Structural highlights
Disease
S17A5_HUMAN Salla disease;Intermediate severe Salla disease;Free sialic acid storage disease, infantile form. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry.
Function
S17A5_HUMAN Multifunctional anion transporter that operates via two distinct transport mechanisms, namely proton-coupled anion cotransport and membrane potential-dependent anion transport (PubMed:15510212, PubMed:21781115, PubMed:22778404, PubMed:23889254). Electroneutral proton-coupled acidic monosaccharide symporter, with a sugar to proton stoichiometry of 1:1. Exports glucuronic acid and free sialic acid derived from sialoglycoconjugate degradation out of lysosomes, driven by outwardly directed lysosomal pH gradient. May regulate lysosome function and metabolism of sialylated conjugates that impact oligodendrocyte lineage differentiation and myelinogenesis in the central nervous system (By similarity) (PubMed:15510212, PubMed:21781115, PubMed:22778404, PubMed:23889254). Electrogenic proton-coupled nitrate symporter that transports nitrate ions across the basolateral membrane of salivary gland acinar cells, with nitrate to proton stoichiometry of 2:1. May contribute to nitrate clearance from serum by salivary glands, where it is further concentrated and secreted in the saliva (PubMed:22778404). Uses membrane potential to drive the uptake of acidic amino acids and peptides into synaptic vesicles. Responsible for synaptic vesicular storage of L-aspartate and L-glutamate in pinealocytes as well as vesicular uptake of N-acetyl-L-aspartyl-L-glutamate neuropeptide, relevant to aspartegic-associated glutamatergic neurotransmission and activation of metabotropic receptors that inhibit subsequent transmitter release (By similarity) (PubMed:21781115, PubMed:22778404, PubMed:23889254).[UniProtKB:Q5Q0U0][UniProtKB:Q8BN82][1] [2] [3] [4] Receptor for CM101, a polysaccharide produced by group B Streptococcus with antipathoangiogenic properties.[UniProtKB:Q9MZD1]
References
- ↑ Morin P, Sagne C, Gasnier B. Functional characterization of wild-type and mutant human sialin. EMBO J. 2004 Nov 24;23(23):4560-70. doi: 10.1038/sj.emboj.7600464. Epub 2004 Oct , 28. PMID:15510212 doi:http://dx.doi.org/10.1038/sj.emboj.7600464
- ↑ Miyaji T, Omote H, Moriyama Y. Functional characterization of vesicular excitatory amino acid transport by human sialin. J Neurochem. 2011 Oct;119(1):1-5. doi: 10.1111/j.1471-4159.2011.07388.x. Epub , 2011 Aug 22. PMID:21781115 doi:http://dx.doi.org/10.1111/j.1471-4159.2011.07388.x
- ↑ Qin L, Liu X, Sun Q, Fan Z, Xia D, Ding G, Ong HL, Adams D, Gahl WA, Zheng C, Qi S, Jin L, Zhang C, Gu L, He J, Deng D, Ambudkar IS, Wang S. Sialin (SLC17A5) functions as a nitrate transporter in the plasma membrane. Proc Natl Acad Sci U S A. 2012 Aug 14;109(33):13434-9. doi: , 10.1073/pnas.1116633109. Epub 2012 Jul 9. PMID:22778404 doi:http://dx.doi.org/10.1073/pnas.1116633109
- ↑ Lodder-Gadaczek J, Gieselmann V, Eckhardt M. Vesicular uptake of N-acetylaspartylglutamate is catalysed by sialin (SLC17A5). Biochem J. 2013 Aug 15;454(1):31-8. PMID:23889254 doi:10.1042/BJ20130300
