GBRA6_MOUSE
ID GBRA6_MOUSE Reviewed; 453 AA.
AC P16305; Q5SUU5; Q9R0V3; Q9R0V4; Q9R0V5;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 188.
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; Synonyms=Gabra-6;
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 [MRNA] (ISOFORM 2).
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=2167378; DOI=10.1016/0022-2836(90)90276-r;
RA Kato K.;
RT "Novel GABAA receptor alpha subunit is expressed only in cerebellar granule
RT cells.";
RL J. Mol. Biol. 214:619-624(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=129/Sv;
RA Glencorse T.A., Montgomery K.I., Livingston D., Davies R.W.;
RT "Characterization of the murine GABAA receptor alpha 6 subunit gene.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Cerebellum;
RA Buck K.J., Lischka T.R.;
RT "Detection and ethanol regulation of two forms of the GABA-A receptor
RT alpha-6 subunit in DBA/2J and C57BL/6J mice.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH UBQLN1.
RX PubMed=11528422; DOI=10.1038/nn0901-908;
RA Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA Wisden W., Triller A., Smart T.G., Moss S.J.;
RT "GABA(A) receptor cell surface number and subunit stability are regulated
RT by the ubiquitin-like protein Plic-1.";
RL Nat. Neurosci. 4:908-916(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Binds UBQLN1.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane; Multi-pass membrane
CC protein. Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P16305-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P16305-2; Sequence=VSP_000086;
CC Name=3;
CC IsoId=P16305-3; Sequence=VSP_000085;
CC Name=4;
CC IsoId=P16305-4; Sequence=VSP_000085, VSP_000086;
CC -!- TISSUE SPECIFICITY: Only found in cerebellar granule cells.
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; X51986; CAA36244.1; -; mRNA.
DR EMBL; U77411; AAD52001.1; -; Genomic_DNA.
DR EMBL; U77409; AAD52001.1; JOINED; Genomic_DNA.
DR EMBL; U77410; AAD52001.1; JOINED; Genomic_DNA.
DR EMBL; U77411; AAD52002.1; -; Genomic_DNA.
DR EMBL; U77409; AAD52002.1; JOINED; Genomic_DNA.
DR EMBL; U77410; AAD52002.1; JOINED; Genomic_DNA.
DR EMBL; U77411; AAD52003.1; -; Genomic_DNA.
DR EMBL; U77409; AAD52003.1; JOINED; Genomic_DNA.
DR EMBL; U77410; AAD52003.1; JOINED; Genomic_DNA.
DR EMBL; U77411; AAD52004.1; -; Genomic_DNA.
DR EMBL; U77409; AAD52004.1; JOINED; Genomic_DNA.
DR EMBL; U77410; AAD52004.1; JOINED; Genomic_DNA.
DR EMBL; AF256197; AAG28024.1; -; mRNA.
DR EMBL; AF256198; AAG28025.1; -; mRNA.
DR EMBL; AK135145; BAE22438.1; -; mRNA.
DR EMBL; AL645823; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC145158; AAI45159.1; -; mRNA.
DR EMBL; BC145702; AAI45703.1; -; mRNA.
DR CCDS; CCDS24554.1; -. [P16305-2]
DR CCDS; CCDS48769.1; -. [P16305-1]
DR CCDS; CCDS88145.1; -. [P16305-3]
DR PIR; S11396; S11396.
DR RefSeq; NP_001093111.1; NM_001099641.2. [P16305-1]
DR RefSeq; NP_032094.2; NM_008068.3. [P16305-2]
DR RefSeq; XP_006532260.1; XM_006532197.3.
DR AlphaFoldDB; P16305; -.
DR SMR; P16305; -.
DR ComplexPortal; CPX-2981; GABA-A receptor, alpha-6/beta-3/gamma-2.
DR ComplexPortal; CPX-2986; GABA-A receptor, alpha-6/beta-3/delta.
DR ComplexPortal; CPX-2987; GABA-A receptor, alpha-6/beta-2/delta.
DR STRING; 10090.ENSMUSP00000126114; -.
DR ChEMBL; CHEMBL2094133; -.
DR DrugCentral; P16305; -.
DR GlyConnect; 2437; 2 N-Linked glycans (2 sites). [P16305-3]
DR GlyGen; P16305; 3 sites.
DR iPTMnet; P16305; -.
DR PhosphoSitePlus; P16305; -.
DR MaxQB; P16305; -.
DR PaxDb; P16305; -.
DR PeptideAtlas; P16305; -.
DR PRIDE; P16305; -.
DR ProteomicsDB; 273421; -. [P16305-1]
DR ProteomicsDB; 273422; -. [P16305-2]
DR ProteomicsDB; 273423; -. [P16305-3]
DR ProteomicsDB; 273424; -. [P16305-4]
DR ABCD; P16305; 2 sequenced antibodies.
DR Antibodypedia; 28560; 212 antibodies from 33 providers.
DR DNASU; 14399; -.
DR Ensembl; ENSMUST00000020703; ENSMUSP00000020703; ENSMUSG00000020428. [P16305-2]
DR Ensembl; ENSMUST00000109286; ENSMUSP00000104909; ENSMUSG00000020428. [P16305-3]
DR Ensembl; ENSMUST00000155218; ENSMUSP00000126114; ENSMUSG00000020428. [P16305-1]
DR GeneID; 14399; -.
DR KEGG; mmu:14399; -.
DR UCSC; uc007img.2; mouse. [P16305-2]
DR UCSC; uc007imh.2; mouse. [P16305-1]
DR CTD; 2559; -.
DR MGI; MGI:95618; Gabra6.
DR VEuPathDB; HostDB:ENSMUSG00000020428; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000156722; -.
DR HOGENOM; CLU_010920_2_2_1; -.
DR InParanoid; P16305; -.
DR OMA; YIILWVE; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; P16305; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14399; 4 hits in 71 CRISPR screens.
DR PRO; PR:P16305; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P16305; protein.
DR Bgee; ENSMUSG00000020428; Expressed in cerebellum lobe and 34 other tissues.
DR Genevisible; P16305; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0099192; C:cerebellar Golgi cell to granule cell synapse; IDA:SynGO.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
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:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0008503; F:benzodiazepine receptor activity; ISO:MGI.
DR GO; GO:0050809; F:diazepam binding; ISO:MGI.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; ISO:MGI.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; ISO:MGI.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
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; ISO:MGI.
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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Chloride; Chloride channel;
KW Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Ligand-gated ion channel; Membrane; Phosphoprotein;
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..453
FT /note="Gamma-aminobutyric acid receptor subunit alpha-6"
FT /id="PRO_0000000448"
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 301..324
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 325..419
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 420..441
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 375
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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"
FT VAR_SEQ 1..13
FT /note="MVLLLPWLFIILW -> MRNMKDLEDFSR (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_000085"
FT VAR_SEQ 76..85
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:2167378"
FT /id="VSP_000086"
FT CONFLICT 357
FT /note="Q -> E (in Ref. 1; CAA36244, 2; AAD52001/AAD52002/
FT AAD52003/AAD52004 and 3; AAG28024/AAG28025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 51106 MW; ACCDF38AE8D4695D CRC64;
MVLLLPWLFI ILWLENAQAQ LEDEGNFYSE NVSRILDNLL EGYDNRLRPG FGGAVTEVKT
DIYVTSFGPV SDVEMEYTMD VFFRQTWTDE RLKFKGPAEI LSLNNLMVSK IWTPDTFFRN
GKKSIAHNMT TPNKLFRLMQ NGTILYTMRL TINADCPMRL VNFPMDGHAC PLKFGSYAYP
KTEIIYTWKK GPLYSVEVPE ESSSLLQYDL IGQTVSSETI KSNTGEYVIM TVYFHLQRKM
GYFMIQIYTP CIMTVILSQV SFWINKESVP ARTVFGITTV LTMTTLSISA RHSLPKVSYA
TAMDWFIAVC FAFVFSALIE FAAVNYFTNL QSQKAERQAQ TAATPPVAKS KASESLQAEI
VVHSDSKYHL KKRISSLTLP IVPSSEASKA LSRTPILKST PVSPPLLLPA TGGTSKIDQY
SRILFPVAFA GFNLVYWIVY LSKDTMEVSS TVE
