GBRA1_BOVIN
ID GBRA1_BOVIN Reviewed; 456 AA.
AC P08219; Q29RI5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 177.
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 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 [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=3037384; DOI=10.1038/328221a0;
RA Schofield P.R., Darlison M.G., Fujita N., Burt D.R., Stephenson F.A.,
RA Rodriguez H., Rhee L.M., Ramachandran J., Reale V., Glencorse T.A.,
RA Seeburg P.H., Barnard E.A.;
RT "Sequence and functional expression of the GABA A receptor shows a ligand-
RT gated receptor super-family.";
RL Nature 328:221-227(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 28-42; 351-367 AND 440-456.
RX PubMed=2557827; DOI=10.1042/bj2640199;
RA Stephenson F.A., Duggan M.J.;
RT "Mapping the benzodiazepine photoaffinity-labelling site with sequence-
RT specific gamma-aminobutyric acidA-receptor antibodies.";
RL Biochem. J. 264:199-206(1989).
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 (PubMed:3037384). 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). The gamma2 subunit is necessary but not sufficient for
CC a rapid formation of active synaptic contacts and the synaptogenic
CC effect of this subunit is influenced by the type of alpha and beta
CC subunits present in the receptor pentamer (By similarity). The
CC alpha1/beta2/gamma2 receptor and the alpha1/beta3/gamma2 receptor
CC exhibit synaptogenic activity (By similarity). GABRA1-mediated
CC plasticity in the orbitofrontal cortex regulates context-dependent
CC action selection (By similarity). Functions also as histamine receptor
CC and mediates cellular responses to histamine (By similarity).
CC {ECO:0000250|UniProtKB:P62812, ECO:0000250|UniProtKB:P62813,
CC ECO:0000269|PubMed:3037384}.
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 (PubMed:3037384). Interacts with UBQLN1 (By
CC similarity). Interacts with TRAK1 (By similarity). Interacts with
CC KIF21B (By similarity). Identified in a complex of 720 kDa composed of
CC LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity).
CC Interacts with LHFPL4 (By similarity). Interacts with NLGN2 (By
CC similarity). Interacts with SHISA7; interaction leads to the regulation
CC of GABA(A) receptor trafficking, channel deactivation kinetics and
CC pharmacology (By similarity). {ECO:0000250|UniProtKB:P14867,
CC ECO:0000250|UniProtKB:P62812, ECO:0000250|UniProtKB:P62813,
CC ECO:0000269|PubMed:3037384}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:3037384}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:3037384}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P62813}.
CC -!- TISSUE SPECIFICITY: Cerebellar granule cells, Purkinje cells and
CC stellate/basket cells.
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000250|UniProtKB:P62812}.
CC -!- PTM: Glycosylated. {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; X05717; CAA29189.1; -; mRNA.
DR EMBL; BC114156; AAI14157.1; -; mRNA.
DR PIR; A27142; A27142.
DR RefSeq; NP_001178048.1; NM_001191119.3.
DR RefSeq; XP_010805879.1; XM_010807577.2.
DR AlphaFoldDB; P08219; -.
DR SMR; P08219; -.
DR STRING; 9913.ENSBTAP00000009483; -.
DR BindingDB; P08219; -.
DR ChEMBL; CHEMBL4680049; -.
DR DrugCentral; P08219; -.
DR PaxDb; P08219; -.
DR PRIDE; P08219; -.
DR Ensembl; ENSBTAT00000009483; ENSBTAP00000009483; ENSBTAG00000030286.
DR GeneID; 780973; -.
DR KEGG; bta:780973; -.
DR CTD; 2554; -.
DR VEuPathDB; HostDB:ENSBTAG00000030286; -.
DR VGNC; VGNC:29191; GABRA1.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000159136; -.
DR HOGENOM; CLU_010920_2_1_1; -.
DR InParanoid; P08219; -.
DR OMA; DICTIQY; -.
DR OrthoDB; 1057372at2759; -.
DR TreeFam; TF315453; -.
DR Reactome; R-BTA-977443; GABA receptor activation.
DR PRO; PR:P08219; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000030286; Expressed in occipital lobe and 50 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0005231; F:excitatory extracellular ligand-gated ion channel activity; 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 ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
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:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IBA:GO_Central.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR001390; GABAAa_rcpt.
DR InterPro; IPR005431; GABBAa1_rcpt.
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; PR01079; GABAARALPHA.
DR PRINTS; PR01614; GABAARALPHA1.
DR PRINTS; PR00253; GABAARECEPTR.
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 Cell membrane; Chloride; Chloride channel; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
KW 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..456
FT /note="Gamma-aminobutyric acid receptor subunit alpha-1"
FT /id="PRO_0000000427"
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..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 422..443
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 456 AA; 51856 MW; AFD4AA144B382CC2 CRC64;
MKKSPGLSDY LWAWTLFLST LTGRSYGQPS LQDELKDNTT VFTRILDRLL DGYDNRLRPG
LGERVTEVKT DIFVTSFGPV SDHDMEYTID VFFRQSWKDE RLKFKGPMTV LRLNNLMASK
IWTPDTFFHN GKKSVAHNMT MPNKLLRITE DGTLLYTMRL TVRAECPMHL EDFPMDAHAC
PLKFGSYAYT RAEVVYEWTR EPARSVVVAE DGSRLNQYDL LGQTVDSGIV QSSTGEYVVM
TTHFHLKRKI GYFVIQTYLP CIMTVILSQV SFWLNRESVP ARTVFGVTTV LTMTTLSISA
RNSLPKVAYA TAMDWFIAVC YAFVFSALIE FATVNYFTKR GYAWDGKSVV PEKPKKVKDP
LIKKNNTYAP TATSYTPNLA RGDPGLATIA KSATIEPKEV KPETKPPEPK KTFNSVSKID
RLSRIAFPLL FGIFNLVYWA TYLNREPQLK APTPHQ
