GBRA4_MOUSE
ID GBRA4_MOUSE Reviewed; 552 AA.
AC Q9D6F4;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 04-MAY-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
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; AK013727; BAB28975.1; -; mRNA.
DR CCDS; CCDS39107.1; -.
DR RefSeq; NP_034381.1; NM_010251.2.
DR AlphaFoldDB; Q9D6F4; -.
DR SMR; Q9D6F4; -.
DR BioGRID; 199800; 2.
DR ComplexPortal; CPX-2988; GABA-A receptor, alpha-4/beta-2/delta.
DR ComplexPortal; CPX-2989; GABA-A receptor, alpha-4/beta-3/delta.
DR STRING; 10090.ENSMUSP00000031121; -.
DR ChEMBL; CHEMBL2094133; -.
DR DrugCentral; Q9D6F4; -.
DR GlyConnect; 2323; 6 N-Linked glycans (2 sites).
DR GlyGen; Q9D6F4; 3 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q9D6F4; -.
DR PhosphoSitePlus; Q9D6F4; -.
DR MaxQB; Q9D6F4; -.
DR PaxDb; Q9D6F4; -.
DR PRIDE; Q9D6F4; -.
DR ProteomicsDB; 273420; -.
DR ABCD; Q9D6F4; 1 sequenced antibody.
DR Antibodypedia; 12041; 427 antibodies from 39 providers.
DR DNASU; 14397; -.
DR Ensembl; ENSMUST00000031121; ENSMUSP00000031121; ENSMUSG00000029211.
DR GeneID; 14397; -.
DR KEGG; mmu:14397; -.
DR UCSC; uc008xqy.1; mouse.
DR CTD; 2557; -.
DR MGI; MGI:95616; Gabra4.
DR VEuPathDB; HostDB:ENSMUSG00000029211; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000159024; -.
DR HOGENOM; CLU_010920_1_6_1; -.
DR InParanoid; Q9D6F4; -.
DR OMA; DANLNMR; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; Q9D6F4; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14397; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q9D6F4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D6F4; protein.
DR Bgee; ENSMUSG00000029211; Expressed in lateral geniculate body and 144 other tissues.
DR ExpressionAtlas; Q9D6F4; baseline and differential.
DR Genevisible; Q9D6F4; MM.
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:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
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..552
FT /note="Gamma-aminobutyric acid receptor subunit alpha-4"
FT /id="PRO_0000000442"
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..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..474
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"
SQ SEQUENCE 552 AA; 60878 MW; 213C16C423D7F97B CRC64;
MVSVQKVPAI ALCSGVSLAL LHFLCLAACL 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 KSRTEVGNHS SKTSAVQESS
EATPKAHLAS SPNPFSRANA AETMSAAARG LSSAASPSPH GTLRPASLGS ASTRPAFGSR
LGRIKTTVNT TGAAGNVSAT PPPPAPPPSG SGTSKIDKYA RILFPVTFGA FNMVYWVVYL
SKDTMEKSES LM
