SLC1A5

From Wikipedia, the free encyclopedia

Solute carrier family 1 (neutral amino acid transporter), member 5

Identifiers

SLC1A5; AAAT; ASCT2; ATBO; FLJ31068; M7V1; M7VS1; R16; RDRC

External IDs

OMIM: 109190 MGI: 105305 HomoloGene: 21155

Gene ontology
Molecular Function:	• receptor activity • neutral amino acid transmembrane transporter activity • symporter activity • sodium:dicarboxylate symporter activity
Cellular Component:	• membrane fraction • integral to plasma membrane • membrane
Biological Process:	• transport • dicarboxylic acid transport • neutral amino acid transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005628 (mRNA)
NP_005619 (protein)

NM_009201 (mRNA)
NP_033227 (protein)

Location

Chr 19: 51.97 - 51.98 Mb

Chr 7: 15.94 - 15.96 Mb

Pubmed search

[1]

[2]

Solute carrier family 1 (neutral amino acid transporter), member 5, also known as SLC1A5, is a human gene.^[1]

[edit] See also

[edit] References

^ Entrez Gene: SLC1A5 solute carrier family 1 (neutral amino acid transporter), member 5.

[edit] Further reading

Kekuda R, Prasad PD, Fei YJ, et al. (1996). "Cloning of the sodium-dependent, broad-scope, neutral amino acid transporter Bo from a human placental choriocarcinoma cell line.". J. Biol. Chem. 271 (31): 18657-61. PMID 8702519.
Rasko JE, Battini JL, Gottschalk RJ, et al. (1999). "The RD114/simian type D retrovirus receptor is a neutral amino acid transporter.". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2129-34. PMID 10051606.
Tailor CS, Nouri A, Zhao Y, et al. (1999). "A sodium-dependent neutral-amino-acid transporter mediates infections of feline and baboon endogenous retroviruses and simian type D retroviruses.". J. Virol. 73 (5): 4470-4. PMID 10196349.
Tailor CS, Marin M, Nouri A, et al. (2001). "Truncated forms of the dual function human ASCT2 neutral amino acid transporter/retroviral receptor are translationally initiated at multiple alternative CUG and GUG codons.". J. Biol. Chem. 276 (29): 27221-30. doi:10.1074/jbc.M100737200. PMID 11350958.
Lavillette D, Marin M, Ruggieri A, et al. (2002). "The envelope glycoprotein of human endogenous retrovirus type W uses a divergent family of amino acid transporters/cell surface receptors.". J. Virol. 76 (13): 6442-52. PMID 12050356.
Kudo Y, Boyd CA (2003). "Changes in expression and function of syncytin and its receptor, amino acid transport system B(0) (ASCT2), in human placental choriocarcinoma BeWo cells during syncytialization.". Placenta 23 (7): 536-41. PMID 12175968.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932.
Potter SJ, Lu A, Wilcken B, et al. (2003). "Hartnup disorder: polymorphisms identified in the neutral amino acid transporter SLC1A5.". J. Inherit. Metab. Dis. 25 (6): 437-48. PMID 12555937.
Marin M, Lavillette D, Kelly SM, Kabat D (2003). "N-linked glycosylation and sequence changes in a critical negative control region of the ASCT1 and ASCT2 neutral amino acid transporters determine their retroviral receptor functions.". J. Virol. 77 (5): 2936-45. PMID 12584318.
Kudo Y, Boyd CA, Sargent IL, Redman CW (2003). "Hypoxia alters expression and function of syncytin and its receptor during trophoblast cell fusion of human placental BeWo cells: implications for impaired trophoblast syncytialisation in pre-eclampsia.". Biochim. Biophys. Acta 1638 (1): 63-71. PMID 12757936.
Knerr I, Weigel C, Linnemann K, et al. (2003). "Transcriptional effects of hypoxia on fusiogenic syncytin and its receptor ASCT2 in human cytotrophoblast BeWo cells and in ex vivo perfused placental cotyledons.". Am. J. Obstet. Gynecol. 189 (2): 583-8. PMID 14520239.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334.
Palmada M, Speil A, Jeyaraj S, et al. (2005). "The serine/threonine kinases SGK1, 3 and PKB stimulate the amino acid transporter ASCT2.". Biochem. Biophys. Res. Commun. 331 (1): 272-7. doi:10.1016/j.bbrc.2005.03.159. PMID 15845389.
Uchiyama T, Matsuda Y, Wada M, et al. (2005). "Functional regulation of Na+-dependent neutral amino acid transporter ASCT2 by S-nitrosothiols and nitric oxide in Caco-2 cells.". FEBS Lett. 579 (11): 2499-506. doi:10.1016/j.febslet.2005.03.065. PMID 15848195.
Bungard CI, McGivan JD (2006). "Identification of the promoter elements involved in the stimulation of ASCT2 expression by glutamine availability in HepG2 cells and the probable involvement of FXR/RXR dimers.". Arch. Biochem. Biophys. 443 (1-2): 53-9. doi:10.1016/j.abb.2005.08.016. PMID 16197915.
Brauers E, Vester U, Zerres K, Eggermann T (2006). "Search for mutations in SLC1A5 (19q13) in cystinuria patients.". J. Inherit. Metab. Dis. 28 (6): 1169-71. doi:10.1007/s10545-005-0094-x. PMID 16435221.
Gegelashvili M, Rodriguez-Kern A, Pirozhkova I, et al. (2006). "High-affinity glutamate transporter GLAST/EAAT1 regulates cell surface expression of glutamine/neutral amino acid transporter ASCT2 in human fetal astrocytes.". Neurochem. Int. 48 (6-7): 611-5. doi:10.1016/j.neuint.2005.12.033. PMID 16516348.
Cheynet V, Oriol G, Mallet F (2006). "Identification of the hASCT2-binding domain of the Env ERVWE1/syncytin-1 fusogenic glycoprotein.". Retrovirology 3: 41. doi:10.1186/1742-4690-3-41. PMID 16820059.
Chi A, Valencia JC, Hu ZZ, et al. (2007). "Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.". J. Proteome Res. 5 (11): 3135-44. doi:10.1021/pr060363j. PMID 17081065.

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v • d • e Membrane proteins, carrier proteins: membrane transport proteins

ABC-transporter	A1, A2, A3, A4, A7, A8, A12, B1 B2-3, B2, B3, B4, B5, B6, B7, B9, B11 C1, C2, C3, C4, C5, C6, C8, C8-9, C10, C13, C11 D1, D2, D3, D4, E1, F1, F2 G1, G2, G4, Sterolin (G5, G8)

Solute carrier	1A1-7, 1A1, 1A2, 1A3, 1A4, 1A5, 2A1, 2A2, 2A3, 2A4, 2A5, 2A6, 2A8, 2A9, 2A10, 2A12, 3A1, 3A2, 4A1, 4A2, 4A3, 4A4, 4A5, 4A7, 4A8, 4A11, 5A1-2, 5A1, 5A3, 5A5, 5A8, 6A1, 6A2, 6A3, 6A4, 6A5, 6A8, 6A9, 6A19, 7A1, 7A2, 7A3, 7A4, 7A5, 7A7, 7A8, 7A9, 7A11, 8A1-3, 9A1, 9A2, 9A3, 9A3R1, 9A3R2, 9A5, 9A6, 9A8, 10A1, 10A2, 10A3, 10A7, 11A1, 11A2, 11A3, 12A1-2, 12A3, 12A4, 12A5, 12A6, 12A7, 14A1, 13A3, 14A2, 15A1, 15A2, 16A1, 16A2, 16A3, 16A4, 17A1, 17A5, 17A6-8, 17A7, 18A1, 18A2, 18A3, 19A1, 19A2, 19A3, 20A1, 20A2, 22A1, 22A2, 22A3, 22A4, 22A5, 22A6, 22A7, 22A9, 22A11, 22A12, 22A18, 23A1, 23A2, 24A1-2, 24A5, 25A1, 25A3, 25A4, 25A4-6, 25A8, 25A10, 25A11, 25A12, 25A13, 25A14, 25A15, 25A17, 25A19, 25A20, 25A27, 25A31, 25A37, 25A39, 26A2, 26A3, 26A4, 26A5, 26A6, 26A7, 26A8, 27A1, 27A2, 27A3, 27A4, 28A1, 28A2, 29A1, 29A2, 29A4, 30A4, 30A7, 30A8, 31A1, 31A2, 32A1, 34A1, 34A2, 34A3, 35A1, 35A2, 35B2, 35B4, 35C1, 36A1, 37A4, 38A2, 38A3, 39A1, 39A2, 39A3, 39A4, 39A6, 39A7, 40A1, 43A1 44A1, 44A2, 44A4, 45A2, O1A2, O1B1, O1B3, O2B1, O431, O4A1

Monosaccharide	GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, GLUT6, GLUT8, GLUT9

Other	Amino acid (CD98) - Fatty acid (CD36) - Ion channels - Ion pumps - Mitochondrial membrane transport protein - Neurotransmitter transport proteins - Nuclear (Importin, Karyopherin)