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Glycine receptor subunit alpha-1 (Glycine receptor 48 kDa subunit) (Glycine receptor strychnine-binding subunit)

 GLRA1_MOUSE             Reviewed;         457 AA.
Q64018; Q5NCT8; Q64019; Q9R0Y6; Q9R0Y7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
08-DEC-2000, sequence version 2.
23-MAY-2018, entry version 163.
RecName: Full=Glycine receptor subunit alpha-1;
AltName: Full=Glycine receptor 48 kDa subunit;
AltName: Full=Glycine receptor strychnine-binding subunit;
Flags: Precursor;
Name=Glra1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), VARIANT SPD SER-80, AND
DISEASE.
PubMed=7920629; DOI=10.1038/ng0694-131;
Ryan S.G., Buckwalter M.S., Lynch J.W., Handford C.A., Segura L.,
Shiang R., Wasmuth J.J., Camper S.A., Schofield P., O'Connell P.;
"A missense mutation in the gene encoding the alpha 1 subunit of the
inhibitory glycine receptor in the spasmodic mouse.";
Nat. Genet. 7:131-135(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
STRAIN=BALB/cJ;
PubMed=7507926;
Matzenbach B., Maulet Y., Sefton L., Courtier B., Avner P.,
Guenet J.-L., Betz H.;
"Structural analysis of mouse glycine receptor alpha subunit genes.
Identification and chromosomal localization of a novel variant.";
J. Biol. Chem. 269:2607-2612(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
DISEASE.
PubMed=7874121; DOI=10.1093/hmg/3.11.2025;
Buckwalter M.S., Cook S.A., Davisson M.T., White W.F., Camper S.A.;
"A frameshift mutation in the mouse alpha 1 glycine receptor gene
(Glra1) results in progressive neurological symptoms and juvenile
death.";
Hum. Mol. Genet. 3:2025-2030(1994).
[5]
DISEASE, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9145798; DOI=10.1016/S0306-4522(96)00567-2;
Kling C., Koch M., Saul B., Becker C.M.;
"The frameshift mutation oscillator (Glra1(spd-ot)) produces a
complete loss of glycine receptor alpha1-polypeptide in mouse central
nervous system.";
Neuroscience 78:411-417(1997).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12975813; DOI=10.1002/cne.10852;
Haverkamp S., Mueller U., Harvey K., Harvey R.J., Betz H., Waessle H.;
"Diversity of glycine receptors in the mouse retina: localization of
the alpha3 subunit.";
J. Comp. Neurol. 465:524-539(2003).
[7]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DISEASE.
PubMed=16672662; DOI=10.1523/JNEUROSCI.3991-05.2006;
Graham B.A., Schofield P.R., Sah P., Margrie T.W., Callister R.J.;
"Distinct physiological mechanisms underlie altered glycinergic
synaptic transmission in the murine mutants spastic, spasmodic, and
oscillator.";
J. Neurosci. 26:4880-4890(2006).
[8]
FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND MUTAGENESIS OF ASP-108.
PubMed=17114051; DOI=10.1016/j.neuron.2006.09.035;
Hirzel K., Mueller U., Latal A.T., Huelsmann S., Grudzinska J.,
Seeliger M.W., Betz H., Laube B.;
"Hyperekplexia phenotype of glycine receptor alpha1 subunit mutant
mice identifies Zn(2+) as an essential endogenous modulator of
glycinergic neurotransmission.";
Neuron 52:679-690(2006).
[9]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
420-LYS-LYS-421.
PubMed=24801766; DOI=10.1038/npp.2014.100;
Aguayo L.G., Castro P., Mariqueo T., Munoz B., Xiong W., Zhang L.,
Lovinger D.M., Homanics G.E.;
"Altered sedative effects of ethanol in mice with alpha1 glycine
receptor subunits that are insensitive to Gbetagamma modulation.";
Neuropsychopharmacology 39:2538-2548(2014).
-!- FUNCTION: Glycine receptors are ligand-gated chloride channels.
Channel opening is triggered by extracellular glycine
(PubMed:16672662, PubMed:17114051, PubMed:24801766). Channel
opening is also triggered by taurine and beta-alanine (By
similarity). Channel characteristics depend on the subunit
composition; heteropentameric channels are activated by lower
glycine levels and display faster desensitization (By similarity).
Plays an important role in the down-regulation of neuronal
excitability (PubMed:9145798). Contributes to the generation of
inhibitory postsynaptic currents (PubMed:16672662,
PubMed:17114051, PubMed:24801766). Channel activity is potentiated
by ethanol. Potentiation of channel activity by intoxicating
levels of ethanol contribute to the sedative effects of ethanol
(PubMed:24801766). {ECO:0000250|UniProtKB:P23415,
ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051,
ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}.
-!- ENZYME REGULATION: Inhibited by strychnine. Inhibited by
picrotoxin (PubMed:16672662). Channel activity is enhanced by 5 uM
Zn(2+) and inhibited by 100 uM Zn(2+) (PubMed:17114051).
{ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051}.
-!- SUBUNIT: Homopentamer (in vitro). Interacts with GLRB to form
heteropentameric channels; this is probably the predominant form
in vivo. Heteropentamer composed of two GLRA1 and three GLRB.
Heteropentamer composed of three GLRA1 and two GLRB. Both
homopentamers and heteropentamers form functional ion channels,
but their characteristics are subtly different.
{ECO:0000250|UniProtKB:P23415}.
-!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
membrane {ECO:0000305|PubMed:12975813,
ECO:0000305|PubMed:17114051, ECO:0000305|PubMed:24801766}; Multi-
pass membrane protein {ECO:0000305}. Cell junction, synapse
{ECO:0000269|PubMed:12975813, ECO:0000269|PubMed:17114051,
ECO:0000269|PubMed:24801766}. Perikaryon
{ECO:0000269|PubMed:24801766}. Cell projection, dendrite
{ECO:0000269|PubMed:24801766}. Cell membrane
{ECO:0000269|PubMed:16672662, ECO:0000305|PubMed:9145798}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:P23415, ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a; Synonyms=Long;
IsoId=Q64018-1; Sequence=Displayed;
Name=b; Synonyms=Short;
IsoId=Q64018-2; Sequence=VSP_000080;
-!- TISSUE SPECIFICITY: Detected in spinal cord neurons
(PubMed:9145798, PubMed:17114051, PubMed:24801766). Detected in
brain stem neurons (PubMed:16672662, PubMed:24801766). Detected at
lower levels in hippocampus and cerebellum (PubMed:24801766).
Detected in the inner plexiform layer of the retina (at protein
level) (PubMed:12975813). {ECO:0000269|PubMed:12975813,
ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:17114051,
ECO:0000269|PubMed:24801766, ECO:0000269|PubMed:9145798}.
-!- DOMAIN: The channel pore is formed by pentameric assembly of the
second transmembrane domain from all five subunits. Channel
opening is effected by an outward rotation of the transmembrane
domains that increases the diameter of the pore.
{ECO:0000250|UniProtKB:O93430}.
-!- DISEASE: Note=Defects in Glra1 are the cause of the spasmodic
(spd) phenotype, a mouse mutant which resembles the human
neurological disease, hyperekplexia (or startle disease (STHE))
(PubMed:7920629). Defects in Glra1 are the cause of the lethal
oscillator (spd-ot) phenotype. Mutant mice display a fine motor
tremor and muscle spasms that begin at 2 weeks of age and
progressively worsen, resulting in death by 3 weeks of age
(PubMed:7874121). Heterozygous mice show an increased acoustic
startle response (PubMed:9145798). Neurons from homozygous
oscillator mice have dramatically reduced amplitude and frequency
of glycinergic inhibitory postsynaptic currents (PubMed:16672662).
The oscillator phenotype is due to the complete absence of Glra1
protein (PubMed:9145798). {ECO:0000269|PubMed:16672662,
ECO:0000269|PubMed:7874121, ECO:0000269|PubMed:7920629,
ECO:0000269|PubMed:9145798}.
-!- MISCELLANEOUS: The alpha subunit binds strychnine.
{ECO:0000269|PubMed:16672662, ECO:0000269|PubMed:7874121,
ECO:0000269|PubMed:9145798}.
-!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
family. Glycine receptor (TC 1.A.9.3) subfamily. GLRA1 sub-
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; S73717; AAB32157.2; -; mRNA.
EMBL; S73718; AAB32158.2; -; mRNA.
EMBL; X75832; CAB52398.1; -; Genomic_DNA.
EMBL; X75833; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75834; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75835; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75836; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75837; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75838; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75839; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75840; CAB52398.1; JOINED; Genomic_DNA.
EMBL; X75832; CAB52399.1; -; Genomic_DNA.
EMBL; X75833; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75834; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75835; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75836; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75837; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75838; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75839; CAB52399.1; JOINED; Genomic_DNA.
EMBL; X75840; CAB52399.1; JOINED; Genomic_DNA.
EMBL; AL596207; CAI35359.1; -; Genomic_DNA.
CCDS; CCDS24715.1; -. [Q64018-2]
CCDS; CCDS70190.1; -. [Q64018-1]
PIR; C49970; C49970.
RefSeq; NP_001277750.1; NM_001290821.1. [Q64018-1]
UniGene; Mm.89320; -.
ProteinModelPortal; Q64018; -.
STRING; 10090.ENSMUSP00000099777; -.
iPTMnet; Q64018; -.
PhosphoSitePlus; Q64018; -.
SwissPalm; Q64018; -.
PaxDb; Q64018; -.
PRIDE; Q64018; -.
Ensembl; ENSMUST00000075603; ENSMUSP00000075032; ENSMUSG00000000263. [Q64018-1]
Ensembl; ENSMUST00000102716; ENSMUSP00000099777; ENSMUSG00000000263. [Q64018-2]
GeneID; 14654; -.
KEGG; mmu:14654; -.
UCSC; uc007izo.2; mouse. [Q64018-1]
CTD; 2741; -.
MGI; MGI:95747; Glra1.
eggNOG; KOG3643; Eukaryota.
eggNOG; ENOG410XPWH; LUCA.
GeneTree; ENSGT00760000118821; -.
HOGENOM; HOG000231336; -.
HOVERGEN; HBG051707; -.
InParanoid; Q64018; -.
KO; K05193; -.
OMA; FNFAYGM; -.
OrthoDB; EOG091G0805; -.
PhylomeDB; Q64018; -.
TreeFam; TF315453; -.
Reactome; R-MMU-112314; Neurotransmitter receptors and postsynaptic signal transmission.
PRO; PR:Q64018; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000000263; -.
CleanEx; MM_GLRA1; -.
ExpressionAtlas; Q64018; baseline and differential.
Genevisible; Q64018; MM.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; IDA:MGI.
GO; GO:0016594; F:glycine binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0030977; F:taurine binding; ISS:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
GO; GO:0022824; F:transmitter-gated ion channel activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0007340; P:acrosome reaction; IMP:MGI.
GO; GO:0001508; P:action potential; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0071361; P:cellular response to ethanol; ISS:UniProtKB.
GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
GO; GO:0060080; P:inhibitory postsynaptic potential; IMP:UniProtKB.
GO; GO:0006811; P:ion transport; ISS:UniProtKB.
GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
GO; GO:0051970; P:negative regulation of transmission of nerve impulse; ISS:UniProtKB.
GO; GO:0050905; P:neuromuscular process; IMP:MGI.
GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
GO; GO:2000344; P:positive regulation of acrosome reaction; ISO:MGI.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0051260; P:protein homooligomerization; IEA:Ensembl.
GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
GO; GO:0097305; P:response to alcohol; IMP:UniProtKB.
GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
GO; GO:0060013; P:righting reflex; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; IMP:MGI.
Gene3D; 2.70.170.10; -; 1.
InterPro; IPR006028; GABAA/Glycine_rcpt.
InterPro; IPR008127; Glycine_rcpt_A.
InterPro; IPR008128; Glycine_rcpt_A1.
InterPro; IPR006202; Neur_chan_lig-bd.
InterPro; IPR036734; Neur_chan_lig-bd_sf.
InterPro; IPR006201; Neur_channel.
InterPro; IPR036719; Neuro-gated_channel_TM_sf.
InterPro; IPR006029; Neurotrans-gated_channel_TM.
InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
PANTHER; PTHR18945; PTHR18945; 1.
Pfam; PF02931; Neur_chan_LBD; 1.
Pfam; PF02932; Neur_chan_memb; 1.
PRINTS; PR00253; GABAARECEPTR.
PRINTS; PR01673; GLYRALPHA.
PRINTS; PR01674; GLYRALPHA1.
PRINTS; PR00252; NRIONCHANNEL.
SUPFAM; SSF63712; SSF63712; 1.
SUPFAM; SSF90112; SSF90112; 1.
TIGRFAMs; TIGR00860; LIC; 1.
PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Chloride; Chloride channel; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Ion channel; Ion transport;
Ligand-gated ion channel; Membrane; Metal-binding;
Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
Synapse; Transmembrane; Transmembrane helix; Transport; Zinc.
SIGNAL 1 28 {ECO:0000250|UniProtKB:P07727}.
CHAIN 29 457 Glycine receptor subunit alpha-1.
/FTId=PRO_0000000413.
TOPO_DOM 29 250 Extracellular.
{ECO:0000250|UniProtKB:O93430}.
TRANSMEM 251 272 Helical; Name=1.
{ECO:0000250|UniProtKB:O93430}.
TOPO_DOM 273 277 Cytoplasmic.
{ECO:0000250|UniProtKB:O93430}.
TRANSMEM 278 298 Helical; Name=2.
{ECO:0000250|UniProtKB:O93430}.
TOPO_DOM 299 309 Extracellular.
{ECO:0000250|UniProtKB:O93430}.
TRANSMEM 310 330 Helical; Name=3.
{ECO:0000250|UniProtKB:O93430}.
TOPO_DOM 331 425 Cytoplasmic.
{ECO:0000250|UniProtKB:O93430}.
TRANSMEM 426 446 Helical; Name=4.
{ECO:0000250|UniProtKB:O93430}.
TOPO_DOM 447 457 Extracellular.
{ECO:0000250|UniProtKB:O93430}.
REGION 230 235 Strychnine-binding.
{ECO:0000250|UniProtKB:O93430}.
METAL 220 220 Zinc. {ECO:0000250|UniProtKB:P23415}.
METAL 222 222 Zinc. {ECO:0000250|UniProtKB:P23415}.
METAL 243 243 Zinc. {ECO:0000250|UniProtKB:P23415}.
SITE 289 289 Important for obstruction of the ion pore
in the closed conformation.
{ECO:0000250|UniProtKB:O93430}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 166 180 {ECO:0000250|UniProtKB:P23415}.
DISULFID 226 237 {ECO:0000250|UniProtKB:P23415}.
VAR_SEQ 354 361 Missing (in isoform b).
{ECO:0000303|PubMed:7920629}.
/FTId=VSP_000080.
VARIANT 80 80 A -> S (in spd).
{ECO:0000269|PubMed:7920629}.
MUTAGEN 108 108 D->A: Eliminates potentiation of glycine-
mediated currents by Zn(2+) and causes
neuromotor defects similar to human
startle disease.
{ECO:0000269|PubMed:17114051}.
MUTAGEN 421 422 KK->AA: Reduces the increase of channel
activity in response to ethanol and
improves tolerance of intoxicating levels
of alcohol.
{ECO:0000269|PubMed:24801766}.
CONFLICT 84 84 M -> I (in Ref. 2; CAB52398/CAB52399).
{ECO:0000305}.
CONFLICT 426 429 ISRI -> NISH (in Ref. 2; CAB52398/
CAB52399). {ECO:0000305}.
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


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