SLC6A1

From Wikipedia, the free encyclopedia

Solute carrier family 6 (neurotransmitter transporter, GABA), member 1

Identifiers

SLC6A1; GABATHG; GABATR; GAT1

External IDs

OMIM: 137165 MGI: 95627 HomoloGene: 2290

Gene ontology
Molecular Function:	• neurotransmitter:sodium symporter activity • gamma-aminobutyric acid:sodium symporter activity • symporter activity
Cellular Component:	• membrane fraction • integral to plasma membrane • membrane • axon
Biological Process:	• neurotransmitter transport • synaptic transmission

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003042 (mRNA)
NP_003033 (protein)

XM_975926 (mRNA)
XP_981020 (protein)

Location

Chr 3: 11.01 - 11.06 Mb

Chr 6: 114.25 - 114.28 Mb

Pubmed search

[1]

[2]

Solute carrier family 6 (neurotransmitter transporter, GABA), member 1, also known as SLC6A1, is a human gene.^[1]

[edit] See also

[edit] References

^ Entrez Gene: SLC6A1 solute carrier family 6 (neurotransmitter transporter, GABA), member 1.

[edit] Further reading

Nelson H, Mandiyan S, Nelson N (1990). "Cloning of the human brain GABA transporter.". FEBS Lett. 269 (1): 181–4. PMID 2387399.
Huang F, Shi LJ, Heng HH, et al. (1996). "Assignment of the human GABA transporter gene (GABATHG) locus to chromosome 3p24-p25.". Genomics 29 (1): 302–4. doi:10.1006/geno.1995.1253. PMID 8530094.
Bennett ER, Kanner BI (1997). "The membrane topology of GAT-1, a (Na+ + Cl-)-coupled gamma-aminobutyric acid transporter from rat brain.". J. Biol. Chem. 272 (2): 1203–10. PMID 8995422.
Bismuth Y, Kavanaugh MP, Kanner BI (1997). "Tyrosine 140 of the gamma-aminobutyric acid transporter GAT-1 plays a critical role in neurotransmitter recognition.". J. Biol. Chem. 272 (26): 16096–102. PMID 9195904.
DeFelipe J, González-Albo MC (1998). "Chandelier cell axons are immunoreactive for GAT-1 in the human neocortex.". Neuroreport 9 (3): 467–70. PMID 9512391.
Conti F, Melone M, De Biasi S, et al. (1998). "Neuronal and glial localization of GAT-1, a high-affinity gamma-aminobutyric acid plasma membrane transporter, in human cerebral cortex: with a note on its distribution in monkey cortex.". J. Comp. Neurol. 396 (1): 51–63. PMID 9623887.
Beckman ML, Bernstein EM, Quick MW (1998). "Protein kinase C regulates the interaction between a GABA transporter and syntaxin 1A.". J. Neurosci. 18 (16): 6103–12. PMID 9698305.
Augood SJ, Waldvogel HJ, Münkle MC, et al. (1999). "Localization of calcium-binding proteins and GABA transporter (GAT-1) messenger RNA in the human subthalamic nucleus.". Neuroscience 88 (2): 521–34. PMID 10197772.
Ong WY, Yeo TT, Balcar VJ, Garey LJ (2000). "A light and electron microscopic study of GAT-1-positive cells in the cerebral cortex of man and monkey.". J. Neurocytol. 27 (10): 719–30. PMID 10640187.
Deken SL, Beckman ML, Boos L, Quick MW (2000). "Transport rates of GABA transporters: regulation by the N-terminal domain and syntaxin 1A.". Nat. Neurosci. 3 (10): 998–1003. doi:10.1038/79939. PMID 11017172.
Whitworth TL, Quick MW (2001). "Substrate-induced regulation of gamma-aminobutyric acid transporter trafficking requires tyrosine phosphorylation.". J. Biol. Chem. 276 (46): 42932–7. doi:10.1074/jbc.M107638200. PMID 11555659.
Hachiya Y, Takashima S (2002). "Development of GABAergic neurons and their transporter in human temporal cortex.". Pediatr. Neurol. 25 (5): 390–6. PMID 11744314.
Quick MW (2002). "Substrates regulate gamma-aminobutyric acid transporters in a syntaxin 1A-dependent manner.". Proc. Natl. Acad. Sci. U.S.A. 99 (8): 5686–91. doi:10.1073/pnas.082712899. PMID 11960023.
Kanner BI (2003). "Transmembrane domain I of the gamma-aminobutyric acid transporter GAT-1 plays a crucial role in the transition between cation leak and transport modes.". J. Biol. Chem. 278 (6): 3705–12. doi:10.1074/jbc.M210525200. PMID 12446715.
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.
Zomot E, Kanner BI (2003). "The interaction of the gamma-aminobutyric acid transporter GAT-1 with the neurotransmitter is selectively impaired by sulfhydryl modification of a conformationally sensitive cysteine residue engineered into extracellular loop IV.". J. Biol. Chem. 278 (44): 42950–8. doi:10.1074/jbc.M209307200. PMID 12925537.
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.
Zhou Y, Bennett ER, Kanner BI (2004). "The aqueous accessibility in the external half of transmembrane domain I of the GABA transporter GAT-1 Is modulated by its ligands.". J. Biol. Chem. 279 (14): 13800–8. doi:10.1074/jbc.M311579200. PMID 14744863.
Hu JH, Ma YH, Jiang J, et al. (2004). "Cognitive impairment in mice over-expressing gamma-aminobutyric acid transporter 1 (GAT1).". Neuroreport 15 (1): 9–12. PMID 15106822.
Korkhov VM, Farhan H, Freissmuth M, Sitte HH (2005). "Oligomerization of the {gamma}-aminobutyric acid transporter-1 is driven by an interplay of polar and hydrophobic interactions in transmembrane helix II.". J. Biol. Chem. 279 (53): 55728-36. doi:10.1074/jbc.M409449200. PMID 15496410.

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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)