SLC38A4 Membrane Protein Introduction

Introduction of SLC38A4

Sodium-coupled neutral amino acid transporter 4 (SNAT4, SLC38A4) belongs to the SNAT family of transporters that mediate the transport of neutral amino acids essential for cellular functions. They are classified into two subfamilies - system A and system N. SLC38A4 exhibits functional and regulatory properties of classically defined system A subfamily. It contains 547 amino acid residues with a predicted molecular mass of 55 kDa. SLC38A4 predominantly transports L-alanine followed by L-histidine and L-glutamine. Studies have suggested that SLC38A4 transports amino acids in both sodium-dependent and sodium-independent manner. For tissue distribution, it is primarily expressed in the liver, muscle, and placenta. The topological study has shown that SLC38A4 consists of ten transmembrane segments with both N and C termini facing the extracellular side.

Basic Information of SLC38A4
Protein Name Sodium-coupled neutral amino acid transporter 4
Gene Name SLC38A4
Aliases Amino acid transporter A3, Na(+)-coupled neutral amino acid transporter 4, Solute carrier family 38 member 4, System A amino acid transporter 3, System N amino acid transporter 3, ATA3, NAT3, SNAT4
Organism Homo sapiens (Human)
UniProt ID Q969I6
Transmembrane Times 10
Length (aa) 547

Functions of SLC38A4 Membrane Protein

As a member of the amino acid transporter family, SLC38A4 transports abroad range of amino acids which are required for cellular functions. Besides, in the liver, SLC38A4, together with SLC38A2, is important to provide glutamine and alanine as precursors of glucose for gluconeogenesis, especially in the first hours of fasting. Moreover, studies reported a crucial role of SLC38A4 in liver physiology via PI3-kinase signaling pathway. In the placenta, SLC38A4 was reported to be functional in the first-trimester placenta microvillous membrane but had minimal contributions at term. Besides. microvillous and system A have a strong association with abnormal fetal birth weight and that they may play a crucial role in fetal growth and development.

The 10-transmembrane model of SLC38A4. Fig.1 The 10-transmembrane model of SLC38A4.

Application of SLC38A4 Membrane Protein in Literature

  1. Iyer R.P., et al. Identification of a disulfide bridge important for transport function of SNAT4 neutral amino acid transporter. PloS one. 2013, 8(2): e56792. PubMed ID: 23451088

    This study reported the identification of a disulfide bridge formed by cysteine residues 249 and 321 in SNAT4 that played an important role in the substrate transport but had no effect on trafficking of SNAT4 to the cell surface.

  2. Kondou H., et al. Sodium-coupled neutral amino acid transporter 4 functions as a regulator of protein synthesis during liver development. Hepatology Research. 2013, 43(11): 1211-1223. PubMed ID: 23607685

    This study investigated the regulation of SNAT4 by hepatocyte nuclear factor (HNF4α) and its roles in differentiating hepatocytes. The results showed that SNAT4 functioned downstream of HNF4α and played important roles in liver development through mechanisms of amino acid uptake and protein synthesis.

  3. Padmanabhan R., et al. Residue cysteine 232 is important for substrate transport of neutral amino acid transporter, SNAT4. International journal of biochemistry and molecular biology. 2012, 3(4): 374. PubMed ID: 23301202

    Using hydrosulfate cross-linking MTS reagents, this study investigated the critical amino acid residue(s) involved in substrate transport function of SNAT4. The findings suggested that residue Cys-232 at the 4th transmembrane domain of SNAT4 influenced substrate transport capacity.

  4. Shi Q., et al. Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein. Journal of Biological Chemistry. 2011, 286(44): 38086. PubMed ID: 21917917

    By using chemical labeling, glycosylation, immunofluorescence combined with molecular modeling approaches, this study firstly reported the membrane topological structure of SNAT4.

  5. Desforges M., et al. SNAT4 isoform of system A amino acid transporter is expressed in human placenta. American Journal of Physiology-Cell Physiology. 2006, 290(1): C305-C312. PubMed ID: 16148032

    This study investigated the expression and localization of SNATs, including SNAT1, SNAT2, SNAT4, in human placenta during gestation. The results showed that SMAT4 was located in the microvillous and basal plasma membranes of the syncytiotrophoblast.

SLC38A4 Preparation Options

Creative Biolabs provides unappalled customized membrane protein productions services to our global clients. Based on our cutting-edge Magic™ Membrane Protein Production Platform we can produce your transporters using both cell-based expression and cell-free expression methods. Moreover, we have detergent screening platform and lipid screening platform to optimize the conditions for protein solubilization, stabilization, and isolation. Besides, we can solubilize your proteins in alternative mimetics such as liposomes, nanodiscs, and polymers.

Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC38A4 antibody development services.

Contact us if you want to know more about our membrane protein preparation services.

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