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0GLRA1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameGLRA1
DescriptionGlycine receptor alpha-1 chain precursor (glycine receptor 48 kda subunit) (strychnine binding subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005887 integral to plasma membrane (TAS)
0004891 glycine-inhibited chloride channel activity (TAS)
0007166 cell surface receptor linked signal transdu... (TAS)
0007399 neurogenesis (TAS)
0007268 synaptic transmission (TAS)
0006810 transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands.llowing rapid transmission of signals at chemical synapses .Of the five families known.our have been shown to form a sequence-related superfamily. These are the gamma-aminobutyric acid type A (GABA-A).icotinic acetylcholine.lycine and the serotonin 5HT3 receptors. The ionotropic glutamate receptors () have a distinct primary structure.However.ll these receptors possess a pentameric structure (made up of varying subunits).urrounding a central pore. Each of these subunits contains a large extracellular N-terminal ligand-binding region; 3 hydrophobic transmembrane domains; a large intracellular region; and a fourth hydrophobic domain .This domain represents four transmembrane helices of a variety of neurotransmitter-gated ion-channels.
  IPR006029:Neurotransmitter-gated ion-channel transmembrane region
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands.llowing rapid transmission of signals at chemical synapses .Of the five families known.our have been shown to form a sequence-related superfamily. These are the gamma-aminobutyric acid type A (GABA-A).icotinic acetylcholine.lycine and the serotonin 5HT3 receptors. The ionotropic glutamate receptors () have a distinct primary structure.However.ll these receptors possess a pentameric structure (made up of varying subunits).urrounding a central pore. Each of these subunits contains a large extracellular N-terminal ligand-binding region; 3 hydrophobic transmembrane domains; a large intracellular region; and a fourth hydrophobic domain .This InterPro entry represents the GABA-A.icotinic.lycine.nd 5HT3 receptors.
  IPR006201:Neurotransmitter-gated ion-channel
InterPro domains unassigned to SynO:
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands.llowing rapid transmission of signals at chemical synapses .Of the five families known.our have been shown to form a sequence-related superfamily. These are the gamma-aminobutyric acid type A (GABA-A).icotinic acetylcholine.lycine and the serotonin 5HT3 receptors. The ionotropic glutamate receptors () have a distinct primary structure.However.ll these receptors possess a pentameric structure (made up of varying subunits).urrounding a central pore. Each of these subunits contains a large extracellular N-terminal ligand-binding region; 3 hydrophobic transmembrane domains; a large intracellular region; and a fourth hydrophobic domain . Gamma-aminobutyric acid type A (GABAA) receptors are members of the neurotransmitter ligand-gated ion channels: they mediate neuronal inhibition on binding GABA. The effects of GABA on GABAA receptors are modulated by a range of therapeutically important drugs.ncluding barbiturates.naesthetics and benzodiazepines (BZs) . The BZs are a diverse range of compounds.ncluding widely prescribed drugs.uch as librium and valium.nd their interaction with GABAA receptors provides the most potent pharmacological means of distinguishing different GABAA receptor subtypes. GABAA receptors are pentameric membrane proteins that operate GABA-gated chloride channels . Eight types of receptor subunit have been cloned.ith multiple subtypes within some classes: alpha 1-6.eta 1-4.amma 1-4.elta.psilon.i.ho 1-3 and theta . Subunits are typically 50-60kDa in size and comprise a long N-terminal extracellular domain.ontaining a putative signal peptide and a disulphide-bonded beta structural loop; 4 putative transmembrane (TM) domains; and a large cytoplasmic loop connecting the third and fourth TM domains. Amongst family members.he large cytoplasmic loop displays the most divergence in terms of primary structure.he TM domains showing the highest level of sequence conservation .
  IPR006028:Gamma-aminobutyric acid A receptor
Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands.llowing rapid transmission of signals at chemical synapses .Of the five families known.our have been shown to form a sequence-related superfamily. These are the gamma-aminobutyric acid type A (GABA-A).icotinic acetylcholine.lycine and the serotonin 5HT3 receptors. The ionotropic glutamate receptors () have a distinct primary structure.However.ll these receptors possess a pentameric structure (made up of varying subunits).urrounding a central pore. Each of these subunits contains a large extracellular N-terminal ligand-binding region; 3 hydrophobic transmembrane domains; a large intracellular region; and a fourth hydrophobic domain .This entry presents the extracellular ligand binding domain of these ion channels. This domain forms a pentameric arrangement in the known structure.
  IPR006202:Neurotransmitter-gated ion-channel ligand-binding
Glycine is a major inhibitory neurotransmitter (NT) in the adult vertebratecentral nervous system (CNS). Glycinergic synapses have a well-establishedrole in the processing of motor and sensory information that controlsmovement.ision and audition . This action of glycine is mediatedthrough its interaction with the glycine receptor (GlyR): an intrinsicchloride channel is opened in response to agonist binding. The subsequentinflux of anions prevents membrane depolarisation and neuronal firinginduced by excitatory NTs. Strychnine acts as a competitive antagonist ofglycine binding.hereby reducing the activity of inhibitory neurones.Poisoning with strychnine is characterised by over-excitation.uscle spasmsand convulsions. Whilst glycine is the principal physiological agonist atGlyRs.aurine and beta-alanine also behave as agonists . Compounds thatmodulate GlyR activity include zinc.ome alcohols and anaesthetics.icrotoxin.ocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord.ut havesince been found to be expressed more widely.ncluding the cochlear nuclei.erebellar cortex and forebrain .GlyRs belong to the ligand-gated ion channel family.hich also includes theinhibitory gamma-aminobutyric acid type A (GABAA) and excitatory nicotinicacetylcholine (nACh) and serotonin type 3 (5-HT3) receptors .Affinity-purified GlyR was found to contain two glycosylated membraneproteins of 48kDa and 56kDa.orresponding to alpha and beta subunits.espectively. Four genes encoding alpha subunits have been identified (GLRA1to 4).ogether with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing.ieldingtwo isoforms of GLRA1 to 3 . The characteristics of different GlyRsubtypes.herefore.an be largely explained by their GLRA content.GlyRs are generally believed to adopt a pentameric structure in vivo: fivesubunits assemble to form a ring structure with a central pore. Typically.stoichiometry of 3:2 (alpha:beta) is observed . GlyR subunits share ahigh overall level of sequence similarity both with themselves and with thesubunits of the GABAA and nACh receptors. Four highly conserved segmentshave been proposed to correspond to transmembrane (TM) alpha helices (TM1-4).he second of which is thought to contribute to the pore wall . A long extracellular N-terminal segment precedes TM1 and a long cytoplasmic loop links TM3 and 4. Short cytoplasmic and extracellular loops join TM1-2 andTM2-3.espectively.nd a short C-terminal sequence follows TM4. Studiesusing radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding.he critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structuralrole.ontributing one of its TM domains to the pore wall as well as playinga putative role in postsynaptic clustering of the receptor.In several mammalian species.efects in glycinergic transmission areassociated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia.r startle disease . This ischaracterised by muscular spasms in response to unexpected light or noisestimuli.imilar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4loops.uggesting that these regions are involved in the transduction ofligand binding into channel activation.In humans.he alpha 1 gene is located on chromosome 5p32 . In situhybridisation studies have shown GLRA1 to be expressed in the spinal cord.rain stem and colliculi. GLRA1 trancripts.ogether with GLRA3.redominatein the postnatal CNS.eplacing GLRA2.hich is more abundant in embryonicand neonatal neurones.
  IPR008128:Glycine receptor alpha1
IPR006202:Neur_chan_LBD 
Evalue:-81.6777801513672 
Location:38-248IPR006029:Neur_chan_memb 
Evalue:-54.4202156066895 
Location:255-435IPR008128:GLYRALPHA1 
Evalue:0 
Location:20-33IPR008128:GLYRALPHA1 
Evalue:0 
Location:7-19
SequencesProtein: GLRA1_HUMAN (449 aa)
mRNA: NM_000171
Local Annotation
Synapse Ontology
Postsynaptic compartment is represented by a patch of plasma membrane containing a packed array of neurotransmitter receptors and by an underlying dense matrix, the postsynaptic density (PSD).
sdb:0005 Postsynaptic compartment  (Evidence:keywords,domains)
this kind of receptor usually locates at the postsynaptic plasma membranous region.
sdb:0109 ionotropic receptor  (Evidence:keywords,domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence:keywords,domains)
?
sdb:0297 NMDA receptor  (Evidence:keywords,domains)
?
sdb:0305 binding to postsynaptic receptor and internization  (Evidence:keywords,domains)
?
sdb:0328 transmitters release and endocytosis  (Evidence:keywords,domains)
?
sdb:0334 inhibitory postsynapstic component  (Evidence:keywords,domains)
KO assignmentK05193
  Level 3 annotation:
    glycine receptor, alpha 1
  Level 2 annotation:
    Neuroactive ligand-receptor interaction
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 120 residues, 151182360-151182717Exon2: 51 residues, 151188674-151188821Exon3: 73 residues, 151211143-151211358Exon4: 48 residues, 151214793-151214931Exon5: 29 residues, 151216054-151216137Exon6: 76 residues, 151219538-151219762Exon7: 24 residues, 151246474-151246542Exon8: 44 residues, 151252064-151252192Exon9: 118 residues, 151284247-151284596Exon10: 2 residues, -Jump to GLRA1_HUMAN  
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Loci Cluster (Details)Loci: 4747 151182360-151284596 ~-102K 29808(GLRA1)(-)Loci: 4746 150863846-150928698 ~-65K 29803(FAT2)(-)Link out to UCSC