Proton-coupled amino acid transporter 2 (SLC36A2 or PAT2) belongs to the solute carrier family 36. It is a rheogenic H+ coupled transporter for small, unbranched, dipolar amino and imino acids. The substrates of PAT2 include glycine, alanine, L- and D-proline, trans-4-hydroxyproline, sarcosine, and the amino acid derivative alpha(methyl)aminoisobutyric acid (MeAIB). The transport of SLC36A2 for amino acid derivatives has a narrower substrate selectivity but higher affinity than SLC36A1. In human, SLC36A2 mRNA expression is detected in the kidney and skeletal muscle. Specifically, it is expressed in the S1 segment of the proximal tubule close to the glomerulus. The transport of PAT2 is pH-dependent but the maximal transport is not likely to be altered greatly by changes within the range of pH 7.4-9.3. The gene SLC36A2 is located on human chromosome 5q33.1. The protein comprises 483 amino acids in length and structurally have 11 transmembrane domains.
|Basic Information of SLC36A2|
|Protein Name||Proton-coupled amino acid transporter 2|
|Gene Name||SLC36A2, PAT2, TRAMD1|
|Aliases||Solute carrier family 36 member 2Tramdorin-1|
|Organism||Homo sapiens (Human)|
SLC36A2 is expressed at the apical membrane in the renal proximal tubule and is one of the transport systems that are involved in reabsorption of amino acids and derivatives (glycine, proline, and hydroxyproline) from the renal filtrate. Mutations or dysfunction of this protein cause iminoglycinuria (characterized by excess urinary proline, hydroxyproline, and glycine) and hyperglycinuria (characterized by isolated excess urinary glycine). But studies have shown that the inheritance patterns of mutations leading to these disorders are complex. Further, the transport of drugs via this carrier will be affected, which, in turn, will influence the renal reabsorption and the pharmacokinetics of these drugs.
This study investigates the mechanism and substrate specificity of the PAT2 in 3T3-L1 cells using different substrates such as glycine, L-alanine, and L-tryptophan. The PAT2 is expressed in the 3T3-L1 adipocytes.
Using various proline, GABA and tryptophan derivatives, this study investigates if they function either as transported substrates or non-transported inhibitors of PAT2 following heterologous expression of rat PAT2 in Xenopus laevis oocytes.
This study identifies the membrane surface protein PAT2, together with ASC-1 and P2RX5, like new cell surface markers of adipose cell types using a combination of in silico, in vitro, and in vivo methods.
This study investigates the tissue distribution of the PAT2 protein. The results show that this protein is expressed in the spinal cord and brain, contributing to neuronal transport and sequestration of amino acids. The transport direction can be bidirectional, which is dependent on different forces like substrate concentration, pH gradient, and membrane potential.
This study identifies the transporters that are involved in developmental iminoglycinuria and their contribution to renal reabsorption capacity. In addition, the results show that the Slc6a18, Slc6a19, Slc6a20a, and Slc36a2 have delayed expression and maturation in neonatal mice, which might be the molecular mechanism of developmental iminoglycinuria.
Creative Biolabs has spent years of efforts in the field of membrane protein preparation and reconstitution, and we have successfully established a powerful Magic™ Membrane Protein Production Platform that integrates a wide spectrum of strategies and approaches. The proteins can be prepared with or without the aid of detergents. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC36A2 antibody development services.
Contact us or inquire us if you want to know more about our membrane protein-related services.
All listed customized services & products are for research use only, not intended for pharmaceutical, diagnostic, therapeutic or any in vivo human use.