GBRB3_RAT
ID GBRB3_RAT Reviewed; 473 AA.
AC P63079; P15433;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-3;
DE AltName: Full=GABA(A) receptor subunit beta-3;
DE Flags: Precursor;
GN Name=Gabrb3; Synonyms=Gabrb-3;
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], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
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], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=2540033; DOI=10.1016/0014-5793(89)80271-6;
RA Lolait S.J., O'Carroll A.-M., Kusano K., Muller J.-M., Brownstein M.J.,
RA Mahan L.C.;
RT "Cloning and expression of a novel rat GABAA receptor.";
RL FEBS Lett. 246:145-148(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8382702; DOI=10.1016/s0021-9258(18)53626-7;
RA Kirkness E.F., Fraser C.M.;
RT "A strong promoter element is located between alternative exons of a gene
RT encoding the human gamma-aminobutyric acid-type A receptor beta 3 subunit
RT (GABRB3).";
RL J. Biol. Chem. 268:4420-4428(1993).
RN [4]
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=9092594; DOI=10.1523/jneurosci.17-08-02728.1997;
RA Tretter V., Ehya N., Fuchs K., Sieghart W.;
RT "Stoichiometry and assembly of a recombinant GABAA receptor subtype.";
RL J. Neurosci. 17:2728-2737(1997).
RN [5]
RP INTERACTION WITH UBQLN1.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [7]
RP INTERACTION WITH GIT1.
RX PubMed=25284783; DOI=10.1016/j.celrep.2014.08.061;
RA Smith K.R., Davenport E.C., Wei J., Li X., Pathania M., Vaccaro V., Yan Z.,
RA Kittler J.T.;
RT "GIT1 and betaPIX are essential for GABA(A) receptor synaptic stability and
RT inhibitory neurotransmission.";
RL Cell Rep. 9:298-310(2014).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX WITH
RP NLGN2; GABRA1; GABRB2; 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, PubMed:2540033). Plays
CC an important role in the formation of functional inhibitory GABAergic
CC synapses in addition to mediating synaptic inhibition as a GABA- gated
CC ion channel (By similarity). The gamma2 subunit is necessary but not
CC sufficient for a rapid formation of active synaptic contacts and the
CC synaptogenic effect of this subunit is influenced by the type of alpha
CC and beta subunits present in the receptor pentamer (By similarity). The
CC alpha1/beta3/gamma2 receptor exhibits synatogenic activity whereas the
CC alpha2/beta3/gamma2 receptor shows very little or no synaptogenic
CC activity (By similarity). Functions also as histamine receptor and
CC mediates cellular responses to histamine (By similarity). Plays an
CC important role in somatosensation and in the production of
CC antinociception (By similarity). {ECO:0000250|UniProtKB:P28472,
CC ECO:0000250|UniProtKB:P63080, ECO:0000269|PubMed:2540033,
CC ECO:0000269|PubMed:2548852}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains (PubMed:2548852, PubMed:2540033, PubMed:9092594).
CC Can form functional homopentamers (in vitro) (By similarity). Interacts
CC with UBQLN1 (PubMed:11528422). May interact with KIF21B
CC (PubMed:25172774). Identified in a complex of 720 kDa composed of
CC LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (PubMed:28279354).
CC Interacts with LHFPL4 (By similarity). Interacts with GIT1; this
CC interaction is required for synaptic GABRB3 surface stability and
CC inhibitory synapse strength (PubMed:25284783).
CC {ECO:0000250|UniProtKB:P28472, ECO:0000250|UniProtKB:P63080,
CC ECO:0000269|PubMed:11528422, ECO:0000269|PubMed:25172774,
CC ECO:0000269|PubMed:25284783, ECO:0000269|PubMed:2540033,
CC ECO:0000269|PubMed:2548852, ECO:0000269|PubMed:28279354,
CC ECO:0000269|PubMed:9092594}.
CC -!- INTERACTION:
CC P63079; Q7TSU1: Arfgef2; NbExp=3; IntAct=EBI-6257937, EBI-6257913;
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P28472}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P28472}. Cell membrane
CC {ECO:0000269|PubMed:2540033, ECO:0000269|PubMed:2548852,
CC ECO:0000269|PubMed:9092594}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P28472}. Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:25172774}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC {ECO:0000269|PubMed:25172774}.
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. GABRB3 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; X15468; CAA33495.1; -; mRNA.
DR EMBL; L04310; AAA41180.1; -; Genomic_DNA.
DR PIR; S04466; S04466.
DR RefSeq; NP_058761.1; NM_017065.1.
DR AlphaFoldDB; P63079; -.
DR SMR; P63079; -.
DR ComplexPortal; CPX-280; GABA-A receptor, alpha-4/beta-3/delta.
DR ComplexPortal; CPX-405; GABA-A receptor, alpha-6/beta-3/gamma-2.
DR ComplexPortal; CPX-406; GABA-A receptor, alpha-6/beta-3/delta.
DR ComplexPortal; CPX-409; GABA-A receptor, alpha-3/beta-3/gamma-2.
DR ComplexPortal; CPX-410; GABA-A receptor, alpha-1/beta-3/gamma-2.
DR ComplexPortal; CPX-411; GABA-A receptor, alpha-5/beta-3/gamma-2.
DR ComplexPortal; CPX-412; GABA-A receptor, alpha-2/beta-3/gamma-2.
DR CORUM; P63079; -.
DR DIP; DIP-60770N; -.
DR IntAct; P63079; 5.
DR STRING; 10116.ENSRNOP00000061969; -.
DR BindingDB; P63079; -.
DR ChEMBL; CHEMBL2111374; -.
DR ChEMBL; CHEMBL3883322; -.
DR ChEMBL; CHEMBL4296047; -.
DR ChEMBL; CHEMBL4296048; -.
DR ChEMBL; CHEMBL4296049; -.
DR ChEMBL; CHEMBL4296050; -.
DR ChEMBL; CHEMBL4296051; -.
DR ChEMBL; CHEMBL4296052; -.
DR ChEMBL; CHEMBL4296053; -.
DR ChEMBL; CHEMBL4296054; -.
DR ChEMBL; CHEMBL4296060; -.
DR ChEMBL; CHEMBL4296061; -.
DR ChEMBL; CHEMBL4296062; -.
DR DrugCentral; P63079; -.
DR GlyGen; P63079; 3 sites.
DR PaxDb; P63079; -.
DR PRIDE; P63079; -.
DR ABCD; P63079; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000113752; ENSRNOP00000085111; ENSRNOG00000060599.
DR GeneID; 24922; -.
DR KEGG; rno:24922; -.
DR UCSC; RGD:2651; rat.
DR CTD; 2562; -.
DR RGD; 2651; Gabrb3.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154713; -.
DR InParanoid; P63079; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P63079; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P63079; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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:1902711; C:GABA-A receptor complex; IPI:ComplexPortal.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0035612; F:AP-2 adaptor complex binding; IPI:RGD.
DR GO; GO:0005254; F:chloride channel activity; IDA:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0004890; F:GABA-A receptor activity; IDA:RGD.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0005216; F:ion channel activity; ISO: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:0007420; P:brain development; ISO:RGD.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; ISO:RGD.
DR GO; GO:0021549; P:cerebellum development; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; ISO:RGD.
DR GO; GO:0042747; P:circadian sleep/wake cycle, REM sleep; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0035640; P:exploration behavior; ISO:RGD.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; ISS:UniProtKB.
DR GO; GO:0060022; P:hard palate development; ISO:RGD.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; 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:0007612; P:learning; ISO:RGD.
DR GO; GO:0007613; P:memory; ISO:RGD.
DR GO; GO:0061744; P:motor behavior; ISO:RGD.
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:0007399; P:nervous system development; 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:0019098; P:reproductive behavior; ISO:RGD.
DR GO; GO:0072347; P:response to anesthetic; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IDA:RGD.
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; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..473
FT /note="Gamma-aminobutyric acid receptor subunit beta-3"
FT /id="PRO_0000000464"
FT TOPO_DOM 26..245
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 268..270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 271..293
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 294..304
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 305..327
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 328..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 451..472
FT /note="Helical"
FT /evidence="ECO:0000250"
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"
FT CONFLICT 256
FT /note="L -> M (in Ref. 1; CAA33495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 54166 MW; 6A5ABD8A9143FE45 CRC64;
MWGFAGGRLF GIFSAPVLVA VVCCAQSVND PGNMSFVKET VDKLLKGYDI RLRPDFGGPP
VCVGMNIDIA SIDMVSEVNM DYTLTMYFQQ YWRDKRLAYS GIPLNLTLDN RVADQLWVPD
TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE
SYGYTTDDIE FYWRGGDKAV TGVERIELPQ FSIVEHRLVS RNVVFATGAY PRLSLSFRLK
RNIGYFILQT YMPSILITIL SWVSFWINYD ASAARVALGI TTVLTMTTIN THLRETLPKI
PYVKAIDMYL MGCFVFVFLA LLEYAFVNYI FFGRGPQRQK KLAEKTAKAK NDRSKSEINR
VDAHGNILLA PMDVHNEMNE VAGSVGDTRN SAISFDNSGI QYRKQSMPKE GHGRYMGDRS
IPHKKTHLRR RSSQLKIKIP DLTDVNAIDR WSRIVFPFTF SLFNLVYWLY YVN
