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sialyltransferase 6; N-acetyllactosaminide alpha-2,3-sialyltransferase; CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase; Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase (ST3N, ST3GalII, SIAT6, ST3GAL3)

Function: - catalyzes the formation of the neuAc-alpha-2,3-gal-beta-1,4-GlcNAc-, neuAc-alpha-2,3-gal-beta-1,3-GlcNAc- or neuAc-alpha-2,3-gal-beta-1,3-galNAc- sequences found in terminal carbohydrate groups of glycoproteins & glycolipids - highest activity is toward gal-beta-1,3-GlcNAc & the lowest toward gal-beta-1,3-galNAc (putative) - protein modification; protein glycosylation - the soluble form derives from the membrane form by proteolytic processing CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl-glycoprotein CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N- acetyl-D-glucosaminyl-glycoprotein Structure: belongs to the glycosyltransferase 29 family Compartment: - Golgi, Golgi stack membrane - secreted - membrane-bound form in trans cisternae of Golgi - secreted into the body fluid Alternative splicing: named isoforms=26 Expression: - highly expressed in adult skeletal muscle & in all fetal tissues examined & to a much lesser extent in placenta, lung & liver

General

galactosyltransferase glycoprotein membrane protein sialyltransferase

Properties

SIZE: entity length = 375 aa MW = 42 kD COMPARTMENT: golgi MOTIF: transmembrane domain {9-28} N-glycosylation site {N80} cysteine residue {C160} MODIFICATION: cysteine residue {C314} N-glycosylation site {N171} cysteine residue {C314} MODIFICATION: cysteine residue {C160}

Database Correlations

OMIM 606494 UniProt Q11203 Pfam PF00777 Entrez Gene 6487 Kegg hsa:6487 ENZYME 2.4.99.6

References

  1. UniProt :accession Q11203
  2. GGDB; Note: glycogene database http://ggdb.muse.aist.go.jp/GGDB/index.jsp