ID GBRA1_CHICK Reviewed; 455 AA.
AC P19150;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 24-JAN-2024, entry version 159.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-1;
DE AltName: Full=GABA(A) receptor subunit alpha-1;
DE Flags: Precursor;
GN Name=GABRA1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Commercial Rhode Island cross; TISSUE=Brain;
RX PubMed=1710013; DOI=10.1016/0169-328x(91)90081-8;
RA Bateson A.N., Harvey R.J., Wisden W., Glencorse T.A., Hicks A.A.,
RA Hunt S.P., Barnard E.A., Darlison M.G.;
RT "The chicken GABAA receptor alpha 1 subunit: cDNA sequence and localization
RT of the corresponding mRNA.";
RL Brain Res. Mol. Brain Res. 9:333-339(1991).
CC -!- FUNCTION: Ligand-gated chloride channel which is a component of the
CC heteropentameric receptor for GABA, the major inhibitory
CC neurotransmitter in the brain (By similarity). Plays an important role
CC in the formation of functional inhibitory GABAergic synapses in
CC addition to mediating synaptic inhibition as a GABA-gated ion channel
CC (By similarity). Functions also as histamine receptor and mediates
CC cellular responses to histamine (By similarity).
CC {ECO:0000250|UniProtKB:P62812, ECO:0000250|UniProtKB:P62813}.
CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines, the
CC neuroanesthetic alphaxalone and pentobarbital (By similarity).
CC Inhibited by the antagonist bicuculline (By similarity).
CC {ECO:0000250|UniProtKB:P14867, ECO:0000250|UniProtKB:P62813}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains. {ECO:0000250|UniProtKB:P14867}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P08219}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P62812}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Brain. {ECO:0000269|PubMed:1710013}.
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000250|UniProtKB:P62812}.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRA1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X54244; CAA38148.1; -; mRNA.
DR PIR; A60033; CHCHA1.
DR RefSeq; NP_989649.1; NM_204318.2.
DR RefSeq; XP_015149123.1; XM_015293637.1.
DR AlphaFoldDB; P19150; -.
DR SMR; P19150; -.
DR STRING; 9031.ENSGALP00000002606; -.
DR GlyCosmos; P19150; 2 sites, No reported glycans.
DR PaxDb; 9031-ENSGALP00000002606; -.
DR Ensembl; ENSGALT00000092358; ENSGALP00000073963; ENSGALG00000001698.
DR Ensembl; ENSGALT00010023495.1; ENSGALP00010013552.1; ENSGALG00010009841.1.
DR Ensembl; ENSGALT00015021250; ENSGALP00015011895; ENSGALG00015008829.
DR GeneID; 374214; -.
DR KEGG; gga:374214; -.
DR CTD; 2554; -.
DR VEuPathDB; HostDB:geneid_374214; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000159136; -.
DR HOGENOM; CLU_010920_2_1_1; -.
DR InParanoid; P19150; -.
DR OMA; YLWAYLF; -.
DR PhylomeDB; P19150; -.
DR TreeFam; TF315453; -.
DR Reactome; R-GGA-977443; GABA receptor activation.
DR PRO; PR:P19150; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000001698; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IBA:GO_Central.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated monoatomic ion channel activity; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR CDD; cd19034; LGIC_ECD_GABAAR_A1; 1.
DR CDD; cd19052; LGIC_TM_GABAAR_alpha; 1.
DR Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR001390; GABAAa_rcpt.
DR InterPro; IPR005431; GABBAa1_rcpt.
DR InterPro; IPR047024; Gabra-1-6_TM.
DR InterPro; IPR047079; GABRA1_ECD.
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 NCBIfam; TIGR00860; LIC; 1.
DR PANTHER; PTHR18945:SF514; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-1; 1.
DR PANTHER; PTHR18945; NEUROTRANSMITTER GATED ION CHANNEL; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR01079; GABAARALPHA.
DR PRINTS; PR01614; GABAARALPHA1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..455
FT /note="Gamma-aminobutyric acid receptor subunit alpha-1"
FT /id="PRO_0000000431"
FT TOPO_DOM 28..251
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 252..273
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 279..300
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 313..334
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 335..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000305"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 166..180
FT /evidence="ECO:0000250"
SQ SEQUENCE 455 AA; 51842 MW; 23AD620C56762E8D CRC64;
MKRLLVLCDC LWAWSLLLNA LTERSYGQTS SQDELKDNTT VFTRILDRLL DGYDNRLRPG
LGERVTEVKT DIFVTSFGPV SDHDMEYTID VFFRQSWKDE RLKFKGPMTV LRLNNLMASK
IWTPDTFFHN GKKSVAHNMT MPNKLLRITE DGTLLYTMRL TVRAECPMHL EDFPMDVHAC
PLKFGSYAYT RAEVVYEWTR EPARSVVVAE DGSRLNQYDL LGQTVDSGIV QSSTGEYVVM
TTHFHLKRKI GYFVIQTYLP CIMTVILSQV SFWLNRESVP ARTVFGVTTV LTMTTLSISA
RNSLPKVAYA TAMDWFIAVC YAFVFSALIE FATVNYFTKR GYAWDGKSVV PEKPKKVKDP
LIKKNNTYTA AATSYTPNIA RDPGLATIAK SATIEPKEVK PETKPAEPKK TFNSVSKIDR
LSRIAFPLLF GIFNLVYWAT YLNREPQLKA PTPHQ
//
