GBRB2_MACMU
ID GBRB2_MACMU Reviewed; 512 AA.
AC D1LYT2;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-2 {ECO:0000312|EMBL:ACY69096.1};
DE AltName: Full=GABA(A) receptor subunit beta-2 {ECO:0000250|UniProtKB:P47870};
DE Flags: Precursor;
GN Name=GABRB2 {ECO:0000312|EMBL:ACY69096.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1] {ECO:0000312|EMBL:ACY69096.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=19763268; DOI=10.1371/journal.pone.0006977;
RA Zhao C., Xu Z., Wang F., Chen J., Ng S.K., Wong P.W., Yu Z., Pun F.W.,
RA Ren L., Lo W.S., Tsang S.Y., Xue H.;
RT "Alternative-splicing in the exon-10 region of GABA(A) receptor beta(2)
RT subunit gene: relationships between novel isoforms and psychotic
RT disorders.";
RL PLoS ONE 4:E6977-E6977(2009).
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 (By similarity). 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 (By
CC similarity). {ECO:0000250|UniProtKB:P63137,
CC ECO:0000250|UniProtKB:P63138}.
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 (By similarity). Interacts with UBQLN1 (By
CC similarity). Interacts with KCTD8, KCTD12 and KCTD16; this interaction
CC determines the pharmacology and kinetics of the receptor response, the
CC KCTD proteins markedly accelerating the GABA-B response, although to
CC different extents (By similarity). May interact with KIF21B (By
CC similarity). Identified in a complex of 720 kDa composed of LHFPL4,
CC NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (By similarity).
CC {ECO:0000250|UniProtKB:P63138}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:P63138}.
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; GU086165; ACY69096.1; -; mRNA.
DR RefSeq; NP_001161800.1; NM_001168328.1.
DR RefSeq; XP_014996834.1; XM_015141348.1.
DR RefSeq; XP_014996836.1; XM_015141350.1.
DR AlphaFoldDB; D1LYT2; -.
DR SMR; D1LYT2; -.
DR STRING; 9544.ENSMMUP00000023715; -.
DR Ensembl; ENSMMUT00000025349; ENSMMUP00000023715; ENSMMUG00000018044.
DR GeneID; 696767; -.
DR KEGG; mcc:696767; -.
DR CTD; 2561; -.
DR VEuPathDB; HostDB:ENSMMUG00000018044; -.
DR VGNC; VGNC:72852; GABRB2.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154245; -.
DR InParanoid; D1LYT2; -.
DR OrthoDB; 480926at2759; -.
DR Proteomes; UP000006718; Chromosome 6.
DR Bgee; ENSMMUG00000018044; Expressed in dorsolateral prefrontal cortex and 14 other tissues.
DR ExpressionAtlas; D1LYT2; baseline.
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:1902711; C:GABA-A receptor complex; ISS:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0071420; P:cellular response to histamine; ISS:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:1902476; P:chloride transmembrane transport; ISS:UniProtKB.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:Ensembl.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0060119; P:inner ear receptor cell development; IEA:Ensembl.
DR GO; GO:0060384; P:innervation; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
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:0007605; P:sensory perception of sound; IEA:Ensembl.
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 2: Evidence at transcript 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|UniProtKB:P0C2W5"
FT CHAIN 26..512
FT /note="Gamma-aminobutyric acid receptor subunit beta-2"
FT /evidence="ECO:0000250|UniProtKB:P0C2W5"
FT /id="PRO_0000392919"
FT TOPO_DOM 26..244
FT /note="Extracellular"
FT /evidence="ECO:0000255, 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..489
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255, ECO:0000305"
FT TRANSMEM 490..511
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 441
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|UniProtKB:P02708"
SQ SEQUENCE 512 AA; 59150 MW; C390A0C92815DD89 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 AAEKAASANN EKMRLDVNKI
FYKDIKQNGT QYRSLWDPTG NLSPTRRTTN YDFSLYTMDP HENILLSTLE IKNEMATSEA
VMGLGDPRST MLAYDASSIQ YRKAGLPRHS FGRNALERHV AQKKSRLRRR ASQLKITIPD
LTDVNAIDRW SRIFFPVVFS FFNIVYWLYY VN
