GBRA4_BOVIN
ID GBRA4_BOVIN Reviewed; 555 AA.
AC P20237; Q08E47;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-4;
DE AltName: Full=GABA(A) receptor subunit alpha-4;
DE Flags: Precursor;
GN Name=GABRA4;
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].
RC TISSUE=Brain;
RX PubMed=2556293; DOI=10.1016/0014-5793(89)81630-8;
RA Ymer S., Draguhn A., Koehler M., Schofield P.R., Seeburg P.H.;
RT "Sequence and expression of a novel GABAA receptor alpha subunit.";
RL FEBS Lett. 258:119-122(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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. GABRA4 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X61456; CAA43696.1; -; mRNA.
DR EMBL; BC123424; AAI23425.1; -; mRNA.
DR PIR; S06838; S06838.
DR RefSeq; NP_776968.1; NM_174543.2.
DR AlphaFoldDB; P20237; -.
DR SMR; P20237; -.
DR STRING; 9913.ENSBTAP00000022141; -.
DR ChEMBL; CHEMBL2094107; -.
DR DrugCentral; P20237; -.
DR PaxDb; P20237; -.
DR Ensembl; ENSBTAT00000068378; ENSBTAP00000063141; ENSBTAG00000016645.
DR GeneID; 282238; -.
DR KEGG; bta:282238; -.
DR CTD; 2557; -.
DR VEuPathDB; HostDB:ENSBTAG00000016645; -.
DR VGNC; VGNC:29193; GABRA4.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000159024; -.
DR HOGENOM; CLU_010920_2_2_1; -.
DR InParanoid; P20237; -.
DR OMA; DANLNMR; -.
DR OrthoDB; 1057372at2759; -.
DR TreeFam; TF315453; -.
DR PRO; PR:P20237; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000016645; Expressed in occipital lobe and 31 other tissues.
DR ExpressionAtlas; P20237; baseline.
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; IPR005434; GABBAa4_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; PR01617; GABAARALPHA4.
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..35
FT /evidence="ECO:0000255"
FT CHAIN 36..555
FT /note="Gamma-aminobutyric acid receptor subunit alpha-4"
FT /id="PRO_0000000440"
FT TOPO_DOM 36..258
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 285..306
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 318..340
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 341..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 525..544
FT /note="Helical"
FT /evidence="ECO:0000305"
FT REGION 354..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 172..186
FT /evidence="ECO:0000250"
FT CONFLICT 308
FT /note="H -> PI (in Ref. 1; CAA43696)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 61547 MW; 03B51F1C27304DD7 CRC64;
MVSAKKVPAI AMSFGVSFAL LHFLCLAACL NESPGQNQKE EKLCPENFTR ILDSLLDGYD
NRLRPGFGGP VTEVKTDIYV TSFGPVSDVE MEYTMDVFFR QTWIDKRLKY DGPIEILRLN
NMMVTKVWTP DTFFRNGKKS VSHNMTAPNK LFRIMRNGTI LYTMRLTISA ECPMRLVDFP
MDGHACPLKF GSYAYPKSEM IYTWTKGPEK SVEVPKESSS LVQYDLIGQT VSSETIKSIT
GEYIVMTVYF HLRRKMGYFM IQTYIPCIMT VILSQVSFWI NKESVPARTV FGITTVLTMT
TLSISARHSL PKVSYATAMD WFIAVCFAFV FSALIEFAAV NYFTNVQMEK AKRKTSKAPQ
EISAAPVLRE KHPETPLQNT NANLSMRKRA NALVHSESDV GSRTDVGNHS SKSSTVVQGS
SEATPQSYLA SSPNPFSRAN AAETISAARA IPSALPSTPS RTGYVPRQVP VGSASTQHVF
GSRLQRIKTT VNSIGTSGKL SATTTPSAPP PSGSGTSKID KYARILFPVT FGAFNMVYWV
VYLSKDTMEK SESLM
