995
Secondary Accession Numbers
  • 6283
Name Polypeptide N-acetylgalactosaminyltransferase 3
Synonyms
  1. GalNAc-T3
  2. Polypeptide GalNAc transferase 3
  3. Protein-UDP acetylgalactosaminyltransferase 3
  4. UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
  5. pp-GaNTase 3
Gene Name GALNT3
Protein Type Unknown
Biological Properties
General Function Cell wall/membrane/envelope biogenesis
Specific 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 activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis.
Pathways
  • Mucin type O-Glycan biosynthesis
  • protein glycosylation
Reactions
UDP-N-acetyl-alpha-D-galactosamine + polypeptide → Uridine 5'-diphosphate + N-acetyl-alpha-D-galactosaminyl-polypeptide details
UDP-N-acetyl-D-galactosamine + Protein serine → UDP + Tn antigen details
GO Classification
Biological Process
O-glycan processing
post-translational protein modification
protein O-linked glycosylation via serine
protein O-linked glycosylation via threonine
Cellular Component
Golgi cisterna membrane
perinuclear region of cytoplasm
nucleus
integral to membrane
Golgi membrane
Molecular Function
manganese ion binding
polypeptide N-acetylgalactosaminyltransferase activity
calcium ion binding
Cellular Location
  1. Single-pass type II membrane protein
  2. Golgi apparatus
  3. Golgi stack membrane
Gene Properties
Chromosome Location 2
Locus 2q24-q31
SNPs GALNT3
Gene Sequence
>1902 bp
ATGGCTCACCTAAAGCGACTAGTAAAATTACACATTAAAAGACATTACCATAAAAAGTTC
TGGAAGCTTGGTGCAGTAATTTTTTTCTTTATAATAGTTTTGGTTTTAATGCAAAGAGAA
GTAAGTGTTCAATATTCCAAAGAGGAATCAAGGATGGAAAGGAACATGAAAAACAAAAAC
AAGATGTTGGATTTAATGCTAGAAGCTGTAAACAATATTAAGGATGCCATGCCAAAAATG
CAAATAGGAGCACCTGTCAGGCAAAACATTGATGCTGGTGAGAGACCTTGTTTGCAAGGA
TATTATACAGCAGCAGAATTGAAGCCTGTCCTTGACCGTCCACCTCAGGATTCAAATGCA
CCTGGTGCTTCTGGTAAAGCATTCAAGACAACCAATTTAAGTGTTGAAGAGCAAAAGGAA
AAGGAACGTGGGGAAGCTAAACACTGCTTTAATGCTTTCGCAAGTGACAGGATTTCTTTG
CACCGAGATCTTGGACCAGACACTCGACCTCCTGAATGTATTGAACAAAAATTTAAGCGC
TGCCCTCCCCTGCCCACCACCAGTGTCATAATAGTTTTTCATAATGAAGCGTGGTCCACG
TTGCTTAGAACTGTCCACAGTGTGCTCTATTCTTCACCTGCAATACTGCTGAAGGAAATC
ATTTTGGTGGATGATGCTAGTGTAGATGAGTACTTACATGATAAACTAGATGAATATGTA
AAACAATTTTCTATAGTAAAAATAGTCAGACAAAGAGAAAGAAAAGGTCTGATCACTGCT
CGGTTGCTAGGAGCAACAGTCGCAACAGCTGAAACGCTCACATTTTTAGATGCTCACTGT
GAGTGTTTCTATGGTTGGCTAGAACCTCTGTTGGCCAGAATAGCTGAGAACTACACGGCT
GTCGTAAGTCCAGATATTGCATCCATAGATCTGAACACGTTTGAATTCAACAAACCTTCT
CCTTATGGAAGTAACCATAACCGTGGAAATTTTGACTGGAGTCTTTCATTTGGCTGGGAG
TCGCTTCCTGATCATGAGAAGCAAAGAAGGAAAGATGAAACCTACCCAATTAAAACACCC
ACTTTTGCAGGAGGACTTTTTTCCATATCAAAAGAATATTTTGAGTATATTGGAAGCTAT
GATGAAGAAATGGAAATCTGGGGAGGTGAAAATATAGAAATGTCTTTCAGAGTATGGCAA
TGTGGTGGGCAGTTGGAGATTATGCCTTGCTCTGTTGTTGGACATGTTTTTCGCAGCAAA
AGCCCTCATAGCTTTCCAAAAGGCACTCAGGTGATTGCTAGAAACCAAGTTCGCCTTGCA
GAAGTCTGGATGGATGAATACAAGGAAATATTTTATAGGAGAAATACAGATGCAGCAAAA
ATTGTTAAACAAAAAGCATTTGGTGATCTTTCAAAAAGATTTGAAATAAAACACCGCCTT
CAGTGTAAAAATTTTACATGGTATCTGAACAACATTTATCCAGAGGTGTATGTGCCAGAC
CTTAATCCTGTTATATCTGGATACATTAAAAGCGTTGGTCAGCCTCTATGTCTGGATGTT
GGAGAAAACAATCAAGGAGGCAAACCATTAATTATGTATACATGTCATGGACTTGGGGGA
AACCAGTACTTTGAATACTCTGCTCAACATGAAATTCGGCACAACATCCAGAAGGAATTA
TGTCTTCATGCTGCTCAAGGTCTCGTTCAGCTGAAGGCATGTACCTACAAAGGTCACAAG
ACAGTTGTCACTGGAGAGCAGATATGGGAGATCCAGAAGGATCAACTTCTATACAATCCA
TTCTTAAAAATGTGCCTTTCAGCAAATGGAGAGCATCCAAGTTTAGTGTCATGCAACCCA
TCAGATCCACTCCAAAAATGGATACTTAGCCAAAATGATTAA
Protein Properties
Number of Residues 633
Molecular Weight 72609.79
Theoretical pI 7.983
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Polypeptide N-acetylgalactosaminyltransferase 3
MAHLKRLVKLHIKRHYHKKFWKLGAVIFFFIIVLVLMQREVSVQYSKEESRMERNMKNKN
KMLDLMLEAVNNIKDAMPKMQIGAPVRQNIDAGERPCLQGYYTAAELKPVLDRPPQDSNA
PGASGKAFKTTNLSVEEQKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKR
CPPLPTTSVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLDEYV
KQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWLEPLLARIAENYTA
VVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSFGWESLPDHEKQRRKDETYPIKTP
TFAGGLFSISKEYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSK
SPHSFPKGTQVIARNQVRLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRL
QCKNFTWYLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHGLGG
NQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQIWEIQKDQLLYNP
FLKMCLSANGEHPSLVSCNPSDPLQKWILSQND
GenBank ID Protein 62822129
UniProtKB/Swiss-Prot ID Q14435
UniProtKB/Swiss-Prot Entry Name GALT3_HUMAN
PDB IDs Not Available
GenBank Gene ID AC009495
GeneCard ID GALNT3
GenAtlas ID GALNT3
HGNC ID HGNC:4125
References
General References
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  3. Bennett EP, Hassan H, Clausen H: cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine. Polypeptide N-acetylgalactosaminyltransferase, GalNAc-t3. J Biol Chem. 1996 Jul 19;271(29):17006-12. [PubMed:8663203 ]
  4. Wandall HH, Hassan H, Mirgorodskaya E, Kristensen AK, Roepstorff P, Bennett EP, Nielsen PA, Hollingsworth MA, Burchell J, Taylor-Papadimitriou J, Clausen H: Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [PubMed:9295285 ]
  5. Rottger S, White J, Wandall HH, Olivo JC, Stark A, Bennett EP, Whitehouse C, Berger EG, Clausen H, Nilsson T: Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus. J Cell Sci. 1998 Jan;111 ( Pt 1):45-60. [PubMed:9394011 ]
  6. Onitsuka K, Shibao K, Nakayama Y, Minagawa N, Hirata K, Izumi H, Matsuo K, Nagata N, Kitazato K, Kohno K, Itoh H: Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma. Cancer Sci. 2003 Jan;94(1):32-6. [PubMed:12708471 ]
  7. Topaz O, Shurman DL, Bergman R, Indelman M, Ratajczak P, Mizrachi M, Khamaysi Z, Behar D, Petronius D, Friedman V, Zelikovic I, Raimer S, Metzker A, Richard G, Sprecher E: Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis. Nat Genet. 2004 Jun;36(6):579-81. Epub 2004 May 9. [PubMed:15133511 ]
  8. Frishberg Y, Topaz O, Bergman R, Behar D, Fisher D, Gordon D, Richard G, Sprecher E: Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders. J Mol Med (Berl). 2005 Jan;83(1):33-8. Epub 2004 Dec 15. [PubMed:15599692 ]
  9. Kato K, Jeanneau C, Tarp MA, Benet-Pages A, Lorenz-Depiereux B, Bennett EP, Mandel U, Strom TM, Clausen H: Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation. J Biol Chem. 2006 Jul 7;281(27):18370-7. Epub 2006 Apr 25. [PubMed:16638743 ]