Glycine receptor, alpha 1

Rendering of GLRA1 from PDB 1MOT

Available structures
PDB	1MOT, 1VRY

Identifiers

Symbols

GLRA1; MGC138878; MGC138879; STHE

External IDs

OMIM: 138491 MGI: 95747 HomoloGene: 20083 IUPHAR: α1 GeneCards: GLRA1 Gene

Gene Ontology
Molecular function	• receptor activity • ion channel activity • extracellular ligand-gated ion channel activity • protein binding • glycine binding • extracellular-glycine-gated chloride channel activity • extracellular-glycine-gated chloride channel activity • extracellular-glycine-gated chloride channel activity • transmitter-gated ion channel activity • taurine binding
Cellular component	• plasma membrane • integral to plasma membrane • integral to plasma membrane • integral to plasma membrane • integral to membrane • cell junction • chloride channel complex • intracellular membrane-bounded organelle • synapse • postsynaptic membrane
Biological process	• startle response • ion transport • chloride transport • muscle contraction • neuropeptide signaling pathway • ion transmembrane transport • regulation of membrane potential • negative regulation of transmission of nerve impulse • transmembrane transport • positive regulation of acrosome reaction
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
151.2 – 151.3 Mb

Chr 11:
55.33 – 55.42 Mb

PubMed search

[1]

[2]

Glycine receptor subunit alpha-1 is a protein that in humans is encoded by the GLRA1 gene.^[1]^[2]

The inhibitory glycine receptor mediates postsynaptic inhibition in the spinal cord and other regions of the central nervous system. It is a pentameric receptor composed of alpha and beta subunits. The GLRB gene (MIM 138492) encodes the beta subunit of the receptor.[supplied by OMIM]^[3]

References

^ Ryan SG, Sherman SL, Terry JC, Sparkes RS, Torres MC, Mackey RW (Sep 1992). "Startle disease, or hyperekplexia: response to clonazepam and assignment of the gene (STHE) to chromosome 5q by linkage analysis". Ann Neurol 31 (6): 663–8. doi:10.1002/ana.410310615. PMID 1355335.
^ Shiang R, Ryan SG, Zhu YZ, Hahn AF, O'Connell P, Wasmuth JJ (Mar 1994). "Mutations in the alpha 1 subunit of the inhibitory glycine receptor cause the dominant neurologic disorder, hyperekplexia". Nat Genet 5 (4): 351–8. doi:10.1038/ng1293-351. PMID 8298642.
^ "Entrez Gene: GLRA1 glycine receptor, alpha 1 (startle disease/hyperekplexia, stiff man syndrome)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2741.

Ruiz-Gómez A, Vaello ML, Valdivieso F, Mayor F (1991). "Phosphorylation of the 48-kDa subunit of the glycine receptor by protein kinase C.". J. Biol. Chem. 266 (1): 559–66. PMID 1845981.
Grenningloh G, Schmieden V, Schofield PR, et al. (1990). "Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes.". EMBO J. 9 (3): 771–6. PMC 551735. PMID 2155780. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=551735.
Langosch D, Herbold A, Schmieden V, et al. (1994). "Importance of Arg-219 for correct biogenesis of alpha 1 homooligomeric glycine receptors.". FEBS Lett. 336 (3): 540–4. doi:10.1016/0014-5793(93)80872-R. PMID 7506679.
Shiang R, Ryan SG, Zhu YZ, et al. (1995). "Mutational analysis of familial and sporadic hyperekplexia.". Ann. Neurol. 38 (1): 85–91. doi:10.1002/ana.410380115. PMID 7611730.
Baker E, Sutherland GR, Schofield PR (1995). "Localization of the glycine receptor alpha 1 subunit gene (GLRA1) to chromosome 5q32 by FISH.". Genomics 22 (2): 491–3. doi:10.1006/geno.1994.1419. PMID 7806244.
Rees MI, Andrew M, Jawad S, Owen MJ (1995). "Evidence for recessive as well as dominant forms of startle disease (hyperekplexia) caused by mutations in the alpha 1 subunit of the inhibitory glycine receptor.". Hum. Mol. Genet. 3 (12): 2175–9. doi:10.1093/hmg/3.12.2175. PMID 7881416.
Ryan SG, Buckwalter MS, Lynch JW, et al. (1994). "A missense mutation in the gene encoding the alpha 1 subunit of the inhibitory glycine receptor in the spasmodic mouse.". Nat. Genet. 7 (2): 131–5. doi:10.1038/ng0694-131. PMID 7920629.
Langosch D, Laube B, Rundström N, et al. (1994). "Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia.". EMBO J. 13 (18): 4223–8. PMC 395349. PMID 7925268. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=395349.
Schorderet DF, Pescia G, Bernasconi A, Regli F (1995). "An additional family with Startle disease and a G1192A mutation at the alpha 1 subunit of the inhibitory glycine receptor gene.". Hum. Mol. Genet. 3 (7): 1201. doi:10.1093/hmg/3.7.1201. PMID 7981700.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Bormann J, Rundström N, Betz H, Langosch D (1994). "Residues within transmembrane segment M2 determine chloride conductance of glycine receptor homo- and hetero-oligomers.". EMBO J. 13 (6): 1493. PMC 394970. PMID 8137830. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=394970.
Milani N, Dalprá L, del Prete A, et al. (1996). "A novel mutation (Gln266-->His) in the alpha 1 subunit of the inhibitory glycine-receptor gene (GLRA1) in hereditary hyperekplexia.". Am. J. Hum. Genet. 58 (2): 420–2. PMC 1914546. PMID 8571969. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1914546.
Brune W, Weber RG, Saul B, et al. (1996). "A GLRA1 null mutation in recessive hyperekplexia challenges the functional role of glycine receptors.". Am. J. Hum. Genet. 58 (5): 989–97. PMC 1914607. PMID 8651283. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1914607.
Elmslie FV, Hutchings SM, Spencer V, et al. (1996). "Analysis of GLRA1 in hereditary and sporadic hyperekplexia: a novel mutation in a family cosegregating for hyperekplexia and spastic paraparesis.". J. Med. Genet. 33 (5): 435–6. doi:10.1136/jmg.33.5.435. PMC 1050620. PMID 8733061. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1050620.
Monani U, Burghes AH (1997). "Structure of the human alpha 2 subunit gene of the glycine receptor--use of vectorette and Alu-exon PCR.". Genome Res. 6 (12): 1200–6. doi:10.1101/gr.6.12.1200. PMID 8973915.
Seri M, Bolino A, Galietta LJ, et al. (1997). "Startle disease in an Italian family by mutation (K276E): The alpha-subunit of the inhibiting glycine receptor.". Hum. Mutat. 9 (2): 185–7. doi:10.1002/(SICI)1098-1004(1997)9:2<185::AID-HUMU14>3.0.CO;2-Z. PMID 9067762.
Vergouwe MN, Tijssen MA, Shiang R, et al. (1998). "Hyperekplexia-like syndromes without mutations in the GLRA1 gene.". Clinical neurology and neurosurgery 99 (3): 172–8. doi:10.1016/S0303-8467(97)00022-X. PMID 9350397.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Ion channel, cell surface receptor: ligand-gated ion channels

Cys-loop receptors

5-HT/serotonin	5-HT₃ (A, B, C, D, E)

GABA	GABA_A (α₁, α₂, α₃, α₄, α₅, α₆, β₁, β₂, β₃, γ₁, γ₂, γ₃, δ, ε, π, θ) · GABA_A-ρ (ρ₁, ρ₂, ρ₃)

Glycine	α₁ · α₂ · α₃ · α₄ · β

Nicotinic acetylcholine	monomers: α1 · α2 · α3 · α4 · α5 · α6 · α7 · α9 · α10 · β1 · β2 · β3 · β4 · δ · ε pentamers: (α3)₂(β4)₃ · (α4)₂(β2)₃ · (α7)₅ · (α1)₂(β4)₃ - Ganglion type · (α1)₂β1δε - Muscle type

Zinc	Zinc-activated

Ionotropic glutamates

Ligand-gated only	AMPA (1, 2, 3, 4) · Kainate (1, 2, 3, 4, 5)

Voltage- and ligand-gated	NMDA (1, 2A, 2B, 2C, 2D, 3A, 3B, L1A, L1B)

‘Orphan’	GluD (δ₁, δ₂)

ATP-gated channels

Purinergic receptors	P2X (1, 2, 3, 4, 5, 6, 7)

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

Glycine receptor, alpha 1

See also

References

Further reading