GBRB1_MOUSE
ID GBRB1_MOUSE Reviewed; 474 AA.
AC P50571;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-1;
DE AltName: Full=GABA(A) receptor subunit beta-1;
DE Flags: Precursor;
GN Name=Gabrb1;
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].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX PubMed=7893750; DOI=10.1016/0167-4781(95)00009-6;
RA Kamatchi G.L., Kofuji P., Wang J.B., Fernando J.C., Liu Z., Mathura J.R.,
RA Burt D.R.;
RT "GABAA receptor beta 1, beta 2, and beta 3 subunits: comparisons in DBA/2J
RT and C57BL/6J mice.";
RL Biochim. Biophys. Acta 1261:134-142(1995).
RN [2]
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 [3]
RP INTERACTION WITH KCTD8; KCTD12; KCTD12B AND KCTD16, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20400944; DOI=10.1038/nature08964;
RA Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA Bettler B.;
RT "Native GABA(B) receptors are heteromultimers with a family of auxiliary
RT subunits.";
RL Nature 465:231-235(2010).
CC -!- FUNCTION: Component of the heteropentameric receptor for GABA, the
CC major inhibitory neurotransmitter in the vertebrate brain. Functions
CC also as histamine receptor and mediates cellular responses to histamine
CC (By similarity). Functions as receptor for diazepines and various
CC anesthetics, such as pentobarbital; these are bound at a separate
CC allosteric effector binding site. Functions as ligand-gated chloride
CC channel. {ECO:0000250, ECO:0000269|PubMed:20400944}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains. Binds UBQLN1. Interacts with KCTD8, KCTD12,
CC KCTD12B and KCTD16; this interaction determines the pharmacology and
CC kinetics of the receptor response, the KCTD proteins markedly
CC accelerating the GABA-B response, although to different extents.
CC {ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:20400944}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20400944}. Cell membrane
CC {ECO:0000269|PubMed:20400944}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:20400944}.
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. GABRB1 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; U14418; AAA79973.1; -; mRNA.
DR CCDS; CCDS19329.1; -.
DR PIR; S53530; S53530.
DR RefSeq; NP_032095.1; NM_008069.4.
DR AlphaFoldDB; P50571; -.
DR SMR; P50571; -.
DR BioGRID; 199802; 4.
DR STRING; 10090.ENSMUSP00000031122; -.
DR ChEMBL; CHEMBL2094133; -.
DR DrugCentral; P50571; -.
DR GlyGen; P50571; 3 sites.
DR iPTMnet; P50571; -.
DR PhosphoSitePlus; P50571; -.
DR PaxDb; P50571; -.
DR PeptideAtlas; P50571; -.
DR PRIDE; P50571; -.
DR ProteomicsDB; 268850; -.
DR ABCD; P50571; 1 sequenced antibody.
DR Antibodypedia; 12048; 459 antibodies from 40 providers.
DR DNASU; 14400; -.
DR Ensembl; ENSMUST00000031122; ENSMUSP00000031122; ENSMUSG00000029212.
DR GeneID; 14400; -.
DR KEGG; mmu:14400; -.
DR UCSC; uc008xrb.1; mouse.
DR CTD; 2560; -.
DR MGI; MGI:95619; Gabrb1.
DR VEuPathDB; HostDB:ENSMUSG00000029212; -.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154245; -.
DR HOGENOM; CLU_010920_0_2_1; -.
DR InParanoid; P50571; -.
DR OMA; QTYMPSN; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P50571; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14400; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Gabrb1; mouse.
DR PRO; PR:P50571; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P50571; protein.
DR Bgee; ENSMUSG00000029212; Expressed in subparaventricular zone and 139 other tissues.
DR ExpressionAtlas; P50571; baseline and differential.
DR Genevisible; P50571; 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:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005253; F:anion channel activity; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISS:UniProtKB.
DR GO; GO:0015276; F:ligand-gated ion channel activity; ISS:UniProtKB.
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:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; ISS:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042698; P:ovulation cycle; IEA:Ensembl.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; 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; IPR002289; GABAAb_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; PR01160; GABAARBETA.
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; Ligand-gated ion channel; Membrane;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..474
FT /note="Gamma-aminobutyric acid receptor subunit beta-1"
FT /id="PRO_0000000457"
FT TOPO_DOM 26..245
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 328..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..473
FT /note="Helical"
FT /evidence="ECO:0000305"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..175
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 54100 MW; 986C47E4BD663763 CRC64;
MWTVQNRESL GLLSFPVMVA MVCCAHSSNE PSNMSYVKET VDRLLKGYDI RLRPDFGGPP
VDVGMRIDVA SIDMVSEVNM DYTLTMYFQQ SWKDKRLSYS GIPLNLTLDN RVADQLWVPD
TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE
SYGYTTDDIE FYWNGGEGAV TGVNKIELPQ FSIVDYKMVS KKVEFTTGAY PRLSLSFRLK
RNIGYFILQT YMPSTLITIL SWVSFWINYD ASAARVALGI TTVLTMTTIS THLRETLPKI
PYVKAIDIYL MGCFVFVFLA LLEYAFVNYI FFGKGPQKKG ASKQDQSANE KNRLEMNKVQ
VDAHGNILLS TLEIRNETSG SEVLTGVSDP KATMYSYDSA SIQYRKPLSS REGFGRGLDR
HGVPGKGRIR RRASQLKVKI PDLTDVNSID KWSRMFFPIT FSLFNVVYWL YYVH
