GLRB_HUMAN
ID GLRB_HUMAN Reviewed; 497 AA.
AC P48167; A8K3K2; D3DP23; F5GWE1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Glycine receptor subunit beta;
DE AltName: Full=Glycine receptor 58 kDa subunit;
DE Flags: Precursor;
GN Name=GLRB;
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), FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND INTERACTION WITH GLRA1.
RC TISSUE=Hippocampus;
RX PubMed=8717357; DOI=10.1016/0169-328x(95)00215-e;
RA Handford C.A., Lynch J.W., Baker E., Webb G.C., Ford J.H., Sutherland G.R.,
RA Schofield P.R.;
RT "The human glycine receptor beta subunit: primary structure, functional
RT characterisation and chromosomal localisation of the human and murine
RT genes.";
RL Brain Res. Mol. Brain Res. 35:211-219(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9676428; DOI=10.1006/geno.1998.5324;
RA Milani N., Muelhardt C., Weber R.G., Lichter P., Kioschis P., Poustka A.,
RA Becker C.-M.;
RT "The human glycine receptor beta subunit gene (GLRB): structure, refined
RT chromosomal localization, and population polymorphism.";
RL Genomics 50:341-345(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15028279; DOI=10.1016/j.ygeno.2003.09.023;
RA Jin P., Fu G.K., Wilson A.D., Yang J., Chien D., Hawkins P.R., Au-Young J.,
RA Stuve L.L.;
RT "PCR isolation and cloning of novel splice variant mRNAs from known drug
RT target genes.";
RL Genomics 83:566-571(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
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 [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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP INTERACTION WITH GLRA1.
RX PubMed=14551753; DOI=10.1007/s00249-003-0286-y;
RA Mohammadi B., Krampfl K., Cetinkaya C., Moschref H., Grosskreutz J.,
RA Dengler R., Bufler J.;
RT "Kinetic analysis of recombinant mammalian alpha(1) and alpha(1)beta
RT glycine receptor channels.";
RL Eur. Biophys. J. 32:529-536(2003).
RN [9]
RP INTERACTION WITH GPHN, AND SUBCELLULAR LOCATION.
RX PubMed=12684523; DOI=10.1074/jbc.m301070200;
RA Rees M.I., Harvey K., Ward H., White J.H., Evans L., Duguid I.C.,
RA Hsu C.-C., Coleman S.L., Miller J., Baer K., Waldvogel H.J., Gibbon F.,
RA Smart T.G., Owen M.J., Harvey R.J., Snell R.G.;
RT "Isoform heterogeneity of the human gephyrin gene (GPHN), binding domains
RT to the glycine receptor, and mutation analysis in hyperekplexia.";
RL J. Biol. Chem. 278:24688-24696(2003).
RN [10]
RP FUNCTION, INTERACTION WITH GLRA2, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=15302677; DOI=10.1038/sj.bjp.0705875;
RA Miller P.S., Harvey R.J., Smart T.G.;
RT "Differential agonist sensitivity of glycine receptor alpha2 subunit splice
RT variants.";
RL Br. J. Pharmacol. 143:19-26(2004).
RN [11]
RP FUNCTION, INTERACTION WITH GLRA2, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16144831; DOI=10.1074/jbc.m508303200;
RA Miller P.S., Da Silva H.M., Smart T.G.;
RT "Molecular basis for zinc potentiation at strychnine-sensitive glycine
RT receptors.";
RL J. Biol. Chem. 280:37877-37884(2005).
RN [12]
RP SUBUNIT STOICHIOMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22715885; DOI=10.1021/bi300063m;
RA Yang Z., Taran E., Webb T.I., Lynch J.W.;
RT "Stoichiometry and subunit arrangement of alpha1beta glycine receptors as
RT determined by atomic force microscopy.";
RL Biochemistry 51:5229-5231(2012).
RN [13]
RP SUBUNIT STOICHIOMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=22973015; DOI=10.1523/jneurosci.2050-12.2012;
RA Durisic N., Godin A.G., Wever C.M., Heyes C.D., Lakadamyali M., Dent J.A.;
RT "Stoichiometry of the human glycine receptor revealed by direct subunit
RT counting.";
RL J. Neurosci. 32:12915-12920(2012).
RN [14]
RP INTERACTION WITH GPHN.
RX PubMed=26613940; DOI=10.15252/emmm.201505323;
RG EuroEPINOMICS Dravet working group;
RA Dejanovic B., Djemie T., Gruenewald N., Suls A., Kress V., Hetsch F.,
RA Craiu D., Zemel M., Gormley P., Lal D., Myers C.T., Mefford H.C.,
RA Palotie A., Helbig I., Meier J.C., De Jonghe P., Weckhuysen S., Schwarz G.;
RT "Simultaneous impairment of neuronal and metabolic function of mutated
RT gephyrin in a patient with epileptic encephalopathy.";
RL EMBO Mol. Med. 7:1580-1594(2015).
RN [15]
RP FUNCTION, INTERACTION WITH GLRA1; GLRA2 AND GLRA3, SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25445488; DOI=10.1016/j.neuropharm.2014.10.026;
RA Zhang Y., Dixon C.L., Keramidas A., Lynch J.W.;
RT "Functional reconstitution of glycinergic synapses incorporating defined
RT glycine receptor subunit combinations.";
RL Neuropharmacology 89:391-397(2015).
RN [16]
RP VARIANT HKPX2 ASP-251, CHARACTERIZATION OF VARIANT HKPX2 ASP-251, FUNCTION,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GLRA1.
RX PubMed=11929858; DOI=10.1093/hmg/11.7.853;
RA Rees M.I., Lewis T.M., Kwok J.B.J., Mortier G.R., Govaert P., Snell R.G.,
RA Schofield P.R., Owen M.J.;
RT "Hyperekplexia associated with compound heterozygote mutations in the beta-
RT subunit of the human inhibitory glycine receptor (GLRB).";
RL Hum. Mol. Genet. 11:853-860(2002).
RN [17]
RP VARIANT HKPX2 ARG-199.
RX PubMed=21391991; DOI=10.1111/j.1399-0004.2011.01661.x;
RA Al-Owain M., Colak D., Al-Bakheet A., Al-Hashmi N., Shuaib T.,
RA Al-Hemidan A., Aldhalaan H., Rahbeeni Z., Al-Sayed M., Al-Younes B.,
RA Ozand P.T., Kaya N.;
RT "Novel mutation in GLRB in a large family with hereditary hyperekplexia.";
RL Clin. Genet. 81:479-484(2012).
RN [18]
RP VARIANTS HKPX2 ARG-199; ARG-307 AND CYS-332, CHARACTERIZATION OF VARIANTS
RP HKPX2 ARG-199; ARG-307 AND CYS-332, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH GLRA1.
RX PubMed=23238346; DOI=10.1016/j.nbd.2012.12.001;
RA James V.M., Bode A., Chung S.K., Gill J.L., Nielsen M., Cowan F.M.,
RA Vujic M., Thomas R.H., Rees M.I., Harvey K., Keramidas A., Topf M.,
RA Ginjaar I., Lynch J.W., Harvey R.J.;
RT "Novel missense mutations in the glycine receptor beta subunit gene (GLRB)
RT in startle disease.";
RL Neurobiol. Dis. 52:137-149(2013).
CC -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. GLRB
CC does not form ligand-gated ion channels by itself, but is part of
CC heteromeric ligand-gated chloride channels. Channel opening is
CC triggered by extracellular glycine (PubMed:8717357, PubMed:15302677,
CC PubMed:16144831, PubMed:22715885, PubMed:25445488, PubMed:11929858,
CC PubMed:23238346). Heteropentameric channels composed of GLRB and GLRA1
CC are activated by lower glycine levels than homopentameric GLRA1
CC (PubMed:8717357). Plays an important role in the down-regulation of
CC neuronal excitability (PubMed:11929858, PubMed:23238346). Contributes
CC to the generation of inhibitory postsynaptic currents
CC (PubMed:25445488). {ECO:0000269|PubMed:11929858,
CC ECO:0000269|PubMed:15302677, ECO:0000269|PubMed:16144831,
CC ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:23238346,
CC ECO:0000269|PubMed:25445488, ECO:0000269|PubMed:8717357}.
CC -!- SUBUNIT: Heteropentamer composed of GLRB and GLRA1 (PubMed:8717357,
CC PubMed:14551753, PubMed:22973015, PubMed:22715885, PubMed:25445488,
CC PubMed:11929858, PubMed:23238346). Heteropentamer composed of GLRB and
CC GLRA2 (PubMed:15302677, PubMed:16144831, PubMed:25445488).
CC Heteropentamer composed of GLRB and GLRA3 (PubMed:25445488).
CC Heteropentamer composed of two GLRA1 and three GLRB subunits
CC (PubMed:22715885). Heteropentamer composed of three GLRA1 and two GLRB
CC subunits (PubMed:22973015). Interacts with GPHN
CC (PubMed:12684523,PubMed:26613940). {ECO:0000269|PubMed:11929858,
CC ECO:0000269|PubMed:12684523, ECO:0000269|PubMed:14551753,
CC ECO:0000269|PubMed:15302677, ECO:0000269|PubMed:16144831,
CC ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:22973015,
CC ECO:0000269|PubMed:23238346, ECO:0000269|PubMed:25445488,
CC ECO:0000269|PubMed:26613940, ECO:0000269|PubMed:8717357}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P48168}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000250|UniProtKB:P48168}.
CC Cell projection, dendrite {ECO:0000250|UniProtKB:P48168}. Cell membrane
CC {ECO:0000269|PubMed:11929858, ECO:0000269|PubMed:12684523,
CC ECO:0000269|PubMed:15302677, ECO:0000269|PubMed:16144831,
CC ECO:0000269|PubMed:22715885, ECO:0000269|PubMed:22973015,
CC ECO:0000269|PubMed:23238346, ECO:0000269|PubMed:25445488,
CC ECO:0000269|PubMed:8717357}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415}. Cytoplasm
CC {ECO:0000269|PubMed:12684523}. Note=Retained in the cytoplasm upon
CC heterologous expression by itself. Coexpression with GPHN promotes
CC expression at the cell membrane (PubMed:12684523). Coexpression with
CC GLRA1, GLRA2 or GLRA3 promotes expression at the cell membrane.
CC {ECO:0000250|UniProtKB:P20781, ECO:0000269|PubMed:12684523}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48167-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48167-2; Sequence=VSP_045466, VSP_045467;
CC -!- DISEASE: Hyperekplexia 2 (HKPX2) [MIM:614619]: A neurologic disorder
CC characterized by muscular rigidity of central nervous system origin,
CC particularly in the neonatal period, and by an exaggerated startle
CC response to unexpected acoustic or tactile stimuli.
CC {ECO:0000269|PubMed:11929858, ECO:0000269|PubMed:21391991,
CC ECO:0000269|PubMed:23238346}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glycine receptor (TC 1.A.9.3) subfamily. GLRB sub-subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U33267; AAB37750.1; -; mRNA.
DR EMBL; AF094754; AAC71033.1; -; mRNA.
DR EMBL; AF094755; AAC71034.1; -; mRNA.
DR EMBL; CD013911; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK290617; BAF83306.1; -; mRNA.
DR EMBL; AC079403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471056; EAX04872.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04873.1; -; Genomic_DNA.
DR EMBL; BC032635; AAH32635.1; -; mRNA.
DR CCDS; CCDS3796.1; -. [P48167-1]
DR CCDS; CCDS54813.1; -. [P48167-2]
DR PIR; G02031; G02031.
DR RefSeq; NP_000815.1; NM_000824.4. [P48167-1]
DR RefSeq; NP_001159532.1; NM_001166060.1. [P48167-1]
DR RefSeq; NP_001159533.1; NM_001166061.1. [P48167-2]
DR RefSeq; XP_016863524.1; XM_017008035.1. [P48167-2]
DR PDB; 5BKF; EM; 3.60 A; E=25-355, E=400-497.
DR PDB; 5BKG; EM; 3.80 A; E=25-355, E=400-497.
DR PDB; 7KUY; EM; 3.60 A; E=25-355, E=400-497.
DR PDB; 7L31; EM; 3.80 A; E=25-353, E=400-497.
DR PDBsum; 5BKF; -.
DR PDBsum; 5BKG; -.
DR PDBsum; 7KUY; -.
DR PDBsum; 7L31; -.
DR AlphaFoldDB; P48167; -.
DR SMR; P48167; -.
DR BioGRID; 109005; 40.
DR CORUM; P48167; -.
DR IntAct; P48167; 13.
DR MINT; P48167; -.
DR STRING; 9606.ENSP00000264428; -.
DR BindingDB; P48167; -.
DR ChEMBL; CHEMBL2363052; -.
DR ChEMBL; CHEMBL4106144; -.
DR ChEMBL; CHEMBL4296075; -.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB00145; Glycine.
DR DrugBank; DB00431; Lindane.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB01043; Memantine.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB05885; Seletracetam.
DR DrugCentral; P48167; -.
DR GuidetoPHARMACOLOGY; 427; -.
DR TCDB; 1.A.9.3.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; P48167; 2 sites.
DR iPTMnet; P48167; -.
DR PhosphoSitePlus; P48167; -.
DR BioMuta; GLRB; -.
DR DMDM; 1346173; -.
DR MassIVE; P48167; -.
DR PaxDb; P48167; -.
DR PeptideAtlas; P48167; -.
DR PRIDE; P48167; -.
DR ProteomicsDB; 24087; -.
DR ProteomicsDB; 55869; -. [P48167-1]
DR Antibodypedia; 66124; 184 antibodies from 28 providers.
DR DNASU; 2743; -.
DR Ensembl; ENST00000264428.9; ENSP00000264428.4; ENSG00000109738.11. [P48167-1]
DR Ensembl; ENST00000509282.1; ENSP00000427186.1; ENSG00000109738.11. [P48167-1]
DR Ensembl; ENST00000541722.5; ENSP00000441873.1; ENSG00000109738.11. [P48167-2]
DR GeneID; 2743; -.
DR KEGG; hsa:2743; -.
DR MANE-Select; ENST00000264428.9; ENSP00000264428.4; NM_000824.5; NP_000815.1.
DR UCSC; uc003ipj.3; human. [P48167-1]
DR CTD; 2743; -.
DR DisGeNET; 2743; -.
DR GeneCards; GLRB; -.
DR GeneReviews; GLRB; -.
DR HGNC; HGNC:4329; GLRB.
DR HPA; ENSG00000109738; Tissue enhanced (brain, parathyroid gland).
DR MalaCards; GLRB; -.
DR MIM; 138492; gene.
DR MIM; 614619; phenotype.
DR neXtProt; NX_P48167; -.
DR OpenTargets; ENSG00000109738; -.
DR Orphanet; 3197; Hereditary hyperekplexia.
DR PharmGKB; PA28730; -.
DR VEuPathDB; HostDB:ENSG00000109738; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000156344; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P48167; -.
DR OMA; KFFWGIL; -.
DR OrthoDB; 614790at2759; -.
DR PhylomeDB; P48167; -.
DR TreeFam; TF315453; -.
DR PathwayCommons; P48167; -.
DR Reactome; R-HSA-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR SignaLink; P48167; -.
DR SIGNOR; P48167; -.
DR BioGRID-ORCS; 2743; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; GLRB; human.
DR GeneWiki; GLRB; -.
DR GenomeRNAi; 2743; -.
DR Pharos; P48167; Tclin.
DR PRO; PR:P48167; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P48167; protein.
DR Bgee; ENSG00000109738; Expressed in frontal pole and 161 other tissues.
DR ExpressionAtlas; P48167; baseline and differential.
DR Genevisible; P48167; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0016935; C:glycine-gated chloride channel complex; IDA:UniProtKB.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
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:0016934; F:extracellularly glycine-gated chloride channel activity; IEA:Ensembl.
DR GO; GO:0016933; F:extracellularly glycine-gated ion channel activity; IMP:UniProtKB.
DR GO; GO:0016594; F:glycine binding; IEA:Ensembl.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007340; P:acrosome reaction; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
DR GO; GO:0097112; P:gamma-aminobutyric acid receptor clustering; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001964; P:startle response; IMP:UniProtKB.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR008060; Glycine_rcpt_B.
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 PANTHER; PTHR18945:SF29; PTHR18945:SF29; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01677; GLYRBETA.
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; Cell projection;
KW Chloride; Chloride channel; Cytoplasm; Disease variant; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..497
FT /note="Glycine receptor subunit beta"
FT /id="PRO_0000000423"
FT TOPO_DOM 23..268
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 269..290
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 291..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 296..316
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 317..327
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 328..348
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TOPO_DOM 349..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT TRANSMEM 476..496
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 247..253
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT SITE 307
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT MOD_RES 391
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P20781"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 183..197
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT DISULFID 243..255
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT VAR_SEQ 303
FT /note="I -> W (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15028279"
FT /id="VSP_045466"
FT VAR_SEQ 304..497
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15028279"
FT /id="VSP_045467"
FT VARIANT 199
FT /note="M -> R (in HKPX2; heteropentameric channel complexes
FT with GLRA1 require much higher glycine levels for channel
FT activation; no effect on expression at the cell membrane;
FT dbSNP:rs398122856)"
FT /evidence="ECO:0000269|PubMed:21391991,
FT ECO:0000269|PubMed:23238346"
FT /id="VAR_068246"
FT VARIANT 251
FT /note="G -> D (in HKPX2; heteropentameric channel complexes
FT with GLRA1 require much higher glycine levels for channel
FT activation; dbSNP:rs121909749)"
FT /evidence="ECO:0000269|PubMed:11929858"
FT /id="VAR_035070"
FT VARIANT 307
FT /note="L -> R (in HKPX2; heteropentameric channel complexes
FT with GLRA1 have reduced expression at the cell membrane and
FT display spontaneous channel opening in the absence of
FT extracellular glycine)"
FT /evidence="ECO:0000269|PubMed:23238346"
FT /id="VAR_075502"
FT VARIANT 332
FT /note="W -> C (in HKPX2; heteropentameric channel complexes
FT with GLRA1 have reduced expression at the cell membrane and
FT reduced channel activity)"
FT /evidence="ECO:0000269|PubMed:23238346"
FT /id="VAR_075503"
SQ SEQUENCE 497 AA; 56122 MW; C1F0B407601D3625 CRC64;
MKFLLTTAFL ILISLWVEEA YSKEKSSKKG KGKKKQYLCP SQQSAEDLAR VPANSTSNIL
NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD YRVNIFLRQK WNDPRLKLPS
DFRGSDALTV DPTMYKCLWK PDLFFANEKS ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT
LSCPLDLTLF PMDTQRCKMQ LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY
GNCTKYYKGT GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP
LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV QVMLNNPKRV
EAEKARIAKA EQADGKGGNV AKKNTVNGTG TPVHISTLQV GETRCKKVCT SKSDLRSNDF
SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK SQAKNNKKPP PAKPVIPTAA KRIDLYARAL
FPFCFLFFNV IYWSIYL
