TCDB is operated by the Saier Lab Bioinformatics Group
Transporter Information:
Name: solute carrier family 7, (neutral amino acid transporter, y+ system) member 10
Symbol: SLC7A10
TC: 2.A.3.8.6
Locations: 19q13.1
Aliases: asc-1
GenBank: AB037670
Swiss-Prot: Q9NS82
Accession Number: NM_019849
Old Name: solute carrier family 7, (cationic amino acid transporter, y+ system) member 10
PubMed (10734121): Fukasawa Y, Segawa H, Kim JY, Chairoungdua A, Kim DK, Matsuo H, Cha SH,Endou H, Kanai Y. Identification and characterization of a Na(+)-independent neutral amino acidtransporter that associates with the 4F2 heavy chain and exhibits substrateselectivity for small neutral D- and L-amino acids.J Biol Chem. 2000 Mar 31;275(13):9690-8. PMID: 10734121 [PubMed - indexed for MEDLINE]

A cDNA was isolated from the mouse brain that encodes a novel Na(+)-independent neutral amino acid transporter. The encoded protein, designated as Asc-1 (asc-type amino acid transporter 1), was found to be structurally related to recently identified mammalian amino acid transporters for the transport systems L, y(+)L, x(C)(-), and b(0,+), which are linked, via a disulfide bond, to the type II membrane glycoproteins, 4F2 heavy chain (4F2hc), or rBAT (related to b(0,+) amino acid transporter). Asc-1 required 4F2hc for its functional expression. In Western blot analysis in the nonreducing condition, a 118-kDa band, which seems to correspond to the heterodimeric complex of Asc-1 and 4F2hc, was detected in the mouse brain. The band shifted to 33 kDa in the reducing condition, confirming that Asc-1 and 4F2hc are linked via a disulfide bond. Asc-1-mediated transport was not dependent on the presence of Na(+) or Cl(-). Although Asc-1 showed a high sequence homology (66% identity at the amino acid level) to the Na(+)-independent broad scope neutral amino acid transporter LAT2 (Segawa, H., Fukasawa, Y., Miyamoto, K., Takeda, E., Endou, H., and Kanai, Y. (1999) J. Biol. Chem. 274, 19745-19751), Asc-1 also exhibited distinctive substrate selectivity and transport properties. Asc-1 preferred small neutral amino acids such as Gly, L-Ala, L-Ser, L-Thr, and L-Cys, and alpha-aminoisobutyric acid as substrates. Asc-1 also transported D-isomers of the small neutral amino acids, in particular D-Ser, a putative endogenous modulator of N-methyl-D-aspartate-type glutamate receptors, with high affinity. Asc-1 operated preferentially, although not exclusively, in an exchange mode. Asc-1 mRNA was detected in the brain, lung, small intestine, and placenta. The functional properties of Asc-1 seem to be consistent with those of a transporter subserving the Na(+)-independent small neutral amino acid transport system asc.

PubMed (10863037): Nakauchi J, Matsuo H, Kim DK, Goto A, Chairoungdua A, Cha SH, Inatomi J,Shiokawa Y, Yamaguchi K, Saito I, Endou H, Kanai Y. Cloning and characterization of a human brain Na(+)-independent transporter forsmall neutral amino acids that transports D-serine with high affinity.Neurosci Lett. 2000 Jun 30;287(3):231-5. PMID: 10863037 [PubMed - indexed for MEDLINE]

We isolated a cDNA for the human homologue of system asc transporter Asc-1 from human brain. The encoded protein designated as hAsc-1 (human Asc-1) exhibited 91 % sequence identity to mouse Asc-1. Consistent with mouse Asc-1, hAsc-1 required 4F2 heavy chain for its functional expression in Xenopus oocytes. hAsc-1 exhibited the properties of amino acid transport system asc which transports small neutral amino acids in a Na(+)-independent manner. hAsc-1 transported D-serine at high affinity with a K(m) value of 22.8 microM. In brain, 2.0 kb mRNA was highly expressed. hAsc-1 gene was mapped to human chromosome 19, region q12-q13.1. Because of the high-affinity transport with the K(m) value close to the physiological concentration of D-serine, together with the high levels of expression in brain, hAsc-1 is proposed to play significant roles in the D-serine mobilization in brain.

>sp|Q9NS82|AAA1_HUMAN Asc-type amino acid transporter 1 OS=Homo sapiens GN=SLC7A10 PE=2 SV=1