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

 GLRA1_BOVIN             Reviewed;         457 AA.
P57695; Q9GKE9; Q9GKF0;
08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
08-DEC-2000, sequence version 1.
28-MAR-2018, entry version 136.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), DISEASE,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
PubMed=11178872; DOI=10.1006/mcne.2000.0934;
Pierce K.D., Handford C.A., Morris R., Vafa B., Dennis J.A.,
Healy P.J., Schofield P.R.;
"A nonsense mutation in the alpha1 subunit of the inhibitory glycine
receptor associated with bovine myoclonus.";
Mol. Cell. Neurosci. 17:354-363(2001).
-!- FUNCTION: Glycine receptors are ligand-gated chloride channels.
Channel opening is triggered by extracellular glycine. Channel
opening is also triggered by taurine and beta-alanine. 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:11178872). Contributes to the generation of inhibitory
postsynaptic currents. Channel activity is potentiated by ethanol
(By similarity). Potentiation of channel activity by intoxicating
levels of ethanol contribute to the sedative effects of ethanol
(By similarity). {ECO:0000250|UniProtKB:P23415,
ECO:0000250|UniProtKB:Q64018, ECO:0000269|PubMed:11178872}.
-!- 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:0000250|UniProtKB:Q64018}; Multi-pass membrane
protein {ECO:0000250|UniProtKB:Q64018}. Cell junction, synapse
{ECO:0000250|UniProtKB:Q64018}. Perikaryon
{ECO:0000269|PubMed:11178872}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q64018}. Cell membrane
{ECO:0000269|PubMed:11178872}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P23415, ECO:0000250|UniProtKB:Q64018}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=P57695-1; Sequence=Displayed;
Name=b;
IsoId=P57695-2; Sequence=VSP_021141;
-!- TISSUE SPECIFICITY: Detected on spinal cord neurons (at protein
level). Detected in spinal cord. {ECO:0000269|PubMed:11178872}.
-!- 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 inherited
congenital myoclonus of Poll Hereford calves. It is an autosomal
recessive disease characterized by hyperesthesia and myoclonic
jerks of the skeletal musculature that occur both spontaneously
and in response to sensory stimuli. {ECO:0000269|PubMed:11178872}.
-!- MISCELLANEOUS: The alpha subunit binds strychnine.
{ECO:0000305|PubMed:11178872}.
-!- 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; AF268375; AAG14346.1; -; mRNA.
EMBL; AF268366; AAG41140.1; -; Genomic_DNA.
EMBL; AF268358; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268360; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268361; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268359; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268362; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268364; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268365; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268363; AAG41140.1; JOINED; Genomic_DNA.
EMBL; AF268366; AAG41141.1; -; Genomic_DNA.
EMBL; AF268358; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268360; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268361; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268359; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268362; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268364; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268365; AAG41141.1; JOINED; Genomic_DNA.
EMBL; AF268363; AAG41141.1; JOINED; Genomic_DNA.
RefSeq; NP_776746.1; NM_174321.2. [P57695-1]
UniGene; Bt.5559; -.
ProteinModelPortal; P57695; -.
SMR; P57695; -.
STRING; 9913.ENSBTAP00000019143; -.
PaxDb; P57695; -.
PRIDE; P57695; -.
Ensembl; ENSBTAT00000019143; ENSBTAP00000019143; ENSBTAG00000014395. [P57695-1]
GeneID; 281783; -.
KEGG; bta:281783; -.
CTD; 2741; -.
VGNC; VGNC:29412; GLRA1.
eggNOG; KOG3643; Eukaryota.
eggNOG; ENOG410XPWH; LUCA.
GeneTree; ENSGT00760000118821; -.
HOGENOM; HOG000231336; -.
HOVERGEN; HBG051707; -.
InParanoid; P57695; -.
KO; K05193; -.
OMA; FNFAYGM; -.
OrthoDB; EOG091G0805; -.
TreeFam; TF315453; -.
Reactome; R-BTA-112314; Neurotransmitter receptors and postsynaptic signal transmission.
Proteomes; UP000009136; Chromosome 7.
Bgee; ENSBTAG00000014395; -.
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:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; ISS:UniProtKB.
GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
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; IEA:Ensembl.
GO; GO:0001508; P:action potential; IEA:Ensembl.
GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
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:0006821; P:chloride transport; ISS:UniProtKB.
GO; GO:0060080; P:inhibitory postsynaptic potential; ISS: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:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:Ensembl.
GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IEA:Ensembl.
GO; GO:0097305; P:response to alcohol; ISS:UniProtKB.
GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
GO; GO:0060013; P:righting reflex; IEA:Ensembl.
GO; GO:0001964; P:startle response; ISS:UniProtKB.
GO; GO:0060012; P:synaptic transmission, glycinergic; ISS:UniProtKB.
GO; GO:0007601; P:visual perception; IEA:Ensembl.
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; 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_0000000411.
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:0000255}.
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:11178872}.
/FTId=VSP_021141.
SEQUENCE 457 AA; 52614 MW; 0C60A814C8ADFDDE CRC64;
MYSFNTLRLY LWETIVFFSL AASKEAEAAR SASKPMSPSD 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
QEDEAGEGRF NFSAYGMGPA CLQAKDGISV KGANNSNTTN PPPAPSKSPE EMRKLFIQRA
KKIDKISRIG FPMAFLIFNM FYWIIYKIVR REDVHNQ


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