GLRA1_MOUSE
ID GLRA1_MOUSE Reviewed; 457 AA.
AC Q64018; Q5NCT8; Q64019; Q9R0Y6; Q9R0Y7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Glycine receptor subunit alpha-1;
DE AltName: Full=Glycine receptor 48 kDa subunit;
DE AltName: Full=Glycine receptor strychnine-binding subunit;
DE Flags: Precursor;
GN Name=Glra1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), VARIANT SPD SER-80, AND
RP DISEASE.
RX PubMed=7920629; DOI=10.1038/ng0694-131;
RA Ryan S.G., Buckwalter M.S., Lynch J.W., Handford C.A., Segura L.,
RA Shiang R., Wasmuth J.J., Camper S.A., Schofield P., O'Connell P.;
RT "A missense mutation in the gene encoding the alpha 1 subunit of the
RT inhibitory glycine receptor in the spasmodic mouse.";
RL Nat. Genet. 7:131-135(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=BALB/cJ;
RX PubMed=7507926; DOI=10.1016/s0021-9258(17)41987-9;
RA Matzenbach B., Maulet Y., Sefton L., Courtier B., Avner P., Guenet J.-L.,
RA Betz H.;
RT "Structural analysis of mouse glycine receptor alpha subunit genes.
RT Identification and chromosomal localization of a novel variant.";
RL J. Biol. Chem. 269:2607-2612(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP DISEASE.
RX PubMed=7874121; DOI=10.1093/hmg/3.11.2025;
RA Buckwalter M.S., Cook S.A., Davisson M.T., White W.F., Camper S.A.;
RT "A frameshift mutation in the mouse alpha 1 glycine receptor gene (Glra1)
RT results in progressive neurological symptoms and juvenile death.";
RL Hum. Mol. Genet. 3:2025-2030(1994).
RN [5]
RP DISEASE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9145798; DOI=10.1016/s0306-4522(96)00567-2;
RA Kling C., Koch M., Saul B., Becker C.M.;
RT "The frameshift mutation oscillator (Glra1(spd-ot)) produces a complete
RT loss of glycine receptor alpha1-polypeptide in mouse central nervous
RT system.";
RL Neuroscience 78:411-417(1997).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12975813; DOI=10.1002/cne.10852;
RA Haverkamp S., Mueller U., Harvey K., Harvey R.J., Betz H., Waessle H.;
RT "Diversity of glycine receptors in the mouse retina: localization of the
RT alpha3 subunit.";
RL J. Comp. Neurol. 465:524-539(2003).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISEASE.
RX PubMed=16672662; DOI=10.1523/jneurosci.3991-05.2006;
RA Graham B.A., Schofield P.R., Sah P., Margrie T.W., Callister R.J.;
RT "Distinct physiological mechanisms underlie altered glycinergic synaptic
RT transmission in the murine mutants spastic, spasmodic, and oscillator.";
RL J. Neurosci. 26:4880-4890(2006).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF ASP-108.
RX PubMed=17114051; DOI=10.1016/j.neuron.2006.09.035;
RA Hirzel K., Mueller U., Latal A.T., Huelsmann S., Grudzinska J.,
RA Seeliger M.W., Betz H., Laube B.;
RT "Hyperekplexia phenotype of glycine receptor alpha1 subunit mutant mice
RT identifies Zn(2+) as an essential endogenous modulator of glycinergic
RT neurotransmission.";
RL Neuron 52:679-690(2006).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 420-LYS-LYS-421.
RX PubMed=24801766; DOI=10.1038/npp.2014.100;
RA Aguayo L.G., Castro P., Mariqueo T., Munoz B., Xiong W., Zhang L.,
RA Lovinger D.M., Homanics G.E.;
RT "Altered sedative effects of ethanol in mice with alpha1 glycine receptor
RT subunits that are insensitive to Gbetagamma modulation.";
RL Neuropsychopharmacology 39:2538-2548(2014).
CC -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel
CC opening is triggered by extracellular glycine (PubMed:16672662,
CC PubMed:17114051, PubMed:24801766). Channel opening is also triggered by
CC taurine and beta-alanine (By similarity). Channel characteristics
CC depend on the subunit composition; heteropentameric channels are
CC activated by lower glycine levels and display faster desensitization
CC (By similarity). Plays an important role in the down-regulation of
CC neuronal excitability (PubMed:9145798). Contributes to the generation
CC of inhibitory postsynaptic currents (PubMed:16672662, PubMed:17114051,
CC PubMed:24801766). Channel activity is potentiated by ethanol.
CC Potentiation of channel activity by intoxicating levels of ethanol
CC contribute to the sedative effects of ethanol (PubMed:24801766).
CC {ECO:0000250|UniProtKB:P23415, ECO:0000269|PubMed:16672662,
CC ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766,
CC ECO:0000269|PubMed:9145798}.
CC -!- ACTIVITY REGULATION: Inhibited by strychnine. Inhibited by picrotoxin
CC (PubMed:16672662). Channel activity is enhanced by 5 uM Zn(2+) and
CC inhibited by 100 uM Zn(2+) (PubMed:17114051).
CC {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051}.
CC -!- SUBUNIT: Homopentamer (in vitro). Interacts with GLRB to form
CC heteropentameric channels; this is probably the predominant form in
CC vivo. Heteropentamer composed of two GLRA1 and three GLRB.
CC Heteropentamer composed of three GLRA1 and two GLRB. Both homopentamers
CC and heteropentamers form functional ion channels, but their
CC characteristics are subtly different. {ECO:0000250|UniProtKB:P23415}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000305|PubMed:12975813, ECO:0000305|PubMed:17114051,
CC ECO:0000305|PubMed:24801766}; Multi-pass membrane protein
CC {ECO:0000305}. Synapse {ECO:0000269|PubMed:12975813,
CC ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766}. Perikaryon
CC {ECO:0000269|PubMed:24801766}. Cell projection, dendrite
CC {ECO:0000269|PubMed:24801766}. Cell membrane
CC {ECO:0000269|PubMed:16672662, ECO:0000305|PubMed:9145798}; Multi-pass
CC membrane protein {ECO:0000250|UniProtKB:P23415, ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=Long;
CC IsoId=Q64018-1; Sequence=Displayed;
CC Name=b; Synonyms=Short;
CC IsoId=Q64018-2; Sequence=VSP_000080;
CC -!- TISSUE SPECIFICITY: Detected in spinal cord neurons (PubMed:9145798,
CC PubMed:17114051, PubMed:24801766). Detected in brain stem neurons
CC (PubMed:16672662, PubMed:24801766). Detected at lower levels in
CC hippocampus and cerebellum (PubMed:24801766). Detected in the inner
CC plexiform layer of the retina (at protein level) (PubMed:12975813).
CC {ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:16672662,
CC ECO:0000269|PubMed:17114051, ECO:0000269|PubMed:24801766,
CC ECO:0000269|PubMed:9145798}.
CC -!- DOMAIN: The channel pore is formed by pentameric assembly of the second
CC transmembrane domain from all five subunits. Channel opening is
CC effected by an outward rotation of the transmembrane domains that
CC increases the diameter of the pore. {ECO:0000250|UniProtKB:O93430}.
CC -!- DISEASE: Note=Defects in Glra1 are the cause of the spasmodic (spd)
CC phenotype, a mouse mutant which resembles the human neurological
CC disease, hyperekplexia (or startle disease (STHE)) (PubMed:7920629).
CC Defects in Glra1 are the cause of the lethal oscillator (spd-ot)
CC phenotype. Mutant mice display a fine motor tremor and muscle spasms
CC that begin at 2 weeks of age and progressively worsen, resulting in
CC death by 3 weeks of age (PubMed:7874121). Heterozygous mice show an
CC increased acoustic startle response (PubMed:9145798). Neurons from
CC homozygous oscillator mice have dramatically reduced amplitude and
CC frequency of glycinergic inhibitory postsynaptic currents
CC (PubMed:16672662). The oscillator phenotype is due to the complete
CC absence of Glra1 protein (PubMed:9145798).
CC {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7874121,
CC ECO:0000269|PubMed:7920629, ECO:0000269|PubMed:9145798}.
CC -!- MISCELLANEOUS: The alpha subunit binds strychnine.
CC {ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7874121,
CC ECO:0000269|PubMed:9145798}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glycine receptor (TC 1.A.9.3) subfamily. GLRA1 sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; S73717; AAB32157.2; -; mRNA.
DR EMBL; S73718; AAB32158.2; -; mRNA.
DR EMBL; X75832; CAB52398.1; -; Genomic_DNA.
DR EMBL; X75833; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75834; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75835; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75836; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75837; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75838; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75839; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75840; CAB52398.1; JOINED; Genomic_DNA.
DR EMBL; X75832; CAB52399.1; -; Genomic_DNA.
DR EMBL; X75833; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75834; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75835; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75836; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75837; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75838; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75839; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; X75840; CAB52399.1; JOINED; Genomic_DNA.
DR EMBL; AL596207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24715.1; -. [Q64018-2]
DR CCDS; CCDS70190.1; -. [Q64018-1]
DR PIR; C49970; C49970.
DR RefSeq; NP_001277750.1; NM_001290821.1. [Q64018-1]
DR AlphaFoldDB; Q64018; -.
DR SMR; Q64018; -.
DR BioGRID; 199951; 1.
DR STRING; 10090.ENSMUSP00000099777; -.
DR BindingDB; Q64018; -.
DR ChEMBL; CHEMBL4295860; -.
DR GlyGen; Q64018; 1 site.
DR iPTMnet; Q64018; -.
DR PhosphoSitePlus; Q64018; -.
DR SwissPalm; Q64018; -.
DR MaxQB; Q64018; -.
DR PaxDb; Q64018; -.
DR PRIDE; Q64018; -.
DR ProteomicsDB; 266816; -. [Q64018-1]
DR ProteomicsDB; 266817; -. [Q64018-2]
DR Antibodypedia; 3089; 418 antibodies from 36 providers.
DR DNASU; 14654; -.
DR Ensembl; ENSMUST00000075603; ENSMUSP00000075032; ENSMUSG00000000263. [Q64018-1]
DR Ensembl; ENSMUST00000102716; ENSMUSP00000099777; ENSMUSG00000000263. [Q64018-2]
DR GeneID; 14654; -.
DR KEGG; mmu:14654; -.
DR UCSC; uc007izo.2; mouse. [Q64018-1]
DR CTD; 2741; -.
DR MGI; MGI:95747; Glra1.
DR VEuPathDB; HostDB:ENSMUSG00000000263; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000159047; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; Q64018; -.
DR OMA; FNFAYGM; -.
DR PhylomeDB; Q64018; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-112314; Neurotransmitter receptors and postsynaptic signal transmission.
DR BioGRID-ORCS; 14654; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Glra1; mouse.
DR PRO; PR:Q64018; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q64018; protein.
DR Bgee; ENSMUSG00000000263; Expressed in medial vestibular nucleus and 48 other tissues.
DR ExpressionAtlas; Q64018; baseline and differential.
DR Genevisible; Q64018; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; ISO:MGI.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0098690; C:glycinergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
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; IDA:MGI.
DR GO; GO:0016933; F:extracellularly glycine-gated ion channel activity; ISO:MGI.
DR GO; GO:0016594; F:glycine binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030977; F:taurine binding; ISS:UniProtKB.
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; IDA:SynGO.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR GO; GO:0006820; P:anion transport; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0071361; P:cellular response to ethanol; ISS:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR GO; GO:0019228; P:neuronal action potential; IMP:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IMP:MGI.
DR GO; GO:0097305; P:response to alcohol; IMP:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0060013; P:righting reflex; IMP:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001964; P:startle response; IMP:MGI.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR008127; Glycine_rcpt_A.
DR InterPro; IPR008128; Glycine_rcpt_A1.
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; PR00253; GABAARECEPTR.
DR PRINTS; PR01673; GLYRALPHA.
DR PRINTS; PR01674; GLYRALPHA1.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Chloride;
KW Chloride channel; Disease variant; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Metal-binding; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000250|UniProtKB:P07727"
FT CHAIN 29..457
FT /note="Glycine receptor subunit alpha-1"
FT /id="PRO_0000000413"
FT TOPO_DOM 29..250
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 251..272
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 273..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 278..298
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 299..309
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 310..330
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 331..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 426..446
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 447..457
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 230..235
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT SITE 289
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 166..180
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT DISULFID 226..237
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT VAR_SEQ 354..361
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:7920629"
FT /id="VSP_000080"
FT VARIANT 80
FT /note="A -> S (in spd)"
FT /evidence="ECO:0000269|PubMed:7920629"
FT MUTAGEN 108
FT /note="D->A: Eliminates potentiation of glycine-mediated
FT currents by Zn(2+) and causes neuromotor defects similar to
FT human startle disease."
FT /evidence="ECO:0000269|PubMed:17114051"
FT MUTAGEN 421..422
FT /note="KK->AA: Reduces the increase of channel activity in
FT response to ethanol and improves tolerance of intoxicating
FT levels of alcohol."
FT /evidence="ECO:0000269|PubMed:24801766"
FT CONFLICT 84
FT /note="M -> I (in Ref. 2; CAB52398/CAB52399)"
FT /evidence="ECO:0000305"
FT CONFLICT 426..429
FT /note="ISRI -> NISH (in Ref. 2; CAB52398/CAB52399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 52657 MW; 29268DC4991A6E20 CRC64;
MYSFNTLRFY LWETIVFFSL AASKEAEAAR SAPKPMSPSD FLDKLMGRTS GYDARIRPNF
KGPPVNVSCN IFINSFGSIA ETTMDYRVNI FLRQQWNDPR LAYNEYPDDS LDLDPSMLDS
IWKPDLFFAN EKGAHFHEIT TDNKLLRISR NGNVLYSIRI TLTLACPMDL KNFPMDVQTC
IMQLESFGYT MNDLIFEWQE QGAVQVADGL TLPQFILKEE KDLRYCTKHY NTGKFTCIEA
RFHLERQMGY YLIQMYIPSL LIVILSWISF WINMDAAPAR VGLGITTVLT MTTQSSGSRA
SLPKVSYVKA IDIWMAVCLL FVFSALLEYA AVNFVSRQHK ELLRFRRKRR HHKSPMLNLF
QDDEGGEGRF NFSAYGMGPA CLQAKDGISV KGANNNNTTN PPPAPSKSPE EMRKLFIQRA
KKIDKISRIG FPMAFLIFNM FYWIIYKIVR REDVHNK
