ID GBRB1_HUMAN Reviewed; 474 AA. AC P18505; B2R6U7; D6REL3; Q16166; Q8TBK3; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 2. DT 25-OCT-2017, entry version 181. DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-1; DE AltName: Full=GABA(A) receptor subunit beta-1; DE Flags: Precursor; GN Name=GABRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2465923; DOI=10.1016/0014-5793(89)80563-0; RA Schofield P.R., Pritchett D.B., Sontheimer H., Kettenmann H., RA Seeburg P.H.; RT "Sequence and expression of human GABAA receptor alpha 1 and beta 1 RT subunits."; RL FEBS Lett. 244:361-364(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1655634; DOI=10.1016/0888-7543(91)90189-L; RA Kirkness E.F., Kusiak J.W., Fleming J.T., Menninger J., Gocayne J.D., RA Ward D.C., Venter J.C.; RT "Isolation, characterization, and localization of human genomic DNA RT encoding the beta 1 subunit of the GABAA receptor (GABRB1)."; RL Genomics 10:985-995(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Fetal brain; RX PubMed=24722188; DOI=10.1038/ncomms4650; RA Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., RA Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., RA Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J., RA Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., RA Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., RA Iakoucheva L.M.; RT "Protein interaction network of alternatively spliced isoforms from RT brain links genetic risk factors for autism."; RL Nat. Commun. 5:3650-3650(2014). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP ASN-429. RC TISSUE=Brain; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 19-474 (ISOFORM 1). RX PubMed=2160058; RA Garrett K.M., Saito N., Duman R.S., Abel M.S., Ashton R.A., RA Fujimori S., Beer B., Tallman J.F., Vitek M.P., Blume A.J.; RT "Differential expression of gamma-aminobutyric acidA receptor RT subunits."; RL Mol. Pharmacol. 37:652-657(1990). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 404-434 (ISOFORM 1), AND VARIANT RP GLN-421. RX PubMed=8178835; DOI=10.1002/ajmg.1320540105; RA Coon H., Sobell J., Heston L., Sommer S., Hoff M., Holik J., Umar F., RA Robertson M., Reimherr F., Wender P.; RT "Search for mutations in the beta 1 GABAA receptor subunit gene in RT patients with schizophrenia."; RL Am. J. Med. Genet. 54:12-20(1994). RN [10] RP INVOLVEMENT IN EIEE45, AND VARIANT EIEE45 SER-246. RX PubMed=23934111; DOI=10.1038/nature12439; RG Epi4K Consortium; RG Epilepsy Phenome/Genome Project; RA Allen A.S., Berkovic S.F., Cossette P., Delanty N., Dlugos D., RA Eichler E.E., Epstein M.P., Glauser T., Goldstein D.B., Han Y., RA Heinzen E.L., Hitomi Y., Howell K.B., Johnson M.R., Kuzniecky R., RA Lowenstein D.H., Lu Y.F., Madou M.R., Marson A.G., Mefford H.C., RA Esmaeeli Nieh S., O'Brien T.J., Ottman R., Petrovski S., Poduri A., RA Ruzzo E.K., Scheffer I.E., Sherr E.H., Yuskaitis C.J., Abou-Khalil B., RA Alldredge B.K., Bautista J.F., Berkovic S.F., Boro A., Cascino G.D., RA Consalvo D., Crumrine P., Devinsky O., Dlugos D., Epstein M.P., RA Fiol M., Fountain N.B., French J., Friedman D., Geller E.B., RA Glauser T., Glynn S., Haut S.R., Hayward J., Helmers S.L., Joshi S., RA Kanner A., Kirsch H.E., Knowlton R.C., Kossoff E.H., Kuperman R., RA Kuzniecky R., Lowenstein D.H., McGuire S.M., Motika P.V., RA Novotny E.J., Ottman R., Paolicchi J.M., Parent J.M., Park K., RA Poduri A., Scheffer I.E., Shellhaas R.A., Sherr E.H., Shih J.J., RA Singh R., Sirven J., Smith M.C., Sullivan J., Lin Thio L., Venkat A., RA Vining E.P., Von Allmen G.K., Weisenberg J.L., Widdess-Walsh P., RA Winawer M.R.; RT "De novo mutations in epileptic encephalopathies."; RL Nature 501:217-221(2013). RN [11] RP VARIANT EIEE45 ILE-287. RX PubMed=27273810; DOI=10.1002/ana.24699; RA Lien E., Vaatevik A.K., Oestern R., Haukanes B.I., Houge G.; RT "A second patient with a de novo GABRB1 mutation and epileptic RT encephalopathy."; RL Ann. Neurol. 80:311-312(2016). RN [12] RP CHARACTERIZATION OF VARIANT EIEE45 SER-246, FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=26950270; DOI=10.1002/ana.24631; RA Janve V.S., Hernandez C.C., Verdier K.M., Hu N., Macdonald R.L.; RT "Epileptic encephalopathy de novo GABRB mutations impair GABAA RT receptor function."; RL Ann. Neurol. 0:0-0(2016). CC -!- FUNCTION: Component of the heteropentameric receptor for GABA, the CC major inhibitory neurotransmitter in the vertebrate brain. CC Functions also as histamine receptor and mediates cellular CC responses to histamine. Functions as receptor for diazepines and CC various anesthetics, such as pentobarbital; these are bound at a CC separate allosteric effector binding site. Functions as ligand- CC gated chloride channel. {ECO:0000269|PubMed:26950270}. CC -!- SUBUNIT: Binds UBQLN1 (By similarity). Heteropentamer, formed by a CC combination of alpha, beta, gamma, delta and rho chains. Interacts CC with KCTD8, KCTD12 and KCTD16; this interaction determines the CC pharmacology and kinetics of the receptor response, the KCTD CC proteins markedly accelerating the GABA-B response, although to CC different extents (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell CC membrane {ECO:0000250|UniProtKB:P50571}; Multi-pass membrane CC protein {ECO:0000250|UniProtKB:P50571}. Cell membrane CC {ECO:0000269|PubMed:26950270}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P50571}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P18505-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=P18505-2; Sequence=VSP_055900, VSP_055901; CC -!- DISEASE: Epileptic encephalopathy, early infantile, 45 (EIEE45) CC [MIM:617153]: A form of epileptic encephalopathy, a heterogeneous CC group of severe childhood onset epilepsies characterized by CC refractory seizures, neurodevelopmental impairment, and poor CC prognosis. Development is normal prior to seizure onset, after CC which cognitive and motor delays become apparent. CC {ECO:0000269|PubMed:23934111, ECO:0000269|PubMed:26950270, CC ECO:0000269|PubMed:27273810}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) CC family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. CC GABRB1 sub-subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Forbidden fruit - Issue CC 56 of March 2005; CC URL="http://web.expasy.org/spotlight/back_issues/056"; 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; X14767; CAA32875.1; -; mRNA. DR EMBL; M59216; AAA35862.1; -; Genomic_DNA. DR EMBL; M59212; AAA35862.1; JOINED; Genomic_DNA. DR EMBL; M59214; AAA35862.1; JOINED; Genomic_DNA. DR EMBL; M59215; AAA35862.1; JOINED; Genomic_DNA. DR EMBL; KJ535054; AHW56693.1; -; mRNA. DR EMBL; AK312720; BAG35594.1; -; mRNA. DR EMBL; AC097712; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105394; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107383; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC107392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471069; EAW93031.1; -; Genomic_DNA. DR EMBL; BC022449; AAH22449.1; -; mRNA. DR EMBL; S70733; AAB30712.1; -; mRNA. DR CCDS; CCDS3474.1; -. [P18505-1] DR PIR; A40336; A40336. DR RefSeq; NP_000803.2; NM_000812.3. [P18505-1] DR UniGene; Hs.254117; -. DR UniGene; Hs.27283; -. DR UniGene; Hs.633316; -. DR ProteinModelPortal; P18505; -. DR SMR; P18505; -. DR BioGrid; 108834; 5. DR IntAct; P18505; 4. DR STRING; 9606.ENSP00000295454; -. DR BindingDB; P18505; -. DR ChEMBL; CHEMBL2111392; -. DR DrugBank; DB00659; Acamprosate. DR DrugBank; DB00546; Adinazolam. DR DrugBank; DB00404; Alprazolam. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB01558; Bromazepam. DR DrugBank; DB00237; Butabarbital. DR DrugBank; DB00241; Butalbital. DR DrugBank; DB00475; Chlordiazepoxide. DR DrugBank; DB01594; Cinolazepam. DR DrugBank; DB00349; Clobazam. DR DrugBank; DB01068; Clonazepam. DR DrugBank; DB00628; Clorazepate. DR DrugBank; DB01559; Clotiazepam. DR DrugBank; DB01189; Desflurane. DR DrugBank; DB00829; Diazepam. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01049; Ergoloid mesylate. DR DrugBank; DB01215; Estazolam. DR DrugBank; DB00402; Eszopiclone. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB00189; Ethchlorvynol. DR DrugBank; DB00292; Etomidate. DR DrugBank; DB01567; Fludiazepam. DR DrugBank; DB01205; Flumazenil. DR DrugBank; DB00690; Flurazepam. DR DrugBank; DB01440; Gamma Hydroxybutyric Acid. DR DrugBank; DB01437; Glutethimide. DR DrugBank; DB00801; Halazepam. DR DrugBank; DB01159; Halothane. DR DrugBank; DB00753; Isoflurane. DR DrugBank; DB01587; Ketazolam. DR DrugBank; DB00431; Lindane. DR DrugBank; DB00186; Lorazepam. DR DrugBank; DB00371; Meprobamate. DR DrugBank; DB00463; Metharbital. DR DrugBank; DB01028; Methoxyflurane. DR DrugBank; DB01107; Methyprylon. DR DrugBank; DB00683; Midazolam. DR DrugBank; DB01595; Nitrazepam. DR DrugBank; DB00334; Olanzapine. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB00312; Pentobarbital. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB01588; Prazepam. DR DrugBank; DB00794; Primidone. DR DrugBank; DB00818; Propofol. DR DrugBank; DB01589; Quazepam. DR DrugBank; DB01236; Sevoflurane. DR DrugBank; DB00306; Talbutal. DR DrugBank; DB00231; Temazepam. DR DrugBank; DB11582; Thiocolchicoside. DR DrugBank; DB00273; Topiramate. DR DrugBank; DB00897; Triazolam. DR iPTMnet; P18505; -. DR PhosphoSitePlus; P18505; -. DR BioMuta; GABRB1; -. DR DMDM; 23831128; -. DR EPD; P18505; -. DR PaxDb; P18505; -. DR PeptideAtlas; P18505; -. DR PRIDE; P18505; -. DR DNASU; 2560; -. DR Ensembl; ENST00000295454; ENSP00000295454; ENSG00000163288. [P18505-1] DR Ensembl; ENST00000510909; ENSP00000426766; ENSG00000163288. [P18505-2] DR GeneID; 2560; -. DR KEGG; hsa:2560; -. DR UCSC; uc062wjg.1; human. [P18505-1] DR CTD; 2560; -. DR DisGeNET; 2560; -. DR EuPathDB; HostDB:ENSG00000163288.13; -. DR GeneCards; GABRB1; -. DR H-InvDB; HIX0004191; -. DR H-InvDB; HIX0164000; -. DR HGNC; HGNC:4081; GABRB1. DR HPA; HPA051297; -. DR MalaCards; GABRB1; -. DR MIM; 137190; gene. DR MIM; 617153; phenotype. DR neXtProt; NX_P18505; -. DR OpenTargets; ENSG00000163288; -. DR PharmGKB; PA28495; -. DR eggNOG; KOG3643; Eukaryota. DR eggNOG; ENOG410XPWH; LUCA. DR GeneTree; ENSGT00760000118821; -. DR HOGENOM; HOG000231335; -. DR HOVERGEN; HBG051707; -. DR InParanoid; P18505; -. DR KO; K05181; -. DR OMA; NAGYWIF; -. DR OrthoDB; EOG091G0805; -. DR PhylomeDB; P18505; -. DR TreeFam; TF315453; -. DR Reactome; R-HSA-112314; Neurotransmitter receptors and postsynaptic signal transmission. DR Reactome; R-HSA-975298; Ligand-gated ion channel transport. DR Reactome; R-HSA-977441; GABA A receptor activation. DR GeneWiki; GABRB1; -. DR GenomeRNAi; 2560; -. DR PRO; PR:P18505; -. DR Proteomes; UP000005640; Chromosome 4. DR Bgee; ENSG00000163288; -. DR CleanEx; HS_GABRB1; -. DR ExpressionAtlas; P18505; baseline and differential. DR Genevisible; P18505; HS. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0030425; C:dendrite; IEA:Ensembl. DR GO; GO:1902711; C:GABA-A receptor complex; IDA:UniProtKB. DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB. DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050811; F:GABA receptor binding; IEA:Ensembl. DR GO; GO:0004890; F:GABA-A receptor activity; ISS:UniProtKB. DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IDA:GO_Central. DR GO; GO:0015276; F:ligand-gated ion channel activity; ISS:UniProtKB. DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB. DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl. DR GO; GO:1902476; P:chloride transmembrane transport; IDA:GO_Central. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:UniProtKB. DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome. DR GO; GO:0006811; P:ion transport; ISS:UniProtKB. DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl. DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl. DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR Gene3D; 1.20.58.390; -; 1. DR Gene3D; 2.70.170.10; -; 1. DR InterPro; IPR006028; GABAA/Glycine_rcpt. DR InterPro; IPR002289; GABAAb_rcpt. 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; IPR006029; Neurotrans-gated_channel_TM. DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS. DR PANTHER; PTHR18945; PTHR18945; 1. DR Pfam; PF02931; Neur_chan_LBD; 1. DR Pfam; PF02932; Neur_chan_memb; 1. DR PRINTS; PR01160; GABAARBETA. DR PRINTS; PR00253; GABAARECEPTR. DR PRINTS; PR00252; NRIONCHANNEL. DR SUPFAM; SSF63712; SSF63712; 1. DR SUPFAM; SSF90112; SSF90112; 1. DR TIGRFAMs; TIGR00860; LIC; 1. DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell junction; Cell membrane; Chloride; KW Chloride channel; Complete proteome; Disease mutation; Disulfide bond; KW Epilepsy; Glycoprotein; Ion channel; Ion transport; KW Ligand-gated ion channel; Membrane; Polymorphism; KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; KW Synapse; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 474 Gamma-aminobutyric acid receptor subunit FT beta-1. FT /FTId=PRO_0000000456. FT TOPO_DOM 26 245 Extracellular. {ECO:0000305}. FT TRANSMEM 246 267 Helical. {ECO:0000305}. FT TRANSMEM 271 293 Helical. {ECO:0000305}. FT TRANSMEM 305 327 Helical. {ECO:0000305}. FT TOPO_DOM 328 451 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 452 473 Helical. {ECO:0000305}. FT REGION 120 122 Agonist binding. {ECO:0000250}. FT REGION 180 182 Agonist binding. {ECO:0000250}. FT REGION 290 311 Allosteric effector binding. FT {ECO:0000250}. FT BINDING 225 225 Agonist. {ECO:0000250}. FT CARBOHYD 105 105 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 174 174 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 161 175 {ECO:0000250}. FT VAR_SEQ 59 87 PPVDVGMRIDVASIDMVSEVNMDYTLTMY -> LYTHHVFP FT AVLERQKAFLFWNPTEPHPRQ (in isoform 2). FT {ECO:0000303|PubMed:24722188}. FT /FTId=VSP_055900. FT VAR_SEQ 88 474 Missing (in isoform 2). FT {ECO:0000303|PubMed:24722188}. FT /FTId=VSP_055901. FT VARIANT 246 246 F -> S (in EIEE45; no effect on FT localization to the plasma membrane; FT increased GABA-gated chloride ion channel FT activity; increased single channel burst FT duration). {ECO:0000269|PubMed:23934111, FT ECO:0000269|PubMed:26950270}. FT /FTId=VAR_077104. FT VARIANT 287 287 T -> I (in EIEE45). FT {ECO:0000269|PubMed:27273810}. FT /FTId=VAR_077105. FT VARIANT 421 421 H -> Q (found in 1.1% of population and FT in some schizophrenic patients; FT dbSNP:rs41311286). FT {ECO:0000269|PubMed:8178835}. FT /FTId=VAR_000302. FT VARIANT 429 429 I -> N (in dbSNP:rs17852014). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_035441. FT CONFLICT 35 35 S -> P (in Ref. 1; CAA32875). FT {ECO:0000305}. FT CONFLICT 117 117 W -> C (in Ref. 7; AAH22449). FT {ECO:0000305}. SQ SEQUENCE 474 AA; 54235 MW; 05DA70F6FCD04E54 CRC64; MWTVQNRESL GLLSFPVMIT MVCCAHSTNE PSNMSYVKET VDRLLKGYDI RLRPDFGGPP VDVGMRIDVA SIDMVSEVNM DYTLTMYFQQ SWKDKRLSYS GIPLNLTLDN RVADQLWVPD TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE SYGYTTDDIE FYWNGGEGAV TGVNKIELPQ FSIVDYKMVS KKVEFTTGAY PRLSLSFRLK RNIGYFILQT YMPSTLITIL SWVSFWINYD ASAARVALGI TTVLTMTTIS THLRETLPKI PYVKAIDIYL MGCFVFVFLA LLEYAFVNYI FFGKGPQKKG ASKQDQSANE KNKLEMNKVQ VDAHGNILLS TLEIRNETSG SEVLTSVSDP KATMYSYDSA SIQYRKPLSS REAYGRALDR HGVPSKGRIR RRASQLKVKI PDLTDVNSID KWSRMFFPIT FSLFNVVYWL YYVH //