GBRA6_CHICK
ID GBRA6_CHICK Reviewed; 465 AA.
AC Q90845;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-6;
DE AltName: Full=GABA(A) receptor subunit alpha-6;
DE Flags: Precursor;
GN Name=GABRA6;
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].
RC TISSUE=Embryonic brain;
RX PubMed=8780005; DOI=10.1046/j.1471-4159.1996.66051810.x;
RA Bahn S., Harvey R.J., Darlison M.G., Wisden W.;
RT "Conservation of gamma-aminobutyric acid type A receptor alpha 6 subunit
RT gene expression in cerebellar granule cells.";
RL J. Neurochem. 66:1810-1818(1996).
CC -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the vertebrate
CC brain, mediates neuronal inhibition by binding to the
CC GABA/benzodiazepine receptor and opening an integral chloride channel.
CC -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC chains: alpha, beta, gamma, delta, and rho.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
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. GABRA6 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X94343; CAA64069.1; -; mRNA.
DR RefSeq; NP_990389.1; NM_205058.1.
DR AlphaFoldDB; Q90845; -.
DR SMR; Q90845; -.
DR STRING; 9031.ENSGALP00000002598; -.
DR PaxDb; Q90845; -.
DR Ensembl; ENSGALT00000002601; ENSGALP00000002598; ENSGALG00000001695.
DR GeneID; 395931; -.
DR KEGG; gga:395931; -.
DR CTD; 2559; -.
DR VEuPathDB; HostDB:geneid_395931; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000156722; -.
DR HOGENOM; CLU_010920_2_2_1; -.
DR InParanoid; Q90845; -.
DR OMA; YIILWVE; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; Q90845; -.
DR TreeFam; TF315453; -.
DR Reactome; R-GGA-977443; GABA receptor activation.
DR PRO; PR:Q90845; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000001695; Expressed in cerebellum.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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; IBA:GO_Central.
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: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; IPR005436; GABBAa6_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; PR01619; GABAARALPHA6.
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 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..19
FT /evidence="ECO:0000255"
FT CHAIN 20..465
FT /note="Gamma-aminobutyric acid receptor subunit alpha-6"
FT /id="PRO_0000000450"
FT TOPO_DOM 20..242
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..290
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 325..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 422..443
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 392..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..414
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..170
FT /evidence="ECO:0000250"
SQ SEQUENCE 465 AA; 51718 MW; 969061807FBC0D09 CRC64;
MALLIAWVCV AVSIEKALGG QGDGGDLYSE NITRILDKLL DGYDNRLRPG FGGAVTEVKT
DIYVTSFGPV SDVEMEYTMD VFFRQTWTDE RLKFGGPTEI LRLNNLMVSK IWTPDTFFRN
GKKSIAHNMT TPNKLFRIMQ NGTILYTMRL TINADCPMRL VNFPMDGHAC PLKFGSYAYP
KSEIIYTWKK GPLHSVEVPQ ESSSLLQYDL IGQTVSSETI KSNTGEYVIM TVYFHLQRKM
GYFMIQIYTP CIMTVILSQV SFWINKESVP ARTVFGITTV LTMTTLSISA RHSLPKVSYA
TAMDWFIAVC FAFVFSALIE FAAVNYFTNL QTQRAMRKAA RAAALAAALS AATVPAEDEI
VSHSDSNCNL KKRVNSVTSQ ADQSPEASIV SNSASQCQPV SAPPPAPPAP PPVGGTSKID
QYSRILFPVA FAGFNLVYWV VYLSKDTMEF FEPTAMHLRN DHQSN
