Human ST6GAL1 (NP_003023) VersaClone cDNA Summary
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Background: ST6 Gal Sialyltransferase 1/ST6GAL1
ST6GAL1 (beta-Galactoside alpha-2,6 Sialyltransferase 1; also known as alpha-2,6-ST) is a 48-53 kDa member of the Glycosyltransferase-29 family of proteins. It is one of two alpha-2,6-STs, the first being ST6GAL1 that is widely expressed, and the second being ST6Gal2 that shows neuronal expression. Both enzymes catalyze the transfer of sialic acid to a Gal residue via a 2,6 linkage. Human ST6GAL1 is a 406 amino acid (aa) type II transmembrane protein that resides in the Golgi membrane. Here it participates in the formation of homo- and heteromeric complexes where it is responsible for the sialylation of both membrane-bound and secreted glycoproteins. ST6Gal1 contains a short cytoplasmic tail (aa 1-9) and an extended luminal domain (aa 27-406) that possesses a phosphorylation site at Tyr369. ST6GAL1 reportedly can undergo undergo cleavage to generate a soluble fragment. Depending upon the enzyme involved, both smaller (37-41 kDa) and larger (55 kDa) fragments (relative to the full-length Golgi membrane form) have been reported, the differences possibly due to post-cleavage glycosylation. There is one potential alternative start site at Met232. Over aa 27-406 human ST6Gal1 shares 79% aa sequence identity with mouse ST6GAL1; by contrast, human ST6GAL1 and ST6GAL2 share only 35% aa sequence identity.
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