Glycine receptor, alpha 1

Glycine receptor subunit alpha-1 is a protein that in humans is encoded by the GLRA1 gene.^[5][6]

GLRA1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1MOT, 1VRY, 2M6B, 2M6I, 4X5T
Identifiers
Aliases	GLRA1, HKPX1, STHE, Glycine receptor, alpha 1, glycine receptor alpha 1
External IDs	OMIM: 138491; MGI: 95747; HomoloGene: 20083; GeneCards: GLRA1; OMA:GLRA1 - orthologs
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q33.1 Start 151,822,513 bp[1] End 151,924,851 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 B1.3|11 33.12 cM Start 55,405,064 bp[2] End 55,499,024 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in islet of Langerhans testicle hypothalamus substantia nigra C1 segment ganglionic eminence cerebellum cerebellar cortex cerebellar hemisphere gonad Top expressed in medial vestibular nucleus lumbar subsegment of spinal cord ventromedial nucleus pontine nuclei anterior horn of spinal cord dorsal tegmental nucleus facial motor nucleus deep cerebellar nuclei superior colliculus lateral hypothalamus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function zinc ion binding glycine binding metal ion binding transmitter-gated ion channel activity extracellularly glycine-gated chloride channel activity protein binding extracellularly glycine-gated ion channel activity taurine binding chloride channel activity extracellular ligand-gated ion channel activity ion channel activity identical protein binding transmembrane signaling receptor activity transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential Cellular component integral component of membrane perikaryon postsynaptic membrane cell projection intracellular membrane-bounded organelle membrane plasma membrane synapse integral component of plasma membrane inhibitory synapse intracellular anatomical structure chloride channel complex cell junction dendrite endoplasmic reticulum external side of plasma membrane soma neuron projection calyx of Held glycinergic synapse integral component of presynaptic membrane integral component of postsynaptic specialization membrane Biological process inhibitory postsynaptic potential muscle contraction startle response neuromuscular process controlling posture cellular response to ethanol protein heterooligomerization regulation of respiratory gaseous exchange regulation of membrane potential ion transport anion transport cellular response to zinc ion regulation of respiratory gaseous exchange by nervous system process acrosome reaction positive regulation of acrosome reaction neuromuscular process cellular response to amino acid stimulus synaptic transmission, glycinergic action potential chloride transport righting reflex neuropeptide signaling pathway protein homooligomerization negative regulation of transmission of nerve impulse visual perception adult walking behavior chloride transmembrane transport response to alcohol excitatory postsynaptic potential chemical synaptic transmission ion transmembrane transport signal transduction response to amino acid nervous system process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2741 14654 Ensembl ENSG00000145888 ENSMUSG00000000263 UniProt P23415 Q64018 RefSeq (mRNA) NM_000171 NM_001146040 NM_001292000 NM_001290821 NM_020492 RefSeq (protein) NP_000162 NP_001139512 NP_001278929 NP_001277750 NP_065238 Location (UCSC) Chr 5: 151.82 – 151.92 Mb Chr 11: 55.41 – 55.5 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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 solely of alpha subunits. The GLRB gene encodes the alpha subunit of the receptor.^[7]

Clinical significance

Mutations in the gene have been associated with hyperekplexia, a neurologic syndrome associated with an exaggerated startle reaction.^[8][9]

See also

• Glycine receptor
• Stiff person syndrome
• Hyperekplexia

References

1. GRCh38: Ensembl release 89: ENSG00000145888 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000263 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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): 663–668. doi:10.1002/ana.410310615. PMID 1355335. S2CID 28879043.
6. 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): 351–358. doi:10.1038/ng1293-351. PMID 8298642. S2CID 21410824.
7. "Entrez Gene: GLRA1 glycine receptor, alpha 1 (startle disease/hyperekplexia, stiff man syndrome)".
8. Tijssen MA, Shiang R, van Deutekom J, Boerman RH, Wasmuth JJ, Sandkuijl LA, Frants RR, Padberg GW (June 1995). "Molecular genetic reevaluation of the Dutch hyperekplexia family". Arch. Neurol. 52 (6): 578–582. doi:10.1001/archneur.1995.00540300052012. hdl:2066/20657. PMID 7763205. S2CID 14067463.
9. Zhou L, Chillag KL, Nigro MA (October 2002). "Hyperekplexia: a treatable neurogenetic disease". Brain Dev. 24 (7): 669–674. doi:10.1016/S0387-7604(02)00095-5. PMID 12427512. S2CID 40864297.

Further reading

• 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): 559–566. doi:10.1016/S0021-9258(18)52472-8. PMID 1845981.
• Grenningloh G, Schmieden V, Schofield PR, Seeburg PH, Siddique T, Mohandas TK, Becker CM, Betz H (1990). "Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes". EMBO J. 9 (3): 771–776. doi:10.1002/j.1460-2075.1990.tb08172.x. PMC 551735. PMID 2155780.
• Langosch D, Herbold A, Schmieden V, Borman J, Kirsch J (1994). "Importance of Arg-219 for correct biogenesis of alpha 1 homooligomeric glycine receptors". FEBS Lett. 336 (3): 540–544. doi:10.1016/0014-5793(93)80872-R. PMID 7506679. S2CID 84795107.
• Shiang R, Ryan SG, Zhu YZ, Fielder TJ, Allen RJ, Fryer A, Yamashita S, O'Connell P, Wasmuth JJ (1995). "Mutational analysis of familial and sporadic hyperekplexia". Ann. Neurol. 38 (1): 85–91. doi:10.1002/ana.410380115. PMID 7611730. S2CID 22129217.
• 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): 491–493. 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): 2175–2179. doi:10.1093/hmg/3.12.2175. PMID 7881416.
• Ryan SG, Buckwalter MS, Lynch JW, Handford CA, Segura L, Shiang R, Wasmuth JJ, Camper SA, Schofield P, O'Connell P (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): 131–135. doi:10.1038/ng0694-131. PMID 7920629. S2CID 32946709.
• Langosch D, Laube B, Rundström N, Schmieden V, Bormann J, Betz H (1994). "Decreased agonist affinity and chloride conductance of mutant glycine receptors associated with human hereditary hyperekplexia". EMBO J. 13 (18): 4223–4228. doi:10.1002/j.1460-2075.1994.tb06742.x. PMC 395349. PMID 7925268.
• 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): 171–174. 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. doi:10.1002/j.1460-2075.1994.tb06405.x. PMC 394970. PMID 8137830.
• Milani N, Dalprá L, del Prete A, Zanini R, Larizza L (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): 420–422. PMC 1914546. PMID 8571969.
• Brune W, Weber RG, Saul B, von Knebel Doeberitz M, Grond-Ginsbach C, Kellerman K, Meinck HM, Becker CM (1996). "A GLRA1 null mutation in recessive hyperekplexia challenges the functional role of glycine receptors". Am. J. Hum. Genet. 58 (5): 989–997. PMC 1914607. PMID 8651283.
• Elmslie FV, Hutchings SM, Spencer V, Curtis A, Covanis T, Gardiner RM, Rees M (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): 435–436. doi:10.1136/jmg.33.5.435. PMC 1050620. PMID 8733061.
• 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): 1200–1206. doi:10.1101/gr.6.12.1200. PMID 8973915.
• Seri M, Bolino A, Galietta LJ, Lerone M, Silengo M, Romeo G (1997). "Startle disease in an Italian family by mutation (K276E): The alpha-subunit of the inhibiting glycine receptor". Hum. Mutat. 9 (2): 185–187. doi:10.1002/(SICI)1098-1004(1997)9:2<185::AID-HUMU14>3.0.CO;2-Z. PMID 9067762. S2CID 38078893.
• Vergouwe MN, Tijssen MA, Shiang R, van Dijk JG, al Shahwan S, Ophoff RA, Frants RR (1998). "Hyperekplexia-like syndromes without mutations in the GLRA1 gene". Clinical Neurology and Neurosurgery. 99 (3): 172–178. doi:10.1016/S0303-8467(97)00022-X. PMID 9350397. S2CID 43274005.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.

External links

• Overview of all the structural information available in the PDB for UniProt: P23415 (Glycine receptor subunit alpha-1) at the PDBe-KB.

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