|Name:||solute carrier family 7, (cationic amino acid transporter, y+ system) member 13|
|PubMed (11907033):|| Matsuo H, Kanai Y, Kim JY, Chairoungdua A, Kim do K, Inatomi J, Shigeta Y,Ishimine H, Chaekuntode S, Tachampa K, Choi HW, Babu E, Fukuda J, Endou H. Identification of a novel Na+-independent acidic amino acid transporter withstructural similarity to the member of a heterodimeric amino acid transporterfamily associated with unknown heavy chains.J Biol Chem. 2002 Jun 7;277(23):21017-26. Epub 2002 Mar 20. PMID: 11907033 [PubMed - indexed for MEDLINE]|
We identified a novel Na(+)-independent acidic amino acid transporter designated AGT1 (aspartate/glutamate transporter 1). AGT1 exhibits the highest sequence similarity (48% identity) to the Na(+)-independent small neutral amino acid transporter Asc (asc-type amino acid transporter)-2 a member of the heterodimeric amino acid transporter family presumed to be associated with unknown heavy chains (Chairoungdua, A., Kanai, Y., Matsuo, H., Inatomi, J., Kim, D. K., and Endou, H. (2001) J. Biol. Chem. 276, 49390-49399). The cysteine residue responsible for the disulfide bond formation between transporters (light chains) and heavy chain subunits of the heterodimeric amino acid transporter family is conserved for AGT1. Because AGT1 solely expressed or coexpressed with already known heavy chain 4F2hc (4F2 heavy chain) or rBAT (related to b(0,+)-amino acid transporter) did not induce functional activity, we generated fusion proteins in which AGT1 was connected with 4F2hc or rBAT. The fusion proteins were sorted to the plasma membrane and expressed the Na(+)-independent transport activity for acidic amino acids. Distinct from the Na(+)-independent cystine/glutamate transporter xCT structurally related to AGT1, AGT1 did not accept cystine, homocysteate, and l-alpha-aminoadipate and exhibited high affinity to aspartate as well as glutamate, suggesting that the negative charge recognition site in the side chain-binding site of AGT1 would be closer to the alpha-carbon binding site compared with that of xCT. The AGT1 message was predominantly expressed in kidney. In mouse kidney, AGT1 protein was present in the basolateral membrane of the proximal straight tubules and distal convoluted tubules. In the Western blot analysis, AGT1 was detected as a high molecular mass band in the nonreducing condition, whereas the band shifted to a 40-kDa band corresponding to the AGT1 monomer in the reducing condition, suggesting the association of AGT1 with other protein via a disulfide bond. The finding of AGT1 and Asc-2 has established a new subgroup of the heterodimeric amino acid transporter family whose members associate not with 4F2hc or rBAT but with other unknown heavy chains.
|PubMed (11943479):|| Blondeau JP. Homologues of amino acid permeases: cloning and tissue expression of XAT1 andXAT2.Gene. 2002 Mar 20;286(2):241-8. PMID: 11943479 [PubMed - indexed for MEDLINE]|
The L-type (LAT) family of amino acid transporters is composed of exchangers for neutral, cationic, and anionic amino acids. They form functional heterodimers with membrane glycoproteins, rBAT or 4F2hc/CD98, to which they are linked by a disulphide bond. We report the molecular cloning and tissue expression of new mouse and human homologues of the LAT family, termed mXAT1, mXAT2 and hXAT2. The latter two proteins may correspond to ortholog genes in mouse and human. The hXAT2 gene is located on chromosome 8q21.3. The cloned X amino acid transporter (XAT) cDNAs are predicted to encode proteins of about 50 kDa. From a phylogenetic point of view, the three XAT proteins cluster together, but sequence comparison and secondary structure prediction show that they are also related to the members of the LAT family. Like these transporters, the XAT proteins show 12 transmembrane domains and a conserved cysteine residue, located in the second extracellular loop. This conserved cysteine is involved in the disulphide bond formed between the known members of the LAT family and 4F2hc or rBAT. The mXAT1 and hXAT2 mRNAs are expressed in the kidney but they are not detectable in a variety of other tissues. The corresponding proteins were efficiently translated following transfection of their cDNAs in Chinese hamster ovary (CHO) cells. However, cDNA transfection in CHO cells did not induce amino acid uptake, even when cotransfected with vectors expressing 4F2hc or rBAT. This could be related to the fact that mXAT1 and hXAT2 did not form detectable disulphide-linked heterodimers with 4F2hc or rBAT when they were co-expressed in CHO cells. Identification of other putative partner(s) of these LAT family-related transporters may be necessary to understand their role in renal physiology.
>sp|Q8TCU3|S7A13_HUMAN Solute carrier family 7 member 13 OS=Homo sapiens GN=SLC7A13 PE=2 SV=1 MDRGEKIQLKRVFGYWWGTSFLLINIIGAGIFVSPKGVLAYSCMNVGVSLCVWAGCAILAMTSTLCSAEISISFPCSGAQ YYFLKRYFGSTVAFLNLWTSLFLGSGVVAGQALLLAEYSIQPFFPSCSVPKLPKKCLALAMLWIVGILTSRGVKEVTWLQ IASSVLKVSILSFISLTGVVFLIRGKKENVERFQNAFDAELPDISHLIQAIFQGYFAYSGGACFTLIAGELKKPRTTIPK CIFTALPLVTVVYLLVNISYLTVLTPREILSSDAVAITWADRAFPSLAWIMPFAISTSLFSNLLISIFKSSRPIYLASQE GQLPLLFNTLNSHSSPFTAVLLLVTLGSLAIILTSLIDLINYIFFTGSLWSILLMIGILRRRYQEPNLSIPYKVFLSFPL ATIVIDVGLVVIPLVKSPNVHYVYVLLLVLSGLLFYIPLIHFKIRLAWFEKMTCYLQLLFNICLPDVSEE