TCDB is operated by the Saier Lab Bioinformatics Group
TRANSPORTERS FROM HUMANS:
Transporter Information:
Name: solute carrier family 23 (nucleobase transporters), member 2
Symbol: SLC23A2
TC: 2.A.40.6.1
Locations: 20p13
Aliases: SVCT2, KIAA0238, YSPL2
GenBank: AF058319
Swiss-Prot: Q9UHI7
Accession Number: NM_005116
Old Name: solute carrier family 23 (nucleobase transporters), member 1
GDBGDB:9785326
LocusLink9962
OMIM603791
PubMed (9804989): Faaland CA, Race JE, Ricken G, Warner FJ, Williams WJ, Holtzman EJ. Molecular characterization of two novel transporters from human and mousekidney and from LLC-PK1 cells reveals a novel conserved family that ishomologous to bacterial and Aspergillus nucleobase transporters.Biochim Biophys Acta. 1998 Nov 8;1442(2-3):353-60. PMID: 9804989 [PubMed - indexed for MEDLINE]

Nucleobase transport is important for the metabolism of nucleic acids and antiviral and antineoplastic drugs. This transport has been functionally described in several mammalian cells but has not been well characterized molecularly. We report the cloning of two novel transporters. YSPL2 encodes a 650-residue protein and has an ubiquitous 8 kb transcript. The human and pig homologs are 95% similar. YSPL3 encodes a 598-residue protein with a 3 kb transcript that is expressed only in kidney and liver. Human YSPL2 and YSPL3 are 60% similar at the amino acid level and both show 31% similarity to the first nucleobase permease gene described in vertebrates, YSPL1. These proteins appear to be members of a new family of possible nucleobase transporters with significant sequence similarities with bacterial and Aspergillus nucleobase transporters. Further functional studies will be needed to unveil the role of these transporters in nucleic acid metabolism in normal and in disease states.

PubMed (10331392): Tsukaguchi H, Tokui T, Mackenzie B, Berger UV, Chen XZ, Wang Y, Brubaker RF,Hediger MA. A family of mammalian Na+-dependent L-ascorbic acid transporters.Nature. 1999 May 6;399(6731):70-5. PMID: 10331392 [PubMed - indexed for MEDLINE]

Vitamin C (L-ascorbic acid) is essential for many enzymatic reactions, in which it serves to maintain prosthetic metal ions in their reduced forms (for example, Fe2+, Cu+), and for scavenging free radicals in order to protect tissues from oxidative damage. The facilitative sugar transporters of the GLUT type can transport the oxidized form of the vitamin, dehydroascorbic acid, but these transporters are unlikely to allow significant physiological amounts of vitamin C to be taken up in the presence of normal glucose concentrations, because the vitamin is present in plasma essentially only in its reduced form. Here we describe the isolation of two L-ascorbic acid transporters, SVCT1 and SVCT2, from rat complementary DNA libraries, as the first step in investigating the importance of L-ascorbic acid transport in regulating the supply and metabolism of vitamin C. We find that SVCT1 and SVCT2 each mediate concentrative, high-affinity L-ascorbic acid transport that is stereospecific and is driven by the Na+ electrochemical gradient. Despite their close sequence homology and similar functions, the two isoforms of the transporter are discretely distributed: SVCT1 is mainly confined to epithelial systems (intestine, kidney, liver), whereas SVCT2 serves a host of metabolically active cells and specialized tissues in the brain, eye and other organs.

>sp|Q9UHI7|S23A1_HUMAN Solute carrier family 23 member 1 OS=Homo sapiens GN=SLC23A1 PE=1 SV=3
MRAQEDLEGRTQHETTRDPSTPLPTEPKFDMLYKIEDVPPWYLCILLGFQHYLTCFSGTIAVPFLLAEALCVGHDQHMVS
QLIGTIFTCVGITTLIQTTVGIRLPLFQASAFAFLVPAKAILALERWKCPPEEEIYGNWSLPLNTSHIWHPRIREVQGAI
MVSSVVEVVIGLLGLPGALLNYIGPLTVTPTVSLIGLSVFQAAGDRAGSHWGISACSILLIILFSQYLRNLTFLLPVYRW
GKGLTLLRIQIFKMFPIMLAIMTVWLLCYVLTLTDVLPTDPKAYGFQARTDARGDIMAIAPWIRIPYPCQWGLPTVTAAA
VLGMFSATLAGIIESIGDYYACARLAGAPPPPVHAINRGIFTEGICCIIAGLLGTGNGSTSSSPNIGVLGITKVGSRRVV
QYGAAIMLVLGTIGKFTALFSSLPDPILGGMFCTLFGMITAVGLSNLQFVDMNSSRNLFVLGFSMFFGLTLPNYLESNPG
AINTGILEVDQILIVLLTTEMFVGGCLAFILDNTVPGSPEERGLIQWKAGAHANSDMSSSLKSYDFPIGMGIVKRITFLK
YIPICPVFKGFSSSSKDQIAIPEDTPENTETASVCTKV