GBRB3_HUMAN
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 03-AUG-2022, entry version 214.
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";
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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 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 AlphaFoldDB; P28472; -.
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; 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 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; P28472; -.
DR PeptideAtlas; P28472; -.
DR PRIDE; 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; 344 antibodies from 39 providers.
DR DNASU; 2562; -.
DR Ensembl; ENST00000299267.8; ENSP00000299267.4; ENSG00000166206.15. [P28472-2]
DR Ensembl; ENST00000311550.10; ENSP00000308725.5; ENSG00000166206.15. [P28472-1]
DR Ensembl; ENST00000400188.7; ENSP00000383049.3; ENSG00000166206.15. [P28472-3]
DR Ensembl; ENST00000545868.4; ENSP00000439169.1; ENSG00000166206.15. [P28472-4]
DR Ensembl; ENST00000622697.4; ENSP00000481004.1; ENSG00000166206.15. [P28472-4]
DR Ensembl; ENST00000628124.2; ENSP00000486819.1; ENSG00000166206.15. [P28472-4]
DR Ensembl; ENST00000636466.1; ENSP00000489768.1; ENSG00000166206.15. [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 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; MYWKDTP; -.
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; 11 hits in 1070 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 152 other tissues.
DR ExpressionAtlas; P28472; baseline and differential.
DR Genevisible; P28472; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0005887; C:integral component of plasma membrane; IMP: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:0005231; F:excitatory extracellular ligand-gated ion channel activity; 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:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
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:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IC:ComplexPortal.
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; IPR038050; Neuro_actylchol_rec.
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 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; unknown pathological
FT 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 alpha1beta3gamma2S GABA(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 unknown pathological 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)"
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; unknown pathological
FT 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:4COF"
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:4COF"
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 333..336
FT /evidence="ECO:0007829|PDB:6I53"
FT HELIX 445..470
FT /evidence="ECO:0007829|PDB:6HUJ"
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
