SLC3A1 is encoded by the SLC3A1 gene which is located on 2pter-q32.3. The mutations of the gene can cause cystinuria (CSNU), an autosomal disorder with impaired epithelial cell transport of cystine and dibasic amino acids in the proximal renal tubule and gastrointestinal tract. The gene mutations also associate with hypotonia-cystinuria syndrome (HCS). SLC3A1 belongs to the Solute carrier family. The molecular mass of SLC3A1 is about 78 KDa.
|Basic Information of SLC3A1|
|Protein Name||Neutral and basic amino acid transport protein rBAT|
|Aliases||NBAT, D2h, Solute carrier family 3 member 1, b (0, +)-type amino acid transport protein|
|Organism||Homo sapiens (Human)|
|Transmembrane Times||Single-pass membrane|
SLC3A1 is a single-pass type II membrane protein of which N-terminus is on the cytoplasmic side of the membrane. And its transmembrane domain is located close to the N-terminus and it functions as an anchor. SLC3A1 has amino acid transmembrane transporter activity, protein heterodimerization activity, catalytic activity. It also takes part in cellular amino acid metabolic process, L-cystine transport, basic amino acid transport and some other biological processes. SLC3A1 is mainly expressed in the kidney, small intestine and pancreas, it can also be found in the liver and in the brush border membrane in the kidney. It has been proved that SLC3A1 is a Na+-independent dibasic and neutral amino acid transporter which is a member of the least hydrophobic of mammalian amino acid transporters. SLC3A1 is involved in cystine transport in the kidney and small intestine. Besides, SLC3A1 can stimulate a neutral and dibasic amino acid exchange activity, it may act as an activator of SLC7A9 and be participate in the high-affinity reabsorption of cystine in the kidney tubule.
Fig.1 Topological representation of the rBAT/SLC3A1 subunit (Bröer, 2002).
Authors of this article use co-immunoprecipitation followed by mass spectrometry to explore the unknown partner of rBAT/SLC3A1 in the S3 segment. They find that a membrane protein AGT1/SLC7A13 is the second partner of rBAT/SLC3A1. And AGT1 is the long-postulated second cystine transporter in the S3 segment of proximal tubules.
Authors of this article use RT-PCR and immunohistochemistry to evaluate the ontogenetic development of PepT1, NBAT/SLC3A1 along the vertical and horizontal axes of the rat small intestine. They reveal that the expression of NBAT/SLC3A1 is differently regulated according to both the horizontal and vertical axes.
Authors in this group study the N-glycans of rBAT/SLC3A1 and of its C-terminal loop in biogenesis of system b (0, +) is unknown. They identify the five N-glycans of rBAT/SLC3A1. They explore the function of the C-terminal loop and the importance of the N-glycan Asn (575) of rBAT/SLC3A1 in biogenesis of the rBAT-b (0, +) AT heterodimer.
Authors of this article intend to explore genetic variants in three exons (1, 3, and 8) of SLC3A1. They find one mutation in the SLC3A1 gene and identify three polymorphisms. They confirm that cystinuria is a heterogeneous disorder at the molecular level and more studies are needed to identify the distribution and frequency of mutations causing cystinuria in the Iranian population.
Authors of this article want to explore the physiological role of NBAT/SLC3A1. They cloned the gene and analyzed the function and the expression of the SLC3A1. Finally, they found that NBAT/SLC3A1 is related to cystine transport.
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