SLC1A4

From Wikipedia, the free encyclopedia

Solute carrier family 1 (glutamate/neutral amino acid transporter), member 4

Identifiers

SLC1A4; ASCT1; SATT

External IDs

OMIM: 600229 MGI: 2135601 HomoloGene: 20655

Gene ontology
Molecular Function:	• 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_003038 (mRNA)
NP_003029 (protein)

NM_018861 (mRNA)
NP_061349 (protein)

Location

Chr 2: 65.07 - 65.1 Mb

Chr 11: 20.2 - 20.23 Mb

Pubmed search

[1]

[2]

Solute carrier family 1 (glutamate/neutral amino acid transporter), member 4, also known as SLC1A4, is a human gene.^[1]

[edit] See also

[edit] References

^ Entrez Gene: SLC1A4 solute carrier family 1 (glutamate/neutral amino acid transporter), member 4.

[edit] Further reading

Hofmann K, Düker M, Fink T, et al. (1995). "Human neutral amino acid transporter ASCT1: structure of the gene (SLC1A4) and localization to chromosome 2p13-p15.". Genomics 24 (1): 20–6. doi:10.1006/geno.1994.1577. PMID 7896285.
Arriza JL, Kavanaugh MP, Fairman WA, et al. (1993). "Cloning and expression of a human neutral amino acid transporter with structural similarity to the glutamate transporter gene family.". J. Biol. Chem. 268 (21): 15329–32. PMID 8101838.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Shafqat S, Tamarappoo BK, Kilberg MS, et al. (1993). "Cloning and expression of a novel Na(+)-dependent neutral amino acid transporter structurally related to mammalian Na+/glutamate cotransporters.". J. Biol. Chem. 268 (21): 15351–5. PMID 8340364.
Tamarappoo BK, McDonald KK, Kilberg MS (1996). "Expressed human hippocampal ASCT1 amino acid transporter exhibits a pH-dependent change in substrate specificity.". Biochim. Biophys. Acta 1279 (2): 131–6. PMID 8603078.
Zerangue N, Kavanaugh MP (1996). "ASCT-1 is a neutral amino acid exchanger with chloride channel activity.". J. Biol. Chem. 271 (45): 27991–4. PMID 8910405.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Marin M, Tailor CS, Nouri A, Kabat D (2000). "Sodium-dependent neutral amino acid transporter type 1 is an auxiliary receptor for baboon endogenous retrovirus.". J. Virol. 74 (17): 8085–93. PMID 10933718.
Younes M, Pathak M, Finnie D, et al. (2001). "Expression of the neutral amino acids transporter ASCT1 in esophageal carcinomas.". Anticancer Res. 20 (5C): 3775–9. PMID 11268453.
Pinilla J, Barber A, Lostao MP (2002). "Active transport of alanine by the neutral amino-acid exchanger ASCT1.". Can. J. Physiol. Pharmacol. 79 (12): 1023–9. PMID 11824937.
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.
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.
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.
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.
Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4.". Nature 434 (7034): 724–31. doi:10.1038/nature03466. PMID 15815621.
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.

This membrane protein-related article is a stub. You can help Wikipedia by expanding it.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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)