SLC17A5 Membrane Protein Introduction

Introduction of SLC17A5

The solute family 17 (anion/sugar carrier), member 5, is a protein encoded by the SLC17A5 gene in humans. It is also known as SLC17A5 or sialin. The lysogenic acid and free sialic acid separated from the lysosome are separated from the lysate, which is a necessary condition for the myelination of the normal central nervous system. The potential dependence of aspartate and glutamate membranes is absorbed into synaptic vesicles and synaptic-like microvesicles. At the same time, in the serosal membrane of salivary gland acinar cells, it can also act as an electrical 2NO^3-/H⁺ transporter to regulate physiological nitrate effluent, and 25% of circulating nitrate ions are usually removed and secreted in saliva.

Basic Information of SLC17A5
Protein Name	Sialin
Gene Name	SLC17A5
Aliases	H(+)/sialic acid cotransporter, AST, Membrane glycoprotein HP59, Solute carrier family 17 member 5, Vesicular H(+)/Aspartate-glutamate cotransporter
Organism	Homo sapiens (Human)
UniProt ID	Q9NRA2
Transmembrane Times	12
Length (aa)	495
Sequence	MRSPVRDLARNDGEESTDRTPLLPGAPRAEAAPVCCSARYNLAILAFFGFFIVYALRVNLSVALVDMVDSNTTLEDNRTSKACPEHSAPIKVHHNQTGKKYQWDAETQGWILGSFFYGYIITQIPGGYVASKIGGKMLLGFGILGTAVLTLFTPIAADLGVGPLIVLRALEGLGEGVTFPAMHAMWSSWAPPLERSKLLSISYAGAQLGTVISLPLSGIICYYMNWTYVFYFFGTIGIFWFLLWIWLVSDTPQKHKRISHYEKEYILSSLRNQLSSQKSVPWVPILKSLPLWAIVVAHFSYNWTFYTLLTLLPTYMKEILRFNVQENGFLSSLPYLGSWLCMILSGQAADNLRAKWNFSTLCVRRIFSLIGMIGPAVFLVAAGFIGCDYSLAVAFLTISTTLGGFCSSGFSINHLDIAPSYAGILLGITNTFATIPGMVGPVIAKSLTPDNTVGEWQTVFYIAAAINVFGAIFFTLFAKGEVQNWALNDHHGHRH

Function of SLC17A5 Protein

SLC17A5 is a lysosomal membrane sialic acid transport protein encoded by the SLC17A5 gene on chromosome 6 in humans. The lack of protein leads to Salla disease and infant sialic acid storage disease (ISSD). The gene for HP59 is completely within its coding region, the Sialin gene SLC17A5. Infant sialic acid storage disease (ISSD) is a lysosomal storage disease characterized by the accumulation of covalent unchained (free) sialic acid in multiple tissues. ISSD and Salla disease (a major neurological disorder) is an allelic disorder caused by a recessive mutation in the lysosomal anionic monosaccharide transporter, SLC17A5.

SLC17A5 Membrane Protein Introduction Fig.1 The structure of SLC17A5 Protein.

Application of SLC17A5 Protein in Literature

Zielonka M., et al. A cross-sectional quantitative analysis of the natural history of free sialic acid storage disease-an ultra-orphan multisystemic lysosomal storage disorder. Genetics in Medicine. 2018,7. PubMed ID: 29875421

This article reveals that combinations of neurological symptoms, visceral enlargement, malformation, and/or non-immune water corpus should be specifically tested for SASD in a timely manner to reduce diagnostic delay.
Kang, E., et al. Biochemical and molecular analyses of infantile sialic acid storage disease in a patient with nonimmune hydrops fetalis. Clinica chimica acta; international journal of clinical chemistry.2018, 482. PubMed ID: 29654786

The clinical research shows that the patient is compound heterozygous of the c.908G>A (p.Trp303Ter) and the splicing mutation c.1259+5G>T (IVS9+5 G>T) in the SLC17A5 gene.
Tarailograovac, M., et al. Identification of a large intronic transposal insertion inSLC17A5causing sialic acid storage disease. Orphanet Journal of Rare Diseases.2017 (12.1):28. PubMed ID: 28187749

This study describes a novel pathogenic variant of SLC17A5, a translocation inserted in a patient with mild biochemical and clinical phenotypes.
Lines, M. A., et al. Infantile Sialic Acid Storage Disease: Two Unrelated Inuit Cases Homozygous for a Common Novel SLC17A5 Mutation. JIMD Reports. 2014 (12): 79–84. PubMed ID: 23900835

These findings raise the possibility that in this population, a common founder mutation appears as hydrops. Furthermore, significant confirmation of the neuraminidase activity may be helpful in the clinical diagnosis of ISSD if confirmed in subsequent cases.
Loddergadaczek J. V., et al. Vesicular uptake of N-acetylaspartylglutamate is catalysed by sialin (SLC17A5). Biochemical Journal. 2013 (454.1):31-38. PubMed ID: 23889254

This study shows that SLC17A5 is most probably the major and possibly only vesicular transporter for NAAG and NAAG2 because ATP-dependent transport of both peptides has not been detected in vesicles isolated from sialin-deficient mice.

SLC17A5 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC17A5 antibody development services.

Creative Biolabs' skillful scientists are glad to leverage our expertise and advanced technologies to help you with the member protein research. If you are interested, please feel free to contact us for more details.

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

	USA: Europe: Germany:
	Call us at: USA: UK: Germany:
	Fax:
	Email: