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GBRA5_MOUSE
ID   GBRA5_MOUSE             Reviewed;         463 AA.
AC   Q8BHJ7;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-5;
DE   AltName: Full=GABA(A) receptor subunit alpha-5;
DE   Flags: Precursor;
GN   Name=Gabra5;
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, and Hypothalamus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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).
CC   -!- FUNCTION: Ligand-gated chloride channel subunit which is a component of
CC       the heteropentameric receptor for GABA, the major inhibitory
CC       neurotransmitter in the brain. May be involved in GABA-A receptor
CC       assembly, and GABA-A receptor immobilization and accumulation by
CC       gephyrin at the synapse. {ECO:0000250|UniProtKB:P31644}.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A) receptor
CC       chains: alpha, beta, gamma, delta, and rho (By similarity).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8BHJ7; Q5WQV5; Xeno; NbExp=4; IntAct=EBI-8069233, EBI-8069271;
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:P31644}; Multi-pass membrane protein. Cell
CC       membrane {ECO:0000250|UniProtKB:P31644}; 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. GABRA5 sub-
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AK038476; BAC30012.1; -; mRNA.
DR   EMBL; AK083185; BAC38799.1; -; mRNA.
DR   EMBL; BC062112; AAH62112.1; -; mRNA.
DR   CCDS; CCDS21322.1; -.
DR   RefSeq; NP_795916.1; NM_176942.4.
DR   RefSeq; XP_006540619.1; XM_006540556.3.
DR   RefSeq; XP_006540620.1; XM_006540557.3.
DR   RefSeq; XP_006540621.1; XM_006540558.2.
DR   RefSeq; XP_006540622.1; XM_006540559.3.
DR   RefSeq; XP_006540623.1; XM_006540560.3.
DR   AlphaFoldDB; Q8BHJ7; -.
DR   SMR; Q8BHJ7; -.
DR   BioGRID; 225988; 1.
DR   ComplexPortal; CPX-2984; GABA-A receptor, alpha-5/beta-3/gamma-2.
DR   IntAct; Q8BHJ7; 1.
DR   MINT; Q8BHJ7; -.
DR   STRING; 10090.ENSMUSP00000063276; -.
DR   ChEMBL; CHEMBL2304; -.
DR   DrugCentral; Q8BHJ7; -.
DR   GlyConnect; 2324; 6 N-Linked glycans (1 site).
DR   GlyGen; Q8BHJ7; 4 sites, 6 N-linked glycans (1 site).
DR   PhosphoSitePlus; Q8BHJ7; -.
DR   PaxDb; Q8BHJ7; -.
DR   PeptideAtlas; Q8BHJ7; -.
DR   PRIDE; Q8BHJ7; -.
DR   ProteomicsDB; 268849; -.
DR   ABCD; Q8BHJ7; 1 sequenced antibody.
DR   Antibodypedia; 22325; 378 antibodies from 31 providers.
DR   DNASU; 110886; -.
DR   Ensembl; ENSMUST00000068456; ENSMUSP00000063276; ENSMUSG00000055078.
DR   Ensembl; ENSMUST00000206382; ENSMUSP00000146238; ENSMUSG00000055078.
DR   Ensembl; ENSMUST00000206734; ENSMUSP00000145685; ENSMUSG00000055078.
DR   GeneID; 110886; -.
DR   KEGG; mmu:110886; -.
DR   UCSC; uc009heb.1; mouse.
DR   CTD; 2558; -.
DR   MGI; MGI:95617; Gabra5.
DR   VEuPathDB; HostDB:ENSMUSG00000055078; -.
DR   eggNOG; KOG3642; Eukaryota.
DR   GeneTree; ENSGT00940000156234; -.
DR   HOGENOM; CLU_010920_2_1_1; -.
DR   InParanoid; Q8BHJ7; -.
DR   OMA; DSKMSNM; -.
DR   OrthoDB; 1057372at2759; -.
DR   PhylomeDB; Q8BHJ7; -.
DR   TreeFam; TF315453; -.
DR   Reactome; R-MMU-977443; GABA receptor activation.
DR   BioGRID-ORCS; 110886; 0 hits in 73 CRISPR screens.
DR   ChiTaRS; Gabra5; mouse.
DR   PRO; PR:Q8BHJ7; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q8BHJ7; protein.
DR   Bgee; ENSMUSG00000055078; Expressed in hippocampal field and 78 other tissues.
DR   Genevisible; Q8BHJ7; MM.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; IDA: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:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; ISO:MGI.
DR   GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR   GO; GO:0099056; C:integral component of presynaptic 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:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR   GO; GO:0043235; C:receptor complex; ISO:MGI.
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:0050811; F:GABA receptor binding; ISO:MGI.
DR   GO; GO:0004890; F:GABA-A receptor activity; ISO:MGI.
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:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR   GO; GO:1902476; P:chloride transmembrane transport; IBA:GO_Central.
DR   GO; GO:0090102; P:cochlea development; IMP:DFLAT.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IBA:GO_Central.
DR   GO; GO:0060119; P:inner ear receptor cell development; IMP:DFLAT.
DR   GO; GO:0060384; P:innervation; IMP:DFLAT.
DR   GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:DFLAT.
DR   GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR   GO; GO:0048666; P:neuron development; IMP:DFLAT.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IMP:DFLAT.
DR   GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:DFLAT.
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; IPR005435; GABBAa5_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; PR01618; GABAARALPHA5.
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   Cell membrane; Chloride; Chloride channel; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
KW   Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW   Synapse; Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..463
FT                   /note="Gamma-aminobutyric acid receptor subunit alpha-5"
FT                   /id="PRO_0000000445"
FT   TOPO_DOM        26..259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        342..428
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          387..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        45
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        173..187
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        355
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:P31644"
SQ   SEQUENCE   463 AA;  52274 MW;  12C677403D326378 CRC64;
     MDNGMLSRFI MTQTLLVFCI SMTLSSHFGF SQMPTSSVQD ETNDNITIFT RILDGLLDGY
     DNRLRPGLGE RITQVRTDIY VTSFGPVSDT EMEYTIDVFF RQSWKDERLR FKGPMQRLPL
     NNLLASKIWT PDTFFHNGKK SIAHNMTTPN KLLRLEDDGT LLYTMRLTIS AECPMQLEDF
     PMDAHACPLK FGSYAYPNSE VVYVWTNGST KSVVVAEDGS RLNQYHLMGQ TVGTENISTS
     TGEYTIMTAH FHLKRKIGYF VIQTYLPCIM TVILSQVSFW LNRESVPART VFGVTTVLTM
     TTLSISARNS LPKVAYATAM DWFIAVCYAF VFSALIEFAT VNYFTKRGWA WDGKKALEAA
     KIKKKERELI LNKSTNAFTT GKLTHPPNIP KEQPPAGTAN APTVSIKASE EKTAESKKTY
     NSISKIDKMS RIVFPILFGT FNLVYWATYL NREPVIKGAT SPK
 
 
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