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HighlightsSodium-coupled neutral amino acid transporter 5 (SNAT5 or SLC38A5) belongs to the system N subfamily of amino acid transporter family. SLC38A5 shares 61% sequence identity to SLC38A3, which was the first identified system N transporter. Like SLC38A3, SLC38A5 transports zwitterionic amino acids in a Na+-dependent and markedly pH-sensitive manner, displaying limited substrate specificity with a preference for glutamine > histidine > asparagine. SLC38A5 is expressed in the brain and found in astrocytes. Additionally, SLC38A5 is found in other tissues such as the stomach, with very high expression, as well as the lungs, spleen, and colon. Structurally, this protein is demonstrated to have 11 transmembrane segments.
| Basic Information of SLC38A5 | |
| Protein Name | Sodium-coupled neutral amino acid transporter 5 |
| Gene Name | SLC38A5 |
| Aliases | Solute carrier family 38 member 5, System N transporter 2, JM24, SN2, SNAT5 |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q8WUX1 |
| Transmembrane Times | 11 |
| Length (aa) | 472 |
| Sequence | MELQDPKMNGALPSDAVGYRQEREGFLPSRGPAPGSKPVQFMDFEGKTSFGMSVFNLSNAIMGSGILGLAYAMAHTGVIFFLALLLCIALLSSYSIHLLLTCAGIAGIRAYEQLGQRAFGPAGKVVVATVICLHNVGAMSSYLFIIKSELPLVIGTFLYMDPEGDWFLKGNLLIIIVSVLIILPLALMKHLGYLGYTSGLSLTCMLFFLVSVIYKKFQLGCAIGHNETAMESEALVGLPSQGLNSSCEAQMFTVDSQMSYTVPIMAFAFVCHPEVLPIYTELCRPSKRRMQAVANVSIGAMFCMYGLTATFGYLTFYSSVKAEMLHMYSQKDPLILCVRLAVLLAVTLTVPVVLFPIRRALQQLLFPGKAFSWPRHVAIALILLVLVNVLVICVPTIRDIFGVIGSTSAPSLIFILPSIFYLRIVPSEVEPFLSWPKIQALCFGVLGVLFMAVSLGFMFANWATGQSRMSGH |
SLC38A5 is tightly associated with synapses in the brain, together with SNAT3, and participates in the function of the glutamine- GABA-glutamate cycle, being responsible for the glutamine release from the astrocytes in the intercellular space. Moreover, studies have reported that it might contribute to the regulation of glycine concentration in glutamatergic synapses and, therefore, to the functioning of the N-methyl-d-aspartate (NMDA) subtype of glutamate receptors. Besides, in periportal hepatocytes, SLC38A3 and SLC38A5 are likely to be involved in the uptake of glutamine. SLC38A5 is also expressed in the kidney where it is probably involved in ammoniagenesis especially during metabolic acidosis.
This study analyzed the profile of SNAT5 expression during development in comparison with that of other transporters involved in amino acid fluxes in the glutamatergic system. The results showed that the ontogenic emergence of SNAT5 in glial cells occurred in a concerted manner with other glutamate and glutamine transporters.
This study sought to determine the mechanism of regulation of Na-nutrient cotransporter SNAT5 by arachidonic acid metabolites in crypt cells. The findings provided evidence that SNAT5 stimulation in crypt cells was mediated by the leukotriene pathway during chronic intestinal inflammation.
This study investigated the mechanism by which an incretin unresponsive state transforms into an incretin responsive state using the spheroid clusters (K20-SC) as a model. The results showed that the suppression of SNAT5 activity resulted in increased glutamate production and that enhancement of cAMP signaling endowed incretin unresponsive β-cells with incretin responsiveness.
This article reported that rat SNAT5 mediated electroneutral and bidirectional transport of glutamine and glycine at perisynaptic astroglial membranes. It was suggested that this transporter functioned as both a transmitter precursor furnisher and a potential regulator of NMDA receptors.
This study sought to determine the regulation of B0AT1 and SNAT5 by mast cells during chronic enteritis using male rabbit models with chronic intestinal inflammation. The results showed that mast cells probably functioned as a regulator of the B0AT1 in villus cells and SN2 in crypts cells.
Based on our leading-edge Magic™ Membrane Protein Production Platform, Creative Biolabs can offer the most comprehensive one-stop, custom-specific membrane protein production services, including membrane protein expression using both cell-based and cell-free approaches, membrane protein reconstitution in various mimetics, and stably-transfected cells that overexpress your membrane proteins.
Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC38A5 antibody development services.
Contact us if you want to know more about our membrane protein-related services.
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