ID GBRA1_RAT Reviewed; 455 AA. AC P62813; P18504; Q53YK4; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 02-SEP-2026, entry version 162. DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-1; DE AltName: Full=GABA(A) receptor subunit alpha-1 {ECO:0000303|PubMed:11528422}; DE Short=GABAAR subunit alpha-1 {ECO:0000303|PubMed:25172774}; DE Flags: Precursor; GN Name=Gabra1 {ECO:0000312|RGD:61855}; Synonyms=Gabra-1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND RP SUBUNIT. RX PubMed=2540033; DOI=10.1016/0014-5793(89)80271-6; RA Lolait S.J., O'Carroll A.-M., Kusano K., Muller J.-M., Brownstein M.J., RA Mahan L.C.; RT "Cloning and expression of a novel rat GABAA receptor."; RL FEBS Lett. 246:145-148(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2561977; DOI=10.1016/0896-6273(89)90243-2; RA Khrestchatisky M., Maclennan A.J., Chiang M.Y., Xu W., Jackson M.B., RA Brecha N., Sternini C., Olsen R.W., Tobin A.J.; RT "A novel alpha subunit in rat brain GABAA receptors."; RL Neuron 3:745-753(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION, AND RP TRANSPORTER ACTIVITY. RX PubMed=1977069; DOI=10.1016/0169-328x(90)90017-8; RA Malherbe P., Draguhn A., Multhaup G., Beyreuther K., Mohler H.; RT "GABAA-receptor expressed from rat brain alpha- and beta-subunit cDNAs RT displays potentiation by benzodiazepine receptor ligands."; RL Brain Res. Mol. Brain Res. 8:199-208(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Brain; RX PubMed=1966765; DOI=10.1101/sqb.1990.055.01.006; RA Seeburg P.H., Wisden W., Verdoorn T., Pritchett D., Werner P., Herb A., RA Lueddens H., Sprengel R., Sakmann B.; RT "The GABAA receptor family: molecular and functional diversity."; RL Cold Spring Harb. Symp. Quant. Biol. 55:29-40(1990). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RA Groot-Kormelink P.J.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP MUTAGENESIS OF PHE-91, FUNCTION, SUBCELLULAR LOCATION, AND ACTIVITY RP REGULATION. RX PubMed=1376242; DOI=10.1002/j.1460-2075.1992.tb05258.x; RA Sigel E., Baur R., Kellenberger S., Malherbe P.; RT "Point mutations affecting antagonist affinity and agonist dependent gating RT of GABAA receptor channels."; RL EMBO J. 11:2017-2023(1992). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=9464994; DOI=10.1523/jneurosci.18-05-01693.1998; RA Nusser Z., Sieghart W., Somogyi P.; RT "Segregation of different GABAA receptors to synaptic and extrasynaptic RT membranes of cerebellar granule cells."; RL J. Neurosci. 18:1693-1703(1998). RN [9] RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND INTERACTION WITH GABRB3 AND GABRE. RX PubMed=9882711; DOI=10.1124/mol.55.1.168; RA Neelands T.R., Fisher J.L., Bianchi M., Macdonald R.L.; RT "Spontaneous and gamma-aminobutyric acid (GABA)-activated GABA(A) receptor RT channels formed by epsilon subunit-containing isoforms."; RL Mol. Pharmacol. 55:168-178(1999). RN [10] RP INTERACTION WITH UBQLN1. RX PubMed=11528422; DOI=10.1038/nn0901-908; RA Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D., RA Wisden W., Triller A., Smart T.G., Moss S.J.; RT "GABA(A) receptor cell surface number and subunit stability are regulated RT by the ubiquitin-like protein Plic-1."; RL Nat. Neurosci. 4:908-916(2001). RN [11] RP TISSUE SPECIFICITY. RX PubMed=17003036; DOI=10.1074/jbc.m606895200; RA Jin N., Kolliputi N., Gou D., Weng T., Liu L.; RT "A novel function of ionotropic gamma-aminobutyric acid receptors involving RT alveolar fluid homeostasis."; RL J. Biol. Chem. 281:36012-36020(2006). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TRANSPORTER ACTIVITY. RX PubMed=18281286; DOI=10.1074/jbc.m709993200; RA Saras A., Gisselmann G., Vogt-Eisele A.K., Erlkamp K.S., Kletke O., RA Pusch H., Hatt H.; RT "Histamine action on vertebrate GABAA receptors: direct channel gating and RT potentiation of GABA responses."; RL J. Biol. Chem. 283:10470-10475(2008). RN [13] RP INTERACTION WITH KIF21B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=25172774; DOI=10.1016/j.ejcb.2014.07.007; RA Labonte D., Thies E., Kneussel M.; RT "The kinesin KIF21B participates in the cell surface delivery of gamma2 RT subunit-containing GABAA receptors."; RL Eur. J. Cell Biol. 93:338-346(2014). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH RP NLGN2; LHFPL4; GABRB2; GABRG2 AND GABRB3, AND INTERACTION WITH LHFLP4 AND RP NLGN2. RX PubMed=28279354; DOI=10.1016/j.neuron.2017.02.023; RA Yamasaki T., Hoyos-Ramirez E., Martenson J.S., Morimoto-Tomita M., RA Tomita S.; RT "GARLH family proteins stabilize GABAA receptors at synapses."; RL Neuron 93:1138-1152(2017). RN [15] {ECO:0007744|PDB:6DW0, ECO:0007744|PDB:6DW1} RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) OF 1-333 AND 440-474 IN RP COMPLEX WITH GABA, FUNCTION, SUBUNIT, INTERACTION WITH GABRB1 AND GABRG2, RP DISULFIDE BOND, AND GLYCOSYLATION AT ASN-137. RX PubMed=30044221; DOI=10.7554/elife.39383; RA Phulera S., Zhu H., Yu J., Claxton D.P., Yoder N., Yoshioka C., Gouaux E.; RT "Cryo-EM structure of the benzodiazepine-sensitive alpha1beta1gamma2S tri- RT heteromeric GABAA receptor in complex with GABA."; RL Elife 7:0-0(2018). CC -!- FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride CC channel gated by gamma-aminobutyric acid (GABA), a major inhibitory CC neurotransmitter in the brain (PubMed:1376242, PubMed:1977069, CC PubMed:2540033, PubMed:9882711). GABA-gated chloride channels, also CC named GABA(A) receptors (GABAAR), consist of five subunits arranged CC around a central pore and contain GABA active binding site(s) located CC at the alpha and beta subunit interface(s) (PubMed:30044221). When CC activated by GABA, GABAARs selectively allow the flow of chloride CC anions across the cell membrane down their electrochemical gradient CC (PubMed:18281286, PubMed:1977069, PubMed:9882711). Alpha-1/GABRA1- CC containing GABAARs are largely synaptic (PubMed:9464994). Chloride CC influx into the postsynaptic neuron following GABAAR opening decreases CC the neuron ability to generate a new action potential, thereby reducing CC nerve transmission (PubMed:18281286, PubMed:1977069). GABAARs CC containing alpha-1 and beta-2 or -3 subunits exhibit synaptogenic CC activity; the gamma-2 subunit being necessary but not sufficient to CC induce rapid synaptic contacts formation (By similarity). GABAARs CC function also as histamine receptor where histamine binds at the CC interface of two neighboring beta subunits and potentiates GABA CC response (PubMed:18281286, PubMed:1977069). GABAARs containing alpha, CC beta and epsilon subunits also permit spontaneous chloride channel CC activity while preserving the structural information required for GABA- CC gated openings (PubMed:9882711). Alpha-1-mediated plasticity in the CC orbitofrontal cortex regulates context-dependent action selection (By CC similarity). Together with rho subunits, may also control neuronal and CC glial GABAergic transmission in the cerebellum (By similarity). CC {ECO:0000250|UniProtKB:P14867, ECO:0000250|UniProtKB:P62812, CC ECO:0000269|PubMed:1376242, ECO:0000269|PubMed:18281286, CC ECO:0000269|PubMed:1977069, ECO:0000269|PubMed:2540033, CC ECO:0000269|PubMed:30044221, ECO:0000269|PubMed:9464994, CC ECO:0000269|PubMed:9882711}. CC -!- CATALYTIC ACTIVITY: CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, CC ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:18281286, CC ECO:0000269|PubMed:1977069, ECO:0000269|PubMed:9882711}; CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines and CC pentobarbital (PubMed:1977069). Allosterically activated by the CC neuroanesthetic alphaxalone (By similarity). Inhibited by the CC antagonist bicuculline (PubMed:1376242, PubMed:1977069). Potentiated by CC pentobarbital, loreclezole, and lanthanum and inhibited by zinc and CC furosemide (PubMed:9882711). Potentiated by histamine CC (PubMed:18281286). {ECO:0000250|UniProtKB:P14867, CC ECO:0000269|PubMed:1376242, ECO:0000269|PubMed:18281286, CC ECO:0000269|PubMed:1977069, ECO:0000269|PubMed:9882711}. CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha (GABRA1-6), CC beta (GABRB1-3), gamma (GABRG1-3), delta (GABRD), epsilon (GABRE), rho CC (GABRR1-3), pi (GABRP) and theta (GABRQ) subunits, each subunit CC exhibiting distinct physiological and pharmacological properties CC (Probable) (PubMed:18281286, PubMed:2540033, PubMed:30044221). CC Interacts with UBQLN1 (PubMed:11528422). Interacts with TRAK1 (By CC similarity). Interacts with KIF21B (PubMed:25172774). Identified in a CC complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 CC and GABRB3 (PubMed:28279354). Interacts with LHFPL4 (PubMed:28279354). CC Interacts with NLGN2 (PubMed:28279354). Interacts with SHISA7; CC interaction leads to the regulation of GABA(A) receptor trafficking, CC channel deactivation kinetics and pharmacology (By similarity). CC {ECO:0000250|UniProtKB:P62812, ECO:0000269|PubMed:11528422, CC ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:25172774, CC ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:28279354, CC ECO:0000269|PubMed:30044221, ECO:0000305|PubMed:9882711}. CC -!- INTERACTION: CC P62813; Q63787: Pik3r1; NbExp=4; IntAct=EBI-6258192, EBI-518443; CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane CC {ECO:0000269|PubMed:9464994}; Multi-pass membrane protein CC {ECO:0000269|PubMed:30044221}. Cell membrane CC {ECO:0000269|PubMed:1376242, ECO:0000269|PubMed:18281286, CC ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:9464994}; Multi-pass CC membrane protein {ECO:0000269|PubMed:30044221}. Cytoplasmic vesicle CC membrane {ECO:0000269|PubMed:25172774}. Note=The alpha-1 subunits CC (alpha-1-beta-2/3-gamma-2 receptors) are present in Golgi synapses and CC on the extrasynaptic membranes (PubMed:9464994). Mainly located in CC GABAergic synapses on granule cells (PubMed:9464994). CC {ECO:0000269|PubMed:9464994}. CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level). Expressed in CC lungs, in alveolar epithelium (PubMed:17003036). CC {ECO:0000269|PubMed:17003036, ECO:0000269|PubMed:25172774, CC ECO:0000269|PubMed:9464994}. CC -!- DOMAIN: The extracellular domain contributes to synaptic contact CC formation. {ECO:0000250|UniProtKB:P62812}. CC -!- DOMAIN: The GABA-binding pockets are located at the interface between CC neighboring alpha and beta subunits. {ECO:0000269|PubMed:30044221}. CC -!- DOMAIN: GABAARs subunits share a common topological structure: a CC peptide sequence made up of a long extracellular N-terminal, four CC transmembrane domains, intracellular or cytoplasmic domain located CC between the third and the fourth transmembrane domains. CC {ECO:0000269|PubMed:30044221}. CC -!- MISCELLANEOUS: Functions as a receptor for diazepines and various CC anesthetics, such as pentobarbital; these are bound at a separate CC allosteric effector binding site. {ECO:0000269|PubMed:1977069}. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family. CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA1 sub- CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L08490; AAC42029.1; -; Genomic_DNA. DR EMBL; AY574250; AAS90346.1; -; mRNA. DR EMBL; BC100061; AAI00062.1; -; mRNA. DR PIR; JQ0158; JQ0158. DR RefSeq; NP_899155.1; NM_183326.2. DR RefSeq; XP_006246185.1; XM_006246123.5. DR RefSeq; XP_006246186.1; XM_006246124.5. DR PDB; 6DW0; EM; 3.80 A; A/C=1-340, A/C=409-455. DR PDB; 6DW1; EM; 3.10 A; A/C=1-340, A/C=409-455. DR PDB; 9OUO; EM; 2.92 A; A/C=1-455. DR AlphaFoldDB; P62813; -. DR EMDB; EMD-70872; -. DR EMDB; EMD-70873; -. DR EMDB; EMD-70874; -. DR EMDB; EMD-70875; -. DR EMDB; EMD-70876; -. DR EMDB; EMD-70877; -. DR EMDB; EMD-70889; -. DR EMDB; EMD-8922; -. DR EMDB; EMD-8923; -. DR SMR; P62813; -. DR BioGRID; 248322; 4. DR ComplexPortal; CPX-250; GABA-A receptor, alpha1-beta2-gamma2. DR ComplexPortal; CPX-410; GABA-A receptor, alpha1-beta3-gamma2. DR CORUM; P62813; -. DR FunCoup; P62813; 1458. DR IntAct; P62813; 3. DR MINT; P62813; -. DR STRING; 10116.ENSRNOP00000004725; -. DR BindingDB; P62813; -. DR ChEMBL; CHEMBL343; -. DR DrugCentral; P62813; -. DR GlyCosmos; P62813; 2 sites, No reported glycans. DR GlyGen; P62813; 3 sites, 1 O-linked glycan (1 site). DR iPTMnet; P62813; -. DR PhosphoSitePlus; P62813; -. DR PaxDb; 10116-ENSRNOP00000004725; -. DR ABCD; P62813; 2 sequenced antibodies. DR Ensembl; ENSRNOT00000004725.9; ENSRNOP00000004725.5; ENSRNOG00000003512.9. DR Ensembl; ENSRNOT00055008521; ENSRNOP00055006470; ENSRNOG00055005301. DR Ensembl; ENSRNOT00060036907; ENSRNOP00060030419; ENSRNOG00060021305. DR Ensembl; ENSRNOT00065001781; ENSRNOP00065001239; ENSRNOG00065001344. DR GeneID; 29705; -. DR KEGG; rno:29705; -. DR UCSC; RGD:61855; rat. DR AGR; RGD:61855; -. DR CTD; 2554; -. DR RGD; 61855; Gabra1. DR eggNOG; KOG3642; Eukaryota. DR GeneTree; ENSGT00940000159136; -. DR HOGENOM; CLU_010920_2_1_1; -. DR InParanoid; P62813; -. DR OrthoDB; 42535at9989; -. DR PhylomeDB; P62813; -. DR Reactome; R-RNO-977443; GABA receptor activation. DR PRO; PR:P62813; -. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000003512; Expressed in cerebellum and 6 other cell types or tissues. DR ExpressionAtlas; P62813; baseline and differential. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central. DR GO; GO:0043197; C:dendritic spine; ISO:RGD. DR GO; GO:1902710; C:GABA receptor complex; IDA:BHF-UCL. DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO. DR GO; GO:0005886; C:plasma membrane; EXP:UniProtKB. DR GO; GO:0098794; C:postsynapse; IBA:GO_Central. DR GO; GO:0045211; C:postsynaptic membrane; EXP:UniProtKB. DR GO; GO:0099634; C:postsynaptic specialization membrane; IDA:UniProtKB. DR GO; GO:0050809; F:diazepam binding; IDA:RGD. DR GO; GO:0004890; F:GABA-A receptor activity; IDA:UniProtKB. DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IDA:UniProtKB. DR GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO. DR GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; ISO:RGD. DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB. DR GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD. DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB. DR GO; GO:0010996; P:response to auditory stimulus; IEP:RGD. DR GO; GO:1904313; P:response to methamphetamine hydrochloride; IEP:RGD. DR GO; GO:0051932; P:synaptic transmission, GABAergic; IDA:BHF-UCL. DR CDD; cd19034; LGIC_ECD_GABAAR_A1; 1. DR CDD; cd19052; LGIC_TM_GABAAR_alpha; 1. DR FunFam; 2.70.170.10:FF:000001; Gamma-aminobutyric acid A receptor subunit alpha-2; 1. DR FunFam; 1.20.58.390:FF:000002; Putative gamma-aminobutyric acid receptor subunit alpha-5; 1. DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1. DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1. DR InterPro; IPR006028; GABAA/Glycine_rcpt. DR InterPro; IPR001390; GABAAa_rcpt. DR InterPro; IPR005431; GABBAa1_rcpt. DR InterPro; IPR047024; Gabra-1-6_TM. DR InterPro; IPR047079; GABRA1_ECD. DR InterPro; IPR006202; Neur_chan_lig-bd. DR InterPro; IPR036734; Neur_chan_lig-bd_sf. DR InterPro; IPR006201; Neur_channel. DR InterPro; IPR036719; Neuro-gated_channel_TM_sf. DR InterPro; IPR038050; Neuro_actylchol_rec. DR InterPro; IPR006029; Neurotrans-gated_channel_TM. DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS. DR NCBIfam; TIGR00860; LIC; 1. DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 2. DR PRINTS; PR01079; GABAARALPHA. DR PRINTS; PR01614; GABAARALPHA1. DR PRINTS; PR00253; GABAARECEPTR. DR PRINTS; PR00252; NRIONCHANNEL. DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1. DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. DR PDBsum; 6DW0; -. DR PDBsum; 6DW1; -. DR PDBsum; 9OUO; -. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Chloride; Chloride channel; KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Ion channel; KW Ion transport; Ligand-gated ion channel; Membrane; KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..27 FT /evidence="ECO:0000255" FT CHAIN 28..455 FT /note="Gamma-aminobutyric acid receptor subunit alpha-1" FT /id="PRO_0000000430" FT TOPO_DOM 28..252 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 253..273 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P14867" FT TOPO_DOM 274..278 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 279..300 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P14867" FT TOPO_DOM 301..310 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 311..332 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P14867" FT TOPO_DOM 333..420 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 421..440 FT /note="Helical" FT /evidence="ECO:0000250|UniProtKB:P14867" FT TOPO_DOM 441..455 FT /note="Extracellular" FT /evidence="ECO:0000305" FT BINDING 93 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="ligand shared with the neighboring beta FT subunit" FT /evidence="ECO:0000269|PubMed:30044221, FT ECO:0007744|PDB:6DW0, ECO:0007744|PDB:6DW1" FT BINDING 156 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="ligand shared with the neighboring beta FT subunit" FT /evidence="ECO:0000269|PubMed:30044221, FT ECO:0007744|PDB:6DW0, ECO:0007744|PDB:6DW1" FT CARBOHYD 37 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 137 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:30044221, FT ECO:0007744|PDB:6DW0, ECO:0007744|PDB:6DW1" FT DISULFID 165..179 FT /evidence="ECO:0000269|PubMed:30044221, FT ECO:0007744|PDB:6DW0, ECO:0007744|PDB:6DW1" FT MUTAGEN 91 FT /note="F->L: Strongly decreases the affinity for FT GABA-dependent channel gating." FT /evidence="ECO:0000269|PubMed:1376242" FT CONFLICT 91 FT /note="F -> L (in Ref. 3; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 435 FT /note="L -> I (in Ref. 1; no nucleotide entry)" FT /evidence="ECO:0000305" FT HELIX 40..45 FT /evidence="ECO:0007829|PDB:6DW1" FT TURN 46..51 FT /evidence="ECO:0007829|PDB:6DW1" FT TURN 58..61 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 65..76 FT /evidence="ECO:0007829|PDB:6DW1" FT TURN 81..84 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 85..95 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:6DW1" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:6DW1" FT HELIX 117..119 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 145..148 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 157..164 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 176..184 FT /evidence="ECO:0007829|PDB:6DW1" FT TURN 190..192 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:6DW1" FT HELIX 201..203 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 205..207 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 215..225 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:6DW1" FT STRAND 235..247 FT /evidence="ECO:0007829|PDB:6DW1" SQ SEQUENCE 455 AA; 51754 MW; A270B43423B4086E CRC64; MKKSRGLSDY LWAWTLILST LSGRSYGQPS QDELKDNTTV FTRILDRLLD GYDNRLRPGL GERVTEVKTD IFVTSFGPVS DHDMEYTIDV FFRQSWKDER LKFKGPMTVL RLNNLMASKI WTPDTFFHNG KKSVAHNMTM PNKLLRITED GTLLYTMRLT VRAECPMHLE DFPMDAHACP LKFGSYAYTR AEVVYEWTRE PARSVVVAED GSRLNQYDLL GQTVDSGIVQ SSTGEYVVMT THFHLKRKIG YFVIQTYLPC IMTVILSQVS FWLNRESVPA RTVFGVTTVL TMTTLSISAR NSLPKVAYAT AMDWFIAVCY AFVFSALIEF ATVNYFTKRG YAWDGKSVVP EKPKKVKDPL IKKNNTYAPT ATSYTPNLAR GDPGLATIAK SATIEPKEVK PETKPPEPKK TFNSVSKIDR LSRIAFPLLF GIFNLVYWAT YLNREPQLKA PTPHQ //