GBRB2_RAT
ID GBRB2_RAT Reviewed; 474 AA.
AC P63138; P15432;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-2;
DE AltName: Full=GABA(A) receptor subunit beta-2;
DE Flags: Precursor;
GN Name=Gabrb2; Synonyms=Gabrb-2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=2548852; DOI=10.1002/j.1460-2075.1989.tb03557.x;
RA Ymer S., Schofield P.R., Draguhn A., Werner P., Koehler M., Seeburg P.H.;
RT "GABAA receptor beta subunit heterogeneity: functional expression of cloned
RT cDNAs.";
RL EMBO J. 8:1665-1670(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Groot Kormelink P.J.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18281286; DOI=10.1074/jbc.m709993200;
RA Saras A., Gisselmann G., Vogt-Eisele A.K., Erlkamp K.S., Kletke O.,
RA Pusch H., Hatt H.;
RT "Histamine action on vertebrate GABAA receptors: direct channel gating and
RT potentiation of GABA responses.";
RL J. Biol. Chem. 283:10470-10475(2008).
RN [5]
RP INTERACTION WITH KCTD8; KCTD12 AND KCTD16.
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).
RN [6]
RP INTERACTION WITH KIF21B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25172774; DOI=10.1016/j.ejcb.2014.07.007;
RA Labonte D., Thies E., Kneussel M.;
RT "The kinesin KIF21B participates in the cell surface delivery of gamma2
RT subunit-containing GABAA receptors.";
RL Eur. J. Cell Biol. 93:338-346(2014).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX WITH
RP NLGN2; LHFPL4; GABRA1; GABRG2 AND GABRB3.
RX PubMed=28279354; DOI=10.1016/j.neuron.2017.02.023;
RA Yamasaki T., Hoyos-Ramirez E., Martenson J.S., Morimoto-Tomita M.,
RA Tomita S.;
RT "GARLH family proteins stabilize GABAA receptors at synapses.";
RL Neuron 93:1138-1152(2017).
CC -!- FUNCTION: Ligand-gated chloride channel which is a component of the
CC heteropentameric receptor for GABA, the major inhibitory
CC neurotransmitter in the brain (PubMed:2548852). Plays an important role
CC in the formation of functional inhibitory GABAergic synapses in
CC addition to mediating synaptic inhibition as a GABA-gated ion channel
CC (By similarity). The gamma2 subunit is necessary but not sufficient for
CC a rapid formation of active synaptic contacts and the synaptogenic
CC effect of this subunit is influenced by the type of alpha and beta
CC subunits present in the receptor pentamer (By similarity). The
CC alpha1/beta2/gamma2 receptor and the alpha2/beta2/gamma2 receptor
CC exhibit synaptogenic activity (By similarity). Functions also as
CC histamine receptor and mediates cellular responses to histamine
CC (PubMed:18281286). {ECO:0000250|UniProtKB:P63137,
CC ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:2548852}.
CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines and
CC the anesthetic etomidate (By similarity). Inhibited by the antagonist
CC bicuculline (By similarity). {ECO:0000250|UniProtKB:P0C2W5,
CC ECO:0000250|UniProtKB:P47870}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains (PubMed:18281286). Interacts with UBQLN1
CC (PubMed:11528422). Interacts with KCTD8, KCTD12 and KCTD16; this
CC interaction determines the pharmacology and kinetics of the receptor
CC response, the KCTD proteins markedly accelerating the GABA-B response,
CC although to different extents (PubMed:20400944). May interact with
CC KIF21B (PubMed:25172774). Identified in a complex of 720 kDa composed
CC of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (PubMed:28279354).
CC {ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:18281286,
CC ECO:0000269|PubMed:20400944, ECO:0000269|PubMed:25172774,
CC ECO:0000269|PubMed:28279354}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:18281286}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:18281286}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:25172774}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:25172774}.
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000250|UniProtKB:P63137}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P63137}.
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. GABRB2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X15467; CAA33494.1; -; mRNA.
DR EMBL; AY574251; AAS90347.1; -; mRNA.
DR PIR; S04465; S04465.
DR RefSeq; NP_037089.1; NM_012957.2.
DR RefSeq; XP_006246189.1; XM_006246127.2.
DR AlphaFoldDB; P63138; -.
DR SMR; P63138; -.
DR BioGRID; 247486; 1.
DR ComplexPortal; CPX-250; GABA-A receptor, alpha-1/beta-2/gamma-2.
DR ComplexPortal; CPX-407; GABA-A receptor, alpha-6/beta-2/delta.
DR ComplexPortal; CPX-408; GABA-A receptor, alpha-4/beta-2/delta.
DR CORUM; P63138; -.
DR IntAct; P63138; 2.
DR STRING; 10116.ENSRNOP00000004970; -.
DR BindingDB; P63138; -.
DR ChEMBL; CHEMBL2095167; -.
DR ChEMBL; CHEMBL2111327; -.
DR ChEMBL; CHEMBL2111343; -.
DR ChEMBL; CHEMBL2111365; -.
DR ChEMBL; CHEMBL3883322; -.
DR ChEMBL; CHEMBL4296055; -.
DR ChEMBL; CHEMBL4296056; -.
DR ChEMBL; CHEMBL4296063; -.
DR DrugCentral; P63138; -.
DR GlyGen; P63138; 3 sites.
DR iPTMnet; P63138; -.
DR PhosphoSitePlus; P63138; -.
DR PaxDb; P63138; -.
DR PRIDE; P63138; -.
DR Ensembl; ENSRNOT00000118632; ENSRNOP00000081083; ENSRNOG00000003680.
DR GeneID; 25451; -.
DR KEGG; rno:25451; -.
DR UCSC; RGD:2650; rat.
DR CTD; 2561; -.
DR RGD; 2650; Gabrb2.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154245; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P63138; -.
DR OMA; INKMDPH; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P63138; -.
DR TreeFam; TF315453; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P63138; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003680; Expressed in frontal cortex and 5 other tissues.
DR Genevisible; P63138; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:1902710; C:GABA receptor complex; IDA:BHF-UCL.
DR GO; GO:1902711; C:GABA-A receptor complex; IMP:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IMP:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; IMP:UniProtKB.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IEA:Ensembl.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IMP:RGD.
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:RGD.
DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISO:RGD.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0060119; P:inner ear receptor cell development; ISO:RGD.
DR GO; GO:0060384; P:innervation; ISO:RGD.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:RGD.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0048666; P:neuron development; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0043523; P:regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IDA:BHF-UCL.
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; Cytoplasmic vesicle;
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..25
FT /evidence="ECO:0000250"
FT CHAIN 26..474
FT /note="Gamma-aminobutyric acid receptor subunit beta-2"
FT /id="PRO_0000000461"
FT TOPO_DOM 26..244
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 245..266
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 270..292
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 327..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..473
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 403
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63137"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..174
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 54633 MW; 8A815982EB70933E CRC64;
MWRVRKRGYF GIWSFPLIIA AVCAQSVNDP SNMSLVKETV DRLLKGYDIR LRPDFGGPPV
AVGMNIDIAS IDMVSEVNMD YTLTMYFQQA WRDKRLSYNV IPLNLTLDNR VADQLWVPDT
YFLNDKKSFV HGVTVKNRMI RLHPDGTVLY GLRITTTAAC MMDLRRYPLD EQNCTLEIES
YGYTTDDIEF YWRGDDNAVT GVTKIELPQF SIVDYKLITK KVVFSTGSYP RLSLSFKLKR
NIGYFILQTY MPSILITILS WVSFWINYDA SAARVALGIT TVLTMTTINT HLRETLPKIP
YVKAIDMYLM GCFVFVFMAL LEYALVNYIF FGRGPQRQKK AAEKAANANN EKMRLDVNKM
DPHENILLST LEIKNEMATS EAVMGLGDPR STMLAYDASS IQYRKAGLPR HSFGRNALER
HVAQKKSRLR RRASQLKITI PDLTDVNAID RWSRIFFPVV FSFFNIVYWL YYVN
