ID   GBRA4_RAT               Reviewed;         552 AA.
AC   P28471;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   24-JAN-2024, entry version 171.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1655526; DOI=10.1016/0014-5793(91)81076-k;
RA   Wisden W., Herb A., Wieland H., Keinaenen K., Lueddens H., Seeburg P.H.;
RT   "Cloning, pharmacological characteristics and expression pattern of the rat
RT   GABAA receptor alpha 4 subunit.";
RL   FEBS Lett. 289:227-230(1991).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-144, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=24090084; DOI=10.1021/pr400783j;
RA   Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA   Graham M.E., Packer N.H., Cordwell S.J.;
RT   "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT   heterogeneity.";
RL   J. Proteome Res. 12:5791-5800(2013).
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; L08493; AAC42032.1; -; Genomic_DNA.
DR   EMBL; S55933; AAB19902.1; -; mRNA.
DR   PIR; S17551; S17551.
DR   RefSeq; NP_542154.3; NM_080587.3.
DR   AlphaFoldDB; P28471; -.
DR   SMR; P28471; -.
DR   ComplexPortal; CPX-280; GABA-A receptor, alpha-4/beta-3/delta.
DR   ComplexPortal; CPX-408; GABA-A receptor, alpha-4/beta-2/delta.
DR   CORUM; P28471; -.
DR   IntAct; P28471; 2.
DR   STRING; 10116.ENSRNOP00000003191; -.
DR   BindingDB; P28471; -.
DR   ChEMBL; CHEMBL292; -.
DR   DrugCentral; P28471; -.
DR   GuidetoPHARMACOLOGY; 407; -.
DR   GlyCosmos; P28471; 3 sites, 2 glycans.
DR   GlyGen; P28471; 3 sites, 2 N-linked glycans (1 site).
DR   iPTMnet; P28471; -.
DR   PhosphoSitePlus; P28471; -.
DR   PaxDb; 10116-ENSRNOP00000003191; -.
DR   ABCD; P28471; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000003191.7; ENSRNOP00000003191.5; ENSRNOG00000002336.7.
DR   GeneID; 140675; -.
DR   KEGG; rno:140675; -.
DR   UCSC; RGD:621670; rat.
DR   AGR; RGD:621670; -.
DR   CTD; 2557; -.
DR   RGD; 621670; Gabra4.
DR   eggNOG; KOG3642; Eukaryota.
DR   GeneTree; ENSGT00940000159024; -.
DR   HOGENOM; CLU_010920_1_6_1; -.
DR   InParanoid; P28471; -.
DR   OMA; FFCLTTC; -.
DR   OrthoDB; 4265336at2759; -.
DR   Reactome; R-RNO-977443; GABA receptor activation.
DR   PRO; PR:P28471; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002336; Expressed in frontal cortex and 3 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; IPI:ComplexPortal.
DR   GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR   GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0099634; C:postsynaptic specialization membrane; IDA:SynGO.
DR   GO; GO:0045202; C:synapse; IBA:GO_Central.
DR   GO; GO:0004890; F:GABA-A receptor activity; TAS:RGD.
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:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR   GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD.
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; cd19037; LGIC_ECD_GABAAR_A4; 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; IPR005434; GABBAa4_rcpt.
DR   InterPro; IPR047024; Gabra-1-6_TM.
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:SF393; GAMMA-AMINOBUTYRIC ACID RECEPTOR SUBUNIT ALPHA-4; 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; PR01617; GABAARALPHA4.
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.
DR   Genevisible; P28471; RN.
PE   1: Evidence at protein 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..552
FT                   /note="Gamma-aminobutyric acid receptor subunit alpha-4"
FT                   /id="PRO_0000000443"
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..521
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        522..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000305"
FT   REGION          353..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..465
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:0007744|PubMed:24090084"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        172..186
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   552 AA;  60951 MW;  3823335C3554115D CRC64;
     MVSVQKVPAI VLCSGVSLAL LHVLCLATCL NESPGQNSKD 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 NYFTNIQMQK AKKKISKPPP
     EVPAAPVLKE KHTETSLQNT HANLNMRKRT NALVHSESDV NSRTEVGNHS SKTTAAQESS
     ETTPKAHLAS SPNPFSRANA AETISAAARG LSSAASPSPH GTLQPAPLRS ASARPAFGAR
     LGRIKTTVNT TGVPGNVSAT PPPSAPPPSG SGTSKIDKYA RILFPVTFGA FNMVYWVVYL
     SKDTMEKSES LM
//