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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
 
 
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