ID GBRB3_HUMAN Reviewed; 473 AA. AC P28472; B7Z2W1; B7Z825; F5H3D2; H7BYV8; Q14352; Q96FM5; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 27-MAR-2024, entry version 223. DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-3; DE AltName: Full=GABA(A) receptor subunit beta-3; DE Flags: Precursor; GN Name=GABRB3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1664410; DOI=10.1016/0888-7543(91)90034-c; RA Wagstaff J., Chaillet J.R., Lalande M.; RT "The GABAA receptor beta 3 subunit gene: characterization of a human cDNA RT from chromosome 15q11q13 and mapping to a region of conserved synteny on RT mouse chromosome 7."; RL Genomics 11:1071-1078(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Brain, and Testis; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-173. RC TISSUE=Eye; 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 [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80 (ISOFORMS 1 AND 2). RC TISSUE=Fibroblast; RX PubMed=8382702; DOI=10.1016/s0021-9258(18)53626-7; RA Kirkness E.F., Fraser C.M.; RT "A strong promoter element is located between alternative exons of a gene RT encoding the human gamma-aminobutyric acid-type A receptor beta 3 subunit RT (GABRB3)."; RL J. Biol. Chem. 268:4420-4428(1993). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-153 AND 183-227. RX PubMed=1714232; RA Wagstaff J., Knoll J.H.M., Fleming J., Kirkness E.F., Martin-Gallardo A., RA Greenberg F., Graham J.M. Jr., Menninger J., Ward D., Venter J.C., RA Lalande M.; RT "Localization of the gene encoding the GABAA receptor beta 3 subunit to the RT Angelman/Prader-Willi region of human chromosome 15."; RL Am. J. Hum. Genet. 49:330-337(1991). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. 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 [9] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=22243422; DOI=10.1021/bi201772m; RA Chiara D.C., Dostalova Z., Jayakar S.S., Zhou X., Miller K.W., Cohen J.B.; RT "Mapping general anesthetic binding site(s) in human alpha1beta3 gamma- RT aminobutyric acid type A receptors with [3H]TDBzl-etomidate, a RT photoreactive etomidate analogue."; RL Biochemistry 51:836-847(2012). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25489750; DOI=10.3791/52115; RA Brown L.E., Fuchs C., Nicholson M.W., Stephenson F.A., Thomson A.M., RA Jovanovic J.N.; RT "Inhibitory synapse formation in a co-culture model incorporating GABAergic RT medium spiny neurons and HEK293 cells stably expressing GABAA receptors."; RL J. Vis. Exp. 2014:E52115-E52115(2014). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 26-473 IN COMPLEX WITH THE RP AGONIST BENZAMIDINE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, RP GLYCOSYLATION AT ASN-33; ASN-105 AND ASN-174, AND DISULFIDE BOND. RX PubMed=24909990; DOI=10.1038/nature13293; RA Miller P.S., Aricescu A.R.; RT "Crystal structure of a human GABAA receptor."; RL Nature 512:270-275(2014). RN [12] RP VARIANT HIS-217, AND CHARACTERIZATION OF VARIANT HIS-217. RX PubMed=12189488; DOI=10.1007/s00439-002-0766-7; RA Buhr A., Bianchi M.T., Baur R., Courtet P., Pignay V., Boulenger J.P., RA Gallati S., Hinkle D.J., Macdonald R.L., Sigel E.; RT "Functional characterization of the new human GABA(A) receptor mutation RT beta3(R192H)."; RL Hum. Genet. 111:154-160(2002). RN [13] RP VARIANT ECA5 ARG-32, CHARACTERIZATION OF VARIANT ECA5 ARG-32, VARIANTS ECA5 RP SER-11 AND PHE-15 (ISOFORM 2), CHARACTERIZATION OF VARIANTS ECA5 SER-11 AND RP PHE-15 (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=18514161; DOI=10.1016/j.ajhg.2008.04.020; RA Tanaka M., Olsen R.W., Medina M.T., Schwartz E., Alonso M.E., Duron R.M., RA Castro-Ortega R., Martinez-Juarez I.E., Pascual-Castroviejo I., RA Machado-Salas J., Silva R., Bailey J.N., Bai D., Ochoa A., Jara-Prado A., RA Pineda G., Macdonald R.L., Delgado-Escueta A.V.; RT "Hyperglycosylation and reduced GABA currents of mutated GABRB3 polypeptide RT in remitting childhood absence epilepsy."; RL Am. J. Hum. Genet. 82:1249-1261(2008). RN [14] RP CHARACTERIZATION OF VARIANT ECA5 ARG-32, FUNCTION, SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=22303015; DOI=10.1074/jbc.m111.332528; RA Gurba K.N., Hernandez C.C., Hu N., Macdonald R.L.; RT "GABRB3 mutation, G32R, associated with childhood absence epilepsy alters RT alpha1beta3gamma2L gamma-aminobutyric acid type A (GABAA) receptor RT expression and channel gating."; RL J. Biol. Chem. 287:12083-12097(2012). RN [15] RP INVOLVEMENT IN DEE43, AND VARIANT DEE43 ASN-120. 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., Fiol M., RA Fountain N.B., French J., Friedman D., Geller E.B., Glauser T., Glynn S., RA Haut S.R., Hayward J., Helmers S.L., Joshi S., Kanner A., Kirsch H.E., RA Knowlton R.C., Kossoff E.H., Kuperman R., Kuzniecky R., Lowenstein D.H., RA McGuire S.M., Motika P.V., Novotny E.J., Ottman R., Paolicchi J.M., RA Parent J.M., Park K., Poduri A., Scheffer I.E., Shellhaas R.A., Sherr E.H., RA Shih J.J., Singh R., Sirven J., Smith M.C., Sullivan J., Lin Thio L., RA Venkat A., 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 [16] RP VARIANT DEE43 HIS-138 INS. RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772; RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L., RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E., RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S., RA Rouleau G.A., Michaud J.L.; RT "De novo mutations in moderate or severe intellectual disability."; RL PLoS Genet. 10:E1004772-E1004772(2014). RN [17] RP INVOLVEMENT IN DEE43, AND VARIANTS DEE43 ASN-120; MET-157; PHE-182; RP LYS-249; GLN-256; HIS-293 AND THR-305. RX PubMed=27476654; DOI=10.1016/j.ajhg.2016.06.003; RG Epi4K Consortium; RT "De novo mutations in SLC1A2 and CACNA1A are important causes of epileptic RT encephalopathies."; RL Am. J. Hum. Genet. 99:287-298(2016). RN [18] RP CHARACTERIZATION OF VARIANT DEE43 ASN-120, 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 receptor RT function."; RL Ann. Neurol. 79:806-825(2016). RN [19] RP VARIANT DEE43 ILE-287. RX PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263; RA Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A., RA Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L., Kurian M.A., RA Scott R.H.; RT "Improving diagnosis and broadening the phenotypes in early-onset seizure RT and severe developmental delay disorders through gene panel analysis."; RL J. Med. Genet. 53:310-317(2016). RN [20] RP VARIANT GLN-232. RX PubMed=28544625; DOI=10.1002/ajmg.a.38282; RA Le S.V., Le P.H.T., Le T.K.V., Kieu Huynh T.T., Hang Do T.T.; RT "A mutation in GABRB3 associated with Dravet syndrome."; RL Am. J. Med. Genet. A 173:2126-2131(2017). RN [21] RP VARIANTS DEE43 PHE-124 AND PHE-254. RX PubMed=27864847; DOI=10.1002/humu.23149; RG Clinical Study Group; RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D., RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S., RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.; RT "Diagnostic targeted resequencing in 349 patients with drug-resistant RT pediatric epilepsies identifies causative mutations in 30 different RT genes."; RL Hum. Mutat. 38:216-225(2017). CC -!- FUNCTION: Ligand-gated chloride channel which is a component of the CC heteropentameric receptor for GABA, the major inhibitory CC neurotransmitter in the brain (PubMed:18514161, PubMed:22303015, CC PubMed:26950270, PubMed:22243422, PubMed:24909990). Plays an important CC role in the formation of functional inhibitory GABAergic synapses in CC addition to mediating synaptic inhibition as a GABA-gated ion channel CC (PubMed:25489750). The gamma2 subunit is necessary but not sufficient CC for a rapid formation of active synaptic contacts and the synaptogenic CC effect of this subunit is influenced by the type of alpha and beta CC subunits present in the receptor pentamer (By similarity). The CC alpha1/beta3/gamma2 receptor exhibits synaptogenic activity CC (PubMed:25489750). The alpha2/beta3/gamma2 receptor shows very little CC or no synaptogenic activity (By similarity). Functions also as CC histamine receptor and mediates cellular responses to histamine CC (PubMed:18281286). Plays an important role in somatosensation and in CC the production of antinociception (By similarity). CC {ECO:0000250|UniProtKB:P63080, ECO:0000269|PubMed:18281286, CC ECO:0000269|PubMed:18514161, ECO:0000269|PubMed:22243422, CC ECO:0000269|PubMed:22303015, ECO:0000269|PubMed:24909990, CC ECO:0000269|PubMed:25489750, ECO:0000269|PubMed:26950270}. CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma, CC delta and rho chains (PubMed:22243422, PubMed:18281286, CC PubMed:18514161, PubMed:24909990). Can form functional homopentamers CC (in vitro) (PubMed:22303015). Interacts with UBQLN1 (By similarity). CC May interact with KIF21B (By similarity). Identified in a complex of CC 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 CC (By similarity). Interacts with LHFPL4 (By similarity). Interacts with CC GIT1; this interaction is required for synaptic GABRB3 surface CC stability and inhibitory synapse strength (By similarity). CC {ECO:0000250|UniProtKB:P63079, ECO:0000250|UniProtKB:P63080, CC ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:18514161, CC ECO:0000269|PubMed:22243422, ECO:0000269|PubMed:22303015, CC ECO:0000269|PubMed:24909990}. CC -!- INTERACTION: CC P28472; P28472: GABRB3; NbExp=5; IntAct=EBI-6258252, EBI-6258252; CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane CC protein {ECO:0000269|PubMed:24909990}. Cell membrane CC {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:18514161, CC ECO:0000269|PubMed:22243422, ECO:0000269|PubMed:22303015, CC ECO:0000269|PubMed:24909990, ECO:0000269|PubMed:26950270}; Multi-pass CC membrane protein {ECO:0000269|PubMed:24909990}. Cytoplasmic vesicle CC membrane {ECO:0000250|UniProtKB:P63079}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Isoforms differ in their signal region.; CC Name=1; CC IsoId=P28472-1; Sequence=Displayed; CC Name=2; CC IsoId=P28472-2; Sequence=VSP_000088; CC Name=3; CC IsoId=P28472-3; Sequence=VSP_046126; CC Name=4; CC IsoId=P28472-4; Sequence=VSP_046676; CC -!- POLYMORPHISM: GABRB3 variants may be associated with insomnia, a CC condition of inability to initiate or maintain sleep [MIM:137192]. CC -!- DISEASE: Epilepsy, childhood absence 5 (ECA5) [MIM:612269]: A subtype CC of idiopathic generalized epilepsy characterized by an onset at age 6-7 CC years, frequent absence seizures (several per day) and bilateral, CC synchronous, symmetric 3-Hz spike waves on EEG. Tonic-clonic seizures CC often develop in adolescence. Absence seizures may either remit or CC persist into adulthood. {ECO:0000269|PubMed:18514161, CC ECO:0000269|PubMed:22303015}. Note=Disease susceptibility is associated CC with variants affecting the gene represented in this entry. CC -!- DISEASE: Developmental and epileptic encephalopathy 43 (DEE43) CC [MIM:617113]: A form of epileptic encephalopathy, a heterogeneous group CC of severe early-onset epilepsies characterized by refractory seizures, CC neurodevelopmental impairment, and poor prognosis. Development is CC normal prior to seizure onset, after which cognitive and motor delays CC become apparent. DEE43 inheritance is autosomal dominant. CC {ECO:0000269|PubMed:23934111, ECO:0000269|PubMed:25356899, CC ECO:0000269|PubMed:26950270, ECO:0000269|PubMed:26993267, CC ECO:0000269|PubMed:27476654, ECO:0000269|PubMed:27864847}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. 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. GABRB3 sub- CC subfamily. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Forbidden fruit - Issue 56 CC of March 2005; CC URL="https://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; M82919; AAA52511.1; -; mRNA. DR EMBL; AK295167; BAH11997.1; -; mRNA. DR EMBL; AK302822; BAH13811.1; -; mRNA. DR EMBL; AC009878; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011196; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC104569; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC127511; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC135999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC145167; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC145196; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; EU606048; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471151; EAW57655.1; -; Genomic_DNA. DR EMBL; BC010641; AAH10641.1; -; mRNA. DR EMBL; L04311; AAA52508.1; -; Genomic_DNA. DR EMBL; L04311; AAA52507.1; -; Genomic_DNA. DR CCDS; CCDS10018.1; -. [P28472-2] DR CCDS; CCDS10019.1; -. [P28472-1] DR CCDS; CCDS53920.1; -. [P28472-4] DR CCDS; CCDS53921.1; -. [P28472-3] DR PIR; A55275; A55275. DR PIR; B45468; B45468. DR RefSeq; NP_000805.1; NM_000814.5. [P28472-1] DR RefSeq; NP_001178249.1; NM_001191320.1. [P28472-4] DR RefSeq; NP_001178250.1; NM_001191321.2. [P28472-3] DR RefSeq; NP_001265560.1; NM_001278631.1. [P28472-4] DR RefSeq; NP_068712.1; NM_021912.4. [P28472-2] DR PDB; 4COF; X-ray; 2.97 A; A/B/C/D/E=26-332, A/B/C/D/E=447-473. DR PDB; 5O8F; X-ray; 3.20 A; A/B/C/D/E=26-246. DR PDB; 5OJM; X-ray; 3.30 A; A/B/C/D/E=26-242. DR PDB; 6A96; EM; 3.51 A; B/C/D/E=1-332. DR PDB; 6HUG; EM; 3.10 A; B/E=26-473. DR PDB; 6HUJ; EM; 3.04 A; B/E=26-473. DR PDB; 6HUK; EM; 3.69 A; B/E=26-473. DR PDB; 6HUO; EM; 3.26 A; B/E=26-473. DR PDB; 6HUP; EM; 3.58 A; B/E=26-473. DR PDB; 6I53; EM; 3.20 A; B/E=26-473. DR PDB; 6QFA; EM; 2.49 A; A/B/C/D/E=26-332, A/B/C/D/E=447-473. DR PDB; 7PBD; EM; 3.04 A; B/C/E=33-332, B/C/E=447-473. DR PDB; 7PBZ; EM; 2.79 A; B/C/E=26-332, B/C/E=447-473. DR PDB; 7PC0; EM; 3.00 A; B/C/E=33-332, B/C/E=447-473. DR PDB; 7QN5; EM; 2.50 A; B/C/D=1-473. DR PDB; 7QN6; EM; 2.90 A; A/B/C/D=1-473. DR PDB; 7QN7; EM; 3.00 A; B/C/D=1-473. DR PDB; 7QN8; EM; 3.10 A; A/B/C/D=1-473. DR PDB; 7QN9; EM; 2.90 A; B/C/D=1-473. DR PDB; 7QNA; EM; 3.00 A; B/D/E=1-473. DR PDB; 7QNB; EM; 3.10 A; B/D/E=1-473. DR PDB; 7QNC; EM; 2.90 A; B/C/D=1-473. DR PDB; 7QND; EM; 3.40 A; A/B/C/D=1-473. DR PDB; 7QNE; EM; 2.70 A; B/E=1-473. DR PDB; 8PVB; EM; 3.60 A; A=26-332. DR PDBsum; 4COF; -. DR PDBsum; 5O8F; -. DR PDBsum; 5OJM; -. DR PDBsum; 6A96; -. DR PDBsum; 6HUG; -. DR PDBsum; 6HUJ; -. DR PDBsum; 6HUK; -. DR PDBsum; 6HUO; -. DR PDBsum; 6HUP; -. DR PDBsum; 6I53; -. DR PDBsum; 6QFA; -. DR PDBsum; 7PBD; -. DR PDBsum; 7PBZ; -. DR PDBsum; 7PC0; -. DR PDBsum; 7QN5; -. DR PDBsum; 7QN6; -. DR PDBsum; 7QN7; -. DR PDBsum; 7QN8; -. DR PDBsum; 7QN9; -. DR PDBsum; 7QNA; -. DR PDBsum; 7QNB; -. DR PDBsum; 7QNC; -. DR PDBsum; 7QND; -. DR PDBsum; 7QNE; -. DR PDBsum; 8PVB; -. DR AlphaFoldDB; P28472; -. DR EMDB; EMD-0275; -. DR EMDB; EMD-0279; -. DR EMDB; EMD-0280; -. DR EMDB; EMD-0282; -. DR EMDB; EMD-0283; -. DR EMDB; EMD-11610; -. DR EMDB; EMD-11657; -. DR EMDB; EMD-13290; -. DR EMDB; EMD-13314; -. DR EMDB; EMD-13315; -. DR EMDB; EMD-14067; -. DR EMDB; EMD-14068; -. DR EMDB; EMD-14069; -. DR EMDB; EMD-14070; -. DR EMDB; EMD-14071; -. DR EMDB; EMD-14072; -. DR EMDB; EMD-14073; -. DR EMDB; EMD-14074; -. DR EMDB; EMD-14075; -. DR EMDB; EMD-14076; -. DR EMDB; EMD-17960; -. DR EMDB; EMD-4411; -. DR EMDB; EMD-4542; -. DR EMDB; EMD-6998; -. DR SMR; P28472; -. DR BioGRID; 108836; 13. DR ComplexPortal; CPX-2164; GABA-A receptor, alpha-6/beta-3/gamma-2. DR ComplexPortal; CPX-2166; GABA-A receptor, alpha-3/beta-3/gamma-2. DR ComplexPortal; CPX-2167; GABA-A receptor, alpha-1/beta-3/gamma-2. DR ComplexPortal; CPX-2168; GABA-A receptor, alpha-5/beta-3/gamma-2. DR ComplexPortal; CPX-2174; GABA-A receptor, alpha-2/beta-3/gamma-2. DR ComplexPortal; CPX-2951; GABA-A receptor, alpha-6/beta-3/delta. DR ComplexPortal; CPX-2954; GABA-A receptor, alpha-4/beta-3/delta. DR DIP; DIP-61029N; -. DR IntAct; P28472; 8. DR STRING; 9606.ENSP00000308725; -. DR BindingDB; P28472; -. DR ChEMBL; CHEMBL1847; -. DR DrugBank; DB12537; 1,2-Benzodiazepine. DR DrugBank; DB00546; Adinazolam. DR DrugBank; DB00404; Alprazolam. DR DrugBank; DB00543; Amoxapine. DR DrugBank; DB11901; Apalutamide. DR DrugBank; DB14719; Bentazepam. DR DrugBank; DB11859; Brexanolone. DR DrugBank; DB01558; Bromazepam. DR DrugBank; DB09017; Brotizolam. DR DrugBank; DB00237; Butabarbital. DR DrugBank; DB00241; Butalbital. DR DrugBank; DB01489; Camazepam. DR DrugBank; DB00475; Chlordiazepoxide. DR DrugBank; DB14715; Cinazepam. DR DrugBank; DB01594; Cinolazepam. DR DrugBank; DB00349; Clobazam. DR DrugBank; DB01068; Clonazepam. DR DrugBank; DB00628; Clorazepic acid. DR DrugBank; DB01559; Clotiazepam. DR DrugBank; DB01553; Cloxazolam. DR DrugBank; DB01511; Delorazepam. DR DrugBank; DB01189; Desflurane. DR DrugBank; DB00829; Diazepam. DR DrugBank; DB13837; Doxefazepam. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01215; Estazolam. DR DrugBank; DB00402; Eszopiclone. DR DrugBank; DB00898; Ethanol. DR DrugBank; DB00189; Ethchlorvynol. DR DrugBank; DB01545; Ethyl loflazepate. DR DrugBank; DB09166; Etizolam. DR DrugBank; DB00292; Etomidate. DR DrugBank; DB01567; Fludiazepam. DR DrugBank; DB01205; Flumazenil. DR DrugBank; DB01544; Flunitrazepam. DR DrugBank; DB00690; Flurazepam. DR DrugBank; DB06716; Fospropofol. DR DrugBank; DB05087; Ganaxolone. DR DrugBank; DB01437; Glutethimide. DR DrugBank; DB00801; Halazepam. DR DrugBank; DB01159; Halothane. DR DrugBank; DB00753; Isoflurane. DR DrugBank; DB01587; Ketazolam. DR DrugBank; DB00555; Lamotrigine. DR DrugBank; DB00431; Lindane. DR DrugBank; DB13643; Loprazolam. DR DrugBank; DB00186; Lorazepam. DR DrugBank; DB13872; Lormetazepam. DR DrugBank; DB13437; Medazepam. DR DrugBank; DB00603; Medroxyprogesterone acetate. DR DrugBank; DB01043; Memantine. DR DrugBank; DB00371; Meprobamate. DR DrugBank; DB00463; Metharbital. DR DrugBank; DB01028; Methoxyflurane. DR DrugBank; DB01107; Methyprylon. DR DrugBank; DB15489; Mexazolam. DR DrugBank; DB00683; Midazolam. DR DrugBank; DB12458; Muscimol. DR DrugBank; DB01595; Nitrazepam. DR DrugBank; DB14028; Nordazepam. DR DrugBank; DB00842; Oxazepam. DR DrugBank; DB14672; Oxazepam acetate. DR DrugBank; DB00312; Pentobarbital. DR DrugBank; DB00252; Phenytoin. DR DrugBank; DB13335; Pinazepam. DR DrugBank; DB00592; Piperazine. DR DrugBank; DB01708; Prasterone. DR DrugBank; DB01588; Prazepam. DR DrugBank; DB00794; Primidone. DR DrugBank; DB00818; Propofol. DR DrugBank; DB01589; Quazepam. DR DrugBank; DB12404; Remimazolam. DR DrugBank; DB01236; Sevoflurane. DR DrugBank; DB09118; Stiripentol. DR DrugBank; DB00306; Talbutal. DR DrugBank; DB01956; Taurine. DR DrugBank; DB00231; Temazepam. DR DrugBank; DB11582; Thiocolchicoside. DR DrugBank; DB00897; Triazolam. DR DrugCentral; P28472; -. DR GuidetoPHARMACOLOGY; 412; -. DR TCDB; 1.A.9.5.4; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family. DR GlyCosmos; P28472; 3 sites, No reported glycans. DR GlyGen; P28472; 3 sites. DR iPTMnet; P28472; -. DR PhosphoSitePlus; P28472; -. DR BioMuta; GABRB3; -. DR DMDM; 120773; -. DR EPD; P28472; -. DR MassIVE; P28472; -. DR MaxQB; P28472; -. DR PaxDb; 9606-ENSP00000308725; -. DR PeptideAtlas; P28472; -. DR ProteomicsDB; 26235; -. DR ProteomicsDB; 43749; -. DR ProteomicsDB; 54485; -. [P28472-1] DR ProteomicsDB; 54486; -. [P28472-2] DR ABCD; P28472; 3 sequenced antibodies. DR Antibodypedia; 22323; 397 antibodies from 39 providers. DR DNASU; 2562; -. DR Ensembl; ENST00000299267.9; ENSP00000299267.4; ENSG00000166206.16. [P28472-2] DR Ensembl; ENST00000311550.10; ENSP00000308725.5; ENSG00000166206.16. [P28472-1] DR Ensembl; ENST00000400188.7; ENSP00000383049.3; ENSG00000166206.16. [P28472-3] DR Ensembl; ENST00000545868.4; ENSP00000439169.1; ENSG00000166206.16. [P28472-4] DR Ensembl; ENST00000636466.1; ENSP00000489768.1; ENSG00000166206.16. [P28472-4] DR GeneID; 2562; -. DR KEGG; hsa:2562; -. DR MANE-Select; ENST00000311550.10; ENSP00000308725.5; NM_000814.6; NP_000805.1. DR UCSC; uc001zaz.5; human. [P28472-1] DR AGR; HGNC:4083; -. DR CTD; 2562; -. DR DisGeNET; 2562; -. DR GeneCards; GABRB3; -. DR GeneReviews; GABRB3; -. DR HGNC; HGNC:4083; GABRB3. DR HPA; ENSG00000166206; Tissue enhanced (brain, retina). DR MalaCards; GABRB3; -. DR MIM; 137192; gene+phenotype. DR MIM; 612269; phenotype. DR MIM; 617113; phenotype. DR neXtProt; NX_P28472; -. DR OpenTargets; ENSG00000166206; -. DR Orphanet; 64280; Childhood absence epilepsy. DR Orphanet; 2382; Lennox-Gastaut syndrome. DR Orphanet; 106; NON RARE IN EUROPE: Autism. DR PharmGKB; PA28497; -. DR VEuPathDB; HostDB:ENSG00000166206; -. DR eggNOG; KOG3643; Eukaryota. DR GeneTree; ENSGT00940000154713; -. DR HOGENOM; CLU_010920_0_2_1; -. DR InParanoid; P28472; -. DR OMA; EMHNEVG; -. DR OrthoDB; 4265336at2759; -. DR PhylomeDB; P28472; -. DR TreeFam; TF315453; -. DR PathwayCommons; P28472; -. DR Reactome; R-HSA-1236394; Signaling by ERBB4. DR Reactome; R-HSA-977443; GABA receptor activation. DR SignaLink; P28472; -. DR SIGNOR; P28472; -. DR BioGRID-ORCS; 2562; 12 hits in 1158 CRISPR screens. DR ChiTaRS; GABRB3; human. DR GeneWiki; GABRB3; -. DR GenomeRNAi; 2562; -. DR Pharos; P28472; Tclin. DR PRO; PR:P28472; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; P28472; Protein. DR Bgee; ENSG00000166206; Expressed in middle temporal gyrus and 153 other cell types or tissues. DR ExpressionAtlas; P28472; baseline and differential. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:1902711; C:GABA-A receptor complex; IDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045202; C:synapse; IBA:GO_Central. DR GO; GO:0004890; F:GABA-A receptor activity; IMP:UniProtKB. DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IDA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central. DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB. DR GO; GO:1902476; P:chloride transmembrane transport; IDA:GO_Central. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:ComplexPortal. DR GO; GO:1904862; P:inhibitory synapse assembly; IDA:UniProtKB. DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0051932; P:synaptic transmission, GABAergic; NAS:ComplexPortal. DR CDD; cd18999; LGIC_ECD_GABAAR_B; 1. DR CDD; cd19053; LGIC_TM_GABAAR_beta; 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; 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; 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:SF571; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT BETA-3; 1. DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 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; 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 Genevisible; P28472; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Chloride; KW Chloride channel; Cytoplasmic vesicle; Direct protein sequencing; KW Disease variant; Disulfide bond; Epilepsy; 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..25 FT /evidence="ECO:0000255" FT CHAIN 26..473 FT /note="Gamma-aminobutyric acid receptor subunit beta-3" FT /id="PRO_0000000462" FT TOPO_DOM 26..245 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:24909990" FT TRANSMEM 246..267 FT /note="Helical" FT TOPO_DOM 268..270 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:24909990" FT TRANSMEM 271..293 FT /note="Helical" FT TOPO_DOM 294..304 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:24909990" FT TRANSMEM 305..327 FT /note="Helical" FT TOPO_DOM 328..450 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:24909990" FT TRANSMEM 451..472 FT /note="Helical" FT BINDING 120..122 FT /ligand="benzamidine" FT /ligand_id="ChEBI:CHEBI:187892" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24909990" FT BINDING 180..182 FT /ligand="benzamidine" FT /ligand_id="ChEBI:CHEBI:187892" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24909990, FT ECO:0007744|PDB:4COF" FT BINDING 225 FT /ligand="benzamidine" FT /ligand_id="ChEBI:CHEBI:187892" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24909990" FT CARBOHYD 33 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24909990" FT CARBOHYD 105 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24909990" FT CARBOHYD 174 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24909990" FT DISULFID 161..175 FT /evidence="ECO:0000269|PubMed:24909990" FT VAR_SEQ 1..85 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046676" FT VAR_SEQ 1..26 FT /note="MWGLAGGRLFGIFSAPVLVAVVCCAQ -> MCSGLLELLLPIWLSWTLGTRG FT SEPR (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_000088" FT VAR_SEQ 3..80 FT /note="GLAGGRLFGIFSAPVLVAVVCCAQSVNDPGNMSFVKETVDKLLKGYDIRLRP FT DFGGPPVCVGMNIDIASIDMVSEVNM -> ATYQTEE (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046126" FT VARIANT 32 FT /note="G -> R (in ECA5; the mutant protein is FT hyperglycosylated and has reduced mean current densities FT compared to wild-type; dbSNP:rs71651682)" FT /evidence="ECO:0000269|PubMed:18514161, FT ECO:0000269|PubMed:22303015" FT /id="VAR_047957" FT VARIANT 120 FT /note="D -> N (in DEE43; no effect on localization to the FT plasma membrane; decreased GABA-gated chloride ion channel FT activity; decreased single channel open probability; FT dbSNP:rs886037938)" FT /evidence="ECO:0000269|PubMed:23934111, FT ECO:0000269|PubMed:26950270, ECO:0000269|PubMed:27476654" FT /id="VAR_077076" FT VARIANT 124 FT /note="L -> F (in DEE43; dbSNP:rs1057519550)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078223" FT VARIANT 138 FT /note="N -> NH (in DEE43)" FT /evidence="ECO:0000269|PubMed:25356899" FT /id="VAR_078619" FT VARIANT 157 FT /note="T -> M (in DEE43; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27476654" FT /id="VAR_077077" FT VARIANT 173 FT /note="Q -> L (in dbSNP:rs17850679)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_047958" FT VARIANT 182 FT /note="Y -> F (in DEE43; dbSNP:rs886037939)" FT /evidence="ECO:0000269|PubMed:27476654" FT /id="VAR_077078" FT VARIANT 217 FT /note="R -> H (found in a subject suffering from insomnia; FT functional analysis reveals a slower rate of the fast phase FT of desensitization compared with alpha1beta3gamma2SGABA(A) FT receptors; current deactivation is faster in the mutated FT receptors; dbSNP:rs121913125)" FT /evidence="ECO:0000269|PubMed:12189488" FT /id="VAR_047959" FT VARIANT 232 FT /note="R -> Q (found in patients with Dravet syndrome; FT uncertain significance; dbSNP:rs797045045)" FT /evidence="ECO:0000269|PubMed:28544625" FT /id="VAR_079429" FT VARIANT 249 FT /note="Q -> K (in DEE43; dbSNP:rs886037940)" FT /evidence="ECO:0000269|PubMed:27476654" FT /id="VAR_077079" FT VARIANT 254 FT /note="S -> F (in DEE43; dbSNP:rs1057519549)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078224" FT VARIANT 256 FT /note="L -> Q (in DEE43; dbSNP:rs1890228169)" FT /evidence="ECO:0000269|PubMed:27476654" FT /id="VAR_077080" FT VARIANT 287 FT /note="T -> I (in DEE43)" FT /evidence="ECO:0000269|PubMed:26993267" FT /id="VAR_078719" FT VARIANT 293 FT /note="L -> H (in DEE43; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27476654" FT /id="VAR_077081" FT VARIANT 305 FT /note="A -> T (in DEE43; dbSNP:rs886037941)" FT /evidence="ECO:0000269|PubMed:27476654" FT /id="VAR_077082" FT CONFLICT 97 FT /note="L -> H (in Ref. 2; BAH13811)" FT /evidence="ECO:0000305" FT CONFLICT 193 FT /note="W -> R (in Ref. 2; BAH11997)" FT /evidence="ECO:0000305" FT HELIX 35..45 FT /evidence="ECO:0007829|PDB:6QFA" FT TURN 54..57 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 61..76 FT /evidence="ECO:0007829|PDB:6QFA" FT TURN 77..80 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 81..93 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 106..108 FT /evidence="ECO:0007829|PDB:7QN5" FT HELIX 110..115 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 126..131 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 138..143 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 147..160 FT /evidence="ECO:0007829|PDB:6QFA" FT TURN 166..169 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 172..183 FT /evidence="ECO:0007829|PDB:6QFA" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 189..193 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 203..205 FT /evidence="ECO:0007829|PDB:7QN5" FT STRAND 209..224 FT /evidence="ECO:0007829|PDB:6QFA" FT STRAND 229..241 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 244..249 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 251..260 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 261..266 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 272..295 FT /evidence="ECO:0007829|PDB:6QFA" FT HELIX 305..330 FT /evidence="ECO:0007829|PDB:6QFA" FT TURN 335..337 FT /evidence="ECO:0007829|PDB:7QNE" FT HELIX 448..471 FT /evidence="ECO:0007829|PDB:7QN5" FT VARIANT P28472-2:11 FT /note="P -> S (in ECA5, the mutant protein is FT hyperglycosylated and has reduced mean current densities FT compared to wild-type; dbSNP:rs25409)" FT /evidence="ECO:0000269|PubMed:18514161" FT /id="VAR_082790" FT VARIANT P28472-2:15 FT /note="S -> F (in ECA5, the mutant protein is FT hyperglycosylated and has reduced mean current densities FT compared to wild-type; dbSNP:rs121913126)" FT /evidence="ECO:0000269|PubMed:18514161" FT /id="VAR_082791" SQ SEQUENCE 473 AA; 54116 MW; D63597F7FBC69E71 CRC64; MWGLAGGRLF GIFSAPVLVA VVCCAQSVND PGNMSFVKET VDKLLKGYDI RLRPDFGGPP VCVGMNIDIA SIDMVSEVNM DYTLTMYFQQ YWRDKRLAYS GIPLNLTLDN RVADQLWVPD TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE SYGYTTDDIE FYWRGGDKAV TGVERIELPQ FSIVEHRLVS RNVVFATGAY PRLSLSFRLK RNIGYFILQT YMPSILITIL SWVSFWINYD ASAARVALGI TTVLTMTTIN THLRETLPKI PYVKAIDMYL MGCFVFVFLA LLEYAFVNYI FFGRGPQRQK KLAEKTAKAK NDRSKSESNR VDAHGNILLT SLEVHNEMNE VSGGIGDTRN SAISFDNSGI QYRKQSMPRE GHGRFLGDRS LPHKKTHLRR RSSQLKIKIP DLTDVNAIDR WSRIVFPFTF SLFNLVYWLY YVN //