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Search results 101 to 200 out of 211 for Glra1

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Type Details Score
Publication
3429842 | J:9027
First Author: Lane PW
Year: 1987
Journal: J Hered
Title: Spasmodic, a mutation on chromosome 11 in the mouse.
Volume: 78
Issue: 6
Pages: 353-6
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Publication
- | J:78134
     
First Author: JAX Neuroscience Mutagenesis Facility
Year: 2002
Journal: MGI Direct Data Submission
Title: Heritable mouse mutants from JAX NMF ENU Mutagenesis Program
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Publication
9051263 | J:38407
First Author: Heck S
Year: 1997
Journal: Brain Res Dev Brain Res
Title: Expression and mRNA splicing of glycine receptor subunits and gephyrin during neuronal differentiation of P19 cells in vitro, studied by RT-PCR and immunocytochemistry.
Volume: 98
Issue: 2
Pages: 211-20
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Publication
18721822 | J:147002
First Author: Lynch JW
Year: 2009
Journal: Neuropharmacology
Title: Native glycine receptor subtypes and their physiological roles.
Volume: 56
Issue: 1
Pages: 303-9
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Publication
21486797 | J:185249
First Author: Mordel J
Year: 2011
Journal: J Physiol
Title: Activation of glycine receptor phase-shifts the circadian rhythm in neuronal activity in the mouse suprachiasmatic nucleus.
Volume: 589
Issue: Pt 9
Pages: 2287-300
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Publication
- | J:44385
First Author: Becker CM
Year: 1997
Journal: Neuroscientist
Title: Glycine receptors: Molecular heterogeneity and implications for disease.
Volume: 1
Issue: 3
Pages: 130-41
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Publication
7891186 | J:23734
First Author: Adams RH
Year: 1995
Journal: J Neurosci
Title: Gene structure and glial expression of the glycine transporter GlyT1 in embryonic and adult rodents.
Volume: 15
Issue: 3 Pt 2
Pages: 2524-32
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Publication
4557539 | J:5286
First Author: Lane PW
Year: 1972
Journal: J Hered
Title: Two new mutations in linkage group XVI of the house mouse. Flaky tail and varitint-waddler-J.
Volume: 63
Issue: 3
Pages: 135-40
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Publication
22988142 | J:203021
First Author: Kunz PA
Year: 2012
Journal: J Physiol
Title: Glycine receptors support excitatory neurotransmitter release in developing mouse visual cortex.
Volume: 590
Issue: 22
Pages: 5749-64
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Publication
16461637 | J:105913
First Author: Moran JL
Year: 2006
Journal: Genome Res
Title: Utilization of a whole genome SNP panel for efficient genetic mapping in the mouse.
Volume: 16
Issue: 3
Pages: 436-40
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Publication
8406478 | J:13547
First Author: Buckwalter MS
Year: 1993
Journal: Genomics
Title: Genetic mapping and evaluation of candidate genes for spasmodic, a neurological mouse mutation with abnormal startle response.
Volume: 17
Issue: 2
Pages: 279-86
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Publication
489953 | J:6211
First Author: Lane PW
Year: 1979
Journal: J Hered
Title: Gene order in linkage group XVI of the house mouse.
Volume: 70
Issue: 4
Pages: 239-44
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Publication
18854036 | J:160737
 
First Author: Heupel K
Year: 2008
Journal: Neural Dev
Title: Loss of transforming growth factor-beta 2 leads to impairment of central synapse function.
Volume: 3
Pages: 25
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Publication
12183685 | J:78665
First Author: Kirstein SL
Year: 2002
Journal: J Pharmacol Exp Ther
Title: Quantitative trait loci affecting initial sensitivity and acute functional tolerance to ethanol-induced ataxia and brain cAMP signaling in BXD recombinant inbred mice.
Volume: 302
Issue: 3
Pages: 1238-45
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Publication
19723784 | J:159572
First Author: Medrihan L
Year: 2009
Journal: J Physiol
Title: Neurobeachin, a protein implicated in membrane protein traffic and autism, is required for the formation and functioning of central synapses.
Volume: 587
Issue: Pt 21
Pages: 5095-106
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Publication
28706241 | J:253696
First Author: Feng S
Year: 2017
Journal: Sci Rep
Title: Abnormal Paraventricular Nucleus of Hypothalamus and Growth Retardation Associated with Loss of Nuclear Receptor Gene COUP-TFII.
Volume: 7
Issue: 1
Pages: 5282
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Publication
20826655 | J:164295
First Author: Jin K
Year: 2010
Journal: J Neurosci
Title: Early B-cell factors are required for specifying multiple retinal cell types and subtypes from postmitotic precursors.
Volume: 30
Issue: 36
Pages: 11902-16
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Publication
9070927 | J:37827
First Author: Watkins-Chow DE
Year: 1997
Journal: Genomics
Title: Genetic mapping of 21 genes on mouse chromosome 11 reveals disruptions in linkage conservation with human chromosome 5.
Volume: 40
Issue: 1
Pages: 114-22
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Publication
19208226 | J:147160
 
First Author: Chambers D
Year: 2009
Journal: Neural Dev
Title: Rhombomere-specific analysis reveals the repertoire of genetic cues expressed across the developing hindbrain.
Volume: 4
Pages: 6
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Publication
22723691 | J:185665
First Author: Guo Z
Year: 2012
Journal: J Neurosci
Title: Tlx1/3 and Ptf1a control the expression of distinct sets of transmitter and peptide receptor genes in the developing dorsal spinal cord.
Volume: 32
Issue: 25
Pages: 8509-20
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:73065
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
- | J:265051
     
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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Publication
- | J:346132
       
First Author: The Gene Ontology Consortium
Year: 2016
Title: Automatic assignment of GO terms using logical inference, based on on inter-ontology links
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Publication
24952961 | J:215487
First Author: Thompson CL
Year: 2014
Journal: Neuron
Title: A high-resolution spatiotemporal atlas of gene expression of the developing mouse brain.
Volume: 83
Issue: 2
Pages: 309-323
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:155856
       
First Author: The Gene Ontology Consortium
Year: 2014
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat orthologs
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Allele
Tg(Thy1-GLRA1*R271Q)382Wha | MGI:5306914
Name: transgene insertion 382, Hans Weiher
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
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Genotype
Genotype
Symbol: Tg(Thy1-GLRA1*R271Q)382Wha/Tg(Thy1-GLRA1*R271Q)382Wha
Background: involves: C57BL/6 * DBA/2
Zygosity: hm
Has Mutant Allele: true
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Allele
Glra1<spd> | MGI:1856362
 
Name: glycine receptor, alpha 1 subunit; spasmodic
Allele Type: Spontaneous
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Allele
Glra1<tm1Rah> | MGI:2676917
 
Name: glycine receptor, alpha 1 subunit; targeted mutation 1, R Adron Harris
Allele Type: Targeted
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Allele
Glra1<tm1Betz> | MGI:3696673
 
Name: glycine receptor, alpha 1 subunit; targeted mutation 1, Heinrich Betz
Allele Type: Targeted
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Allele
Glra1<spd-ot9J> | MGI:5790694
Name: glycine receptor, alpha 1 subunit; spasmodic oscillator 9 Jackson
Allele Type: Spontaneous
Attribute String: Not Specified
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Allele
Tg(Thy1-GLRA1*R271Q)300Wha | MGI:5086230
Name: transgene insertion 300, Hans Weiher
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
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Transgene
MGI:5306913 | Tg(Thy1-GLRA1*R271Q)382Wha
Type: transgene
Organism: mouse, laboratory
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Genotype
Genotype
Symbol: Glra1/Glra1<+>
Background: involves: 129X1/SvJ * C57BL/6J
Zygosity: ht
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Glra1/Glra1
Background: involves: A/HeJ
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Glra1/Glra1
Background: B6.129P2-Glra1
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Glra1/Glra1
Background: B6.Cg-Glra1/GrsrJ
Zygosity: hm
Has Mutant Allele: true
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DO Term
DOID:0060696 | hyperekplexia 1
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Genotype
Genotype
Symbol: Tg(Thy1-GLRA1*R271Q)300Wha/?
Background: involves: C57BL/6 * DBA/2
Zygosity: ot
Has Mutant Allele: true
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Transgene
MGI:5086224 | Tg(Thy1-GLRA1*R271Q)300Wha
Type: transgene
Organism: mouse, laboratory
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Allele
Gt(ROSA)26Sor<tm1(CAG-GLRA1*,-GFP)Yqd> | MGI:5784524
Name: gene trap ROSA 26, Philippe Soriano; targeted mutation 1, Yu-qiang Ding
Allele Type: Targeted
Attribute String: Conditional ready, Humanized sequence, Inserted expressed sequence, Reporter
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Allele
Gt(ROSA)26Sor<tm3(GLRA1*-GFP)Gpt> | MGI:7299993
Name: gene trap ROSA 26, Philippe Soriano; targeted mutation 3, GemPharmatech Co., Ltd
Allele Type: Targeted
Attribute String: Inserted expressed sequence, Reporter
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Allele
Tg(Thy1-GLRA1)783Wha | MGI:5086269
Name: transgene insertion 783, Hans Weiher
Allele Type: Transgenic
Attribute String: Humanized sequence, Inserted expressed sequence
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Publication
36339258 | J:357184
First Author: Chen K
Year: 2022
Journal: iScience
Title: Single-cell RNA-seq transcriptomic landscape of human and mouse islets and pathological alterations of diabetes.
Volume: 25
Issue: 11
Pages: 105366
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Strain
MGI:5086271 | B6;D2-Tg(Thy1-GLRA1)783Wha/Igc
Attribute String: mutant stock, transgenic
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Genotype
Genotype
Symbol: Tg(Thy1-GLRA1)783Wha/?
Background: involves: C57BL/6 * DBA/2
Zygosity: ot
Has Mutant Allele: true
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Publication
25231486 | J:232456
 
First Author: Hu L
Year: 2014
Journal: Mol Brain
Title: A mouse line for inducible and reversible silencing of specific neurons.
Volume: 7
Pages: 68
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Strain
MGI:5086267 | B6;D2-Tg(Thy1-GLRA1*R271Q)300Wha/Igc
Attribute String: mutant stock, transgenic
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Publication
21562273 | J:173399
First Author: Brooks PL
Year: 2011
Journal: J Neurosci
Title: Impaired GABA and glycine transmission triggers cardinal features of rapid eye movement sleep behavior disorder in mice.
Volume: 31
Issue: 19
Pages: 7111-21
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Strain
MGI:5306931 | B6;D2-Tg(Thy1-GLRA1*R271Q)382Wha/Igc
Attribute String: mutant stock, transgenic
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Genotype
Genotype
Symbol: Tg(Thy1-GLRA1*R271Q)300Wha/Tg(Thy1-GLRA1*R271Q)300Wha
Background: involves: C57BL/6 * DBA/2
Zygosity: hm
Has Mutant Allele: true
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Genotype
Genotype
Symbol: Tg(Thy1-GLRA1*R271Q)382Wha/?
Background: involves: C57BL/6 * DBA/2
Zygosity: ot
Has Mutant Allele: true
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Publication
12036901 | -
First Author: Boultwood J
Year: 2002
Journal: Blood
Title: Narrowing and genomic annotation of the commonly deleted region of the 5q- syndrome.
Volume: 99
Issue: 12
Pages: 4638-41
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Protein Domain
IPR008128 | Glycine_rcpt_A1
Type: Family
Description: Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [, ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [, ].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, vision 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, thereby reducing the activity of inhibitory neurones.Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist atGlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but havesince been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [].GlyRs belong to the ligand-gated ion channel family, which 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, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yieldingtwo isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can 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, astoichiometry 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), the 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, respectively, and a short C-terminal sequence follows TM4. Studiesusing radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing 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, defects in glycinergic transmission areassociated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease []. This ischaracterised by muscular spasms in response to unexpected light or noisestimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4loops,suggesting that these regions are involved in the transduction ofligand binding into channel activation.In humans, the alpha 1 gene is located on chromosome 5p32 []. In situhybridisation studies have shown GLRA1 to be expressed in the spinal cord,brain stem and colliculi. GLRA1 trancripts, together with GLRA3, predominatein the postnatal CNS, replacing GLRA2, which is more abundant in embryonicand neonatal neurones.
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Publication
10414351 | -
 
First Author: Betz H
Year: 1999
Journal: Ann N Y Acad Sci
Title: Structure and functions of inhibitory and excitatory glycine receptors.
Volume: 868
Pages: 667-76
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Publication
11396606 | -
First Author: López-Corcuera B
Year: 2001
Journal: Mol Membr Biol
Title: Glycine neurotransmitter transporters: an update.
Volume: 18
Issue: 1
Pages: 13-20
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Publication
11437237 | -
First Author: Legendre P
Year: 2001
Journal: Cell Mol Life Sci
Title: The glycinergic inhibitory synapse.
Volume: 58
Issue: 5-6
Pages: 760-93
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Publication
9674912 | -
First Author: Cummings CJ
Year: 1998
Journal: Am J Med Genet
Title: Analysis of the genomic structure of the human glycine receptor alpha2 subunit gene and exclusion of this gene as a candidate for Rett syndrome.
Volume: 78
Issue: 2
Pages: 176-8
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Protein Domain
IPR008129 | Glycine_rcpt_A2
Type: Family
Description: Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [, ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [, ].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, vision 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, thereby reducing the activity of inhibitory neurones.Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist atGlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but havesince been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [].GlyRs belong to the ligand-gated ion channel family, which 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, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yieldingtwo isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can 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, astoichiometry 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), the 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, respectively, and a short C-terminal sequence follows TM4. Studiesusing radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing 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, defects in glycinergic transmission areassociated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease []. This ischaracterised by muscular spasms in response to unexpected light or noisestimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.In humans, the GLRA2 gene is located on chromosome Xp22.2-22.1 []. In situhybridisation studies have shown GLRA2 to be expressed in the hippocampus,cerebral cortex and thalamus. GLRA2 trancripts predominate in the neonataland embyonic CNS, and are replaced postnatally by those of GLRA1 and, to alesser extent, GLRA3.
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Protein Domain
IPR008127 | Glycine_rcpt_A
Type: Family
Description: 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, vision 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, thereby reducing the activity of inhibitory neurones.Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist atGlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but havesincebeen found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [].GlyRs belong to the ligand-gated ion channel family, which 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, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yieldingtwo isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can 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, astoichiometry 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), the 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, respectively, and a short C-terminal sequence follows TM4. Studiesusing radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing 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, defects in glycinergic transmission areassociated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease []. This ischaracterised by muscular spasms in response to unexpected light or noisestimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.
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Publication
1323284 | -
First Author: Sato C
Year: 1992
Journal: Biochem Biophys Res Commun
Title: Proposed tertiary structure of the sodium channel.
Volume: 186
Issue: 2
Pages: 1158-67
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Publication
11358478 | -
First Author: Leite JF
Year: 2001
Journal: Mol Cell Neurosci
Title: Structure of ligand-gated ion channels: critical assessment of biochemical data supports novel topology.
Volume: 17
Issue: 5
Pages: 777-92
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Protein
Q64018
Organism: Mus musculus/domesticus
Length: 457  
Fragment?: false
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Protein
Q5NCT9
Organism: Mus musculus/domesticus
Length: 449  
Fragment?: false
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Protein Domain
IPR008060 | Glycine_rcpt_B
Type: Family
Description: Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [, ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [, ].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, vision 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, thereby reducing the activity of inhibitory neurones.Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist atGlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but havesince been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [].GlyRs belong to the ligand-gated ion channel family, which 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, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yieldingtwo isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can 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, astoichiometry of 3:2 (alpha:beta) is observed []. GlyR subunits shareahigh 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), the 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, respectively, and a short C-terminal sequence follows TM4. Studiesusing radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing 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, defects in glycinergic transmission areassociated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease []. This ischaracterised by muscular spasms in response to unexpected light or noisestimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.
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Protein Domain
IPR008130 | Glycine_rcpt_A3
Type: Family
Description: Neurotransmitter ligand-gated ion channels are transmembrane receptor-ion channel complexes that open transiently upon binding of specific ligands, allowing rapid transmission of signals at chemical synapses [, ]. Five of these ion channel receptor families have been shown to form a sequence-related superfamily:Nicotinic acetylcholine receptor (AchR), an excitatory cation channel in vertebrates and invertebrates; in vertebrate motor endplates it is composed of alpha, beta, gamma and delta/epsilon subunits; in neurons it is composed of alpha and non-alpha (or beta) subunits [].Glycine receptor, an inhibitory chloride ion channel composed of alpha and beta subunits [].Gamma-aminobutyric acid (GABA) receptor, an inhibitory chloride ion channel; at least four types of subunits (alpha, beta, gamma and delta) are known [].Serotonin 5HT3 receptor, of which there are seven major types (5HT3-5HT7) [].Glutamate receptor, an excitatory cation channel of which at least three types have been described (kainate, N-methyl-D-aspartate (NMDA) and quisqualate) [].These receptors possess a pentameric structure (made up of varying subunits), surrounding a central pore. All known sequences of subunits from neurotransmitter-gated ion-channels are structurally related. They are composed of a large extracellular glycosylated N-terminal ligand-binding domain, followed by three hydrophobic transmembrane regions which form the ionic channel, followed by an intracellular region of variable length. A fourth hydrophobic region is found at the C-terminal of the sequence [, ].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, vision 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, thereby reducing the activity of inhibitory neurones.Poisoning with strychnine is characterised by over-excitation, muscle spasmsand convulsions. Whilst glycine is the principal physiological agonist atGlyRs, taurine and beta-alanine also behave as agonists []. Compounds thatmodulate GlyR activity include zinc, some alcohols and anaesthetics,picrotoxin, cocaine and some anticonvulsants. GlyRs were thought for sometime to be localised exclusively in the brain stem and spinal cord, but havesince been found to be expressed more widely, including the cochlear nuclei,cerebellar cortex and forebrain [].GlyRs belong to the ligand-gated ion channel family, which 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, corresponding to alpha and beta subunits,respectively. Four genes encoding alpha subunits have been identified (GLRA1to 4), together with a single beta polypeptide (GLRB). The heterogeneity ofalpha subunits is further increased by alternative exon splicing, yieldingtwo isoforms of GLRA1 to 3 []. The characteristics of different GlyRsubtypes, therefore, can 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, astoichiometry 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), the 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, respectively, and a short C-terminal sequence follows TM4. Studiesusing radiolabelled strychnine have shown the alpha subunit to beresponsible for ligand binding, the critical residues for this interaction lying within the N-terminal domain. The beta subunit plays a structuralrole, contributing 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, defects in glycinergic transmission areassociated with complex motor disorders. Mutations in the gene encodingGLRA1 give rise to hyperplexia, or startle disease []. This ischaracterised by muscular spasms in response to unexpected light or noisestimuli, similar to the symptoms of sublethal doses of strychnine. Themutations result in amino acid substitutions within the TM1-2 and TM3-4loops, suggesting that these regions are involved in the transduction ofligand binding into channel activation.GLRA3 is expressed in thecerebellum, olfactory bulb and hippocampus. GLRA3 trancripts, together withGLRA1, predominate in the postnatal CNS, replacing GLRA2, which is moreabundant in embryonic and neonatal neurones.
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Protein
Q7TNC8
Organism: Mus musculus/domesticus
Length: 452  
Fragment?: false
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Protein
Q3UTL8
Organism: Mus musculus/domesticus
Length: 452  
Fragment?: false
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Protein
O54848
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: true
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Protein
Q91XP5
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
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Protein
G5E811
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
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Protein
P48168
Organism: Mus musculus/domesticus
Length: 496  
Fragment?: false
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Protein
Q61603
Organism: Mus musculus/domesticus
Length: 456  
Fragment?: false
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Protein
A1KR23
Organism: Mus musculus/domesticus
Length: 445  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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