GLRA1_BOVIN
ID GLRA1_BOVIN Reviewed; 457 AA.
AC P57695; Q9GKE9; Q9GKF0;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glycine receptor subunit alpha-1;
DE AltName: Full=Glycine receptor 48 kDa subunit;
DE AltName: Full=Glycine receptor strychnine-binding subunit;
DE Flags: Precursor;
GN Name=GLRA1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), DISEASE,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=11178872; DOI=10.1006/mcne.2000.0934;
RA Pierce K.D., Handford C.A., Morris R., Vafa B., Dennis J.A., Healy P.J.,
RA Schofield P.R.;
RT "A nonsense mutation in the alpha1 subunit of the inhibitory glycine
RT receptor associated with bovine myoclonus.";
RL Mol. Cell. Neurosci. 17:354-363(2001).
CC -!- FUNCTION: Glycine receptors are ligand-gated chloride channels. Channel
CC opening is triggered by extracellular glycine. Channel opening is also
CC triggered by taurine and beta-alanine. Channel characteristics depend
CC on the subunit composition; heteropentameric channels are activated by
CC lower glycine levels and display faster desensitization (By
CC similarity). Plays an important role in the down-regulation of neuronal
CC excitability (PubMed:11178872). Contributes to the generation of
CC inhibitory postsynaptic currents. Channel activity is potentiated by
CC ethanol (By similarity). Potentiation of channel activity by
CC intoxicating levels of ethanol contribute to the sedative effects of
CC ethanol (By similarity). {ECO:0000250|UniProtKB:P23415,
CC ECO:0000250|UniProtKB:Q64018, ECO:0000269|PubMed:11178872}.
CC -!- SUBUNIT: Homopentamer (in vitro). Interacts with GLRB to form
CC heteropentameric channels; this is probably the predominant form in
CC vivo. Heteropentamer composed of two GLRA1 and three GLRB.
CC Heteropentamer composed of three GLRA1 and two GLRB. Both homopentamers
CC and heteropentamers form functional ion channels, but their
CC characteristics are subtly different. {ECO:0000250|UniProtKB:P23415}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:Q64018}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q64018}. Synapse {ECO:0000250|UniProtKB:Q64018}.
CC Perikaryon {ECO:0000269|PubMed:11178872}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q64018}. Cell membrane
CC {ECO:0000269|PubMed:11178872}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P23415, ECO:0000250|UniProtKB:Q64018}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P57695-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P57695-2; Sequence=VSP_021141;
CC -!- TISSUE SPECIFICITY: Detected on spinal cord neurons (at protein level).
CC Detected in spinal cord. {ECO:0000269|PubMed:11178872}.
CC -!- DOMAIN: The channel pore is formed by pentameric assembly of the second
CC transmembrane domain from all five subunits. Channel opening is
CC effected by an outward rotation of the transmembrane domains that
CC increases the diameter of the pore. {ECO:0000250|UniProtKB:O93430}.
CC -!- DISEASE: Note=Defects in GLRA1 are the cause of inherited congenital
CC myoclonus of Poll Hereford calves. It is an autosomal recessive disease
CC characterized by hyperesthesia and myoclonic jerks of the skeletal
CC musculature that occur both spontaneously and in response to sensory
CC stimuli. {ECO:0000269|PubMed:11178872}.
CC -!- MISCELLANEOUS: The alpha subunit binds strychnine.
CC {ECO:0000305|PubMed:11178872}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Glycine receptor (TC 1.A.9.3) subfamily. GLRA1 sub-subfamily.
CC {ECO:0000305}.
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DR EMBL; AF268375; AAG14346.1; -; mRNA.
DR EMBL; AF268366; AAG41140.1; -; Genomic_DNA.
DR EMBL; AF268358; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268360; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268361; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268359; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268362; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268364; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268365; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268363; AAG41140.1; JOINED; Genomic_DNA.
DR EMBL; AF268366; AAG41141.1; -; Genomic_DNA.
DR EMBL; AF268358; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268360; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268361; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268359; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268362; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268364; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268365; AAG41141.1; JOINED; Genomic_DNA.
DR EMBL; AF268363; AAG41141.1; JOINED; Genomic_DNA.
DR RefSeq; NP_776746.1; NM_174321.2. [P57695-1]
DR AlphaFoldDB; P57695; -.
DR BMRB; P57695; -.
DR SMR; P57695; -.
DR STRING; 9913.ENSBTAP00000019143; -.
DR PaxDb; P57695; -.
DR Ensembl; ENSBTAT00000019143; ENSBTAP00000019143; ENSBTAG00000014395. [P57695-1]
DR GeneID; 281783; -.
DR KEGG; bta:281783; -.
DR CTD; 2741; -.
DR VEuPathDB; HostDB:ENSBTAG00000014395; -.
DR eggNOG; KOG3644; Eukaryota.
DR GeneTree; ENSGT00940000159047; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P57695; -.
DR OMA; FNFAYGM; -.
DR OrthoDB; 614790at2759; -.
DR TreeFam; TF315453; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014395; Expressed in oocyte and 10 other tissues.
DR ExpressionAtlas; P57695; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl.
DR GO; GO:0060077; C:inhibitory synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016934; F:extracellularly glycine-gated chloride channel activity; ISS:UniProtKB.
DR GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0030977; F:taurine binding; ISS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0007340; P:acrosome reaction; IEA:Ensembl.
DR GO; GO:0007628; P:adult walking behavior; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR GO; GO:0071361; P:cellular response to ethanol; ISS:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0006821; P:chloride transport; ISS:UniProtKB.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR GO; GO:0051970; P:negative regulation of transmission of nerve impulse; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0050884; P:neuromuscular process controlling posture; IEA:Ensembl.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR GO; GO:2000344; P:positive regulation of acrosome reaction; IEA:Ensembl.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IEA:Ensembl.
DR GO; GO:0097305; P:response to alcohol; ISS:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IBA:GO_Central.
DR GO; GO:0060013; P:righting reflex; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0001964; P:startle response; ISS:UniProtKB.
DR GO; GO:0060012; P:synaptic transmission, glycinergic; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR008127; Glycine_rcpt_A.
DR InterPro; IPR008128; Glycine_rcpt_A1.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR01673; GLYRALPHA.
DR PRINTS; PR01674; GLYRALPHA1.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Chloride;
KW Chloride channel; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Metal-binding;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000250|UniProtKB:P07727"
FT CHAIN 29..457
FT /note="Glycine receptor subunit alpha-1"
FT /id="PRO_0000000411"
FT TOPO_DOM 29..250
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 251..272
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 273..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 278..298
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 299..309
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 310..330
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 331..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TRANSMEM 426..446
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT TOPO_DOM 447..457
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT REGION 391..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT BINDING 230..235
FT /ligand="strychnine"
FT /ligand_id="ChEBI:CHEBI:90700"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT SITE 289
FT /note="Important for obstruction of the ion pore in the
FT closed conformation"
FT /evidence="ECO:0000250|UniProtKB:O93430"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 166..180
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT DISULFID 226..237
FT /evidence="ECO:0000250|UniProtKB:P23415"
FT VAR_SEQ 354..361
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:11178872"
FT /id="VSP_021141"
SQ 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
