GBRB2_BOVIN
ID GBRB2_BOVIN Reviewed; 472 AA.
AC P0C2W5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit beta-2;
DE AltName: Full=GABA(A) receptor subunit beta-2;
DE Flags: Precursor; Fragment;
GN Name=GABRB2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 358-374, FUNCTION,
RP 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 PROTEIN SEQUENCE OF 24-35, ACTIVITY REGULATION, ANESTHETIC BINDING SITE,
RP AND SUBCELLULAR LOCATION.
RX PubMed=17093081; DOI=10.1523/jneurosci.3467-06.2006;
RA Li G.D., Chiara D.C., Sawyer G.W., Husain S.S., Olsen R.W., Cohen J.B.;
RT "Identification of a GABAA receptor anesthetic binding site at subunit
RT interfaces by photolabeling with an etomidate analog.";
RL J. Neurosci. 26:11599-11605(2006).
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 (By
CC similarity). {ECO:0000250|UniProtKB:P63137,
CC ECO:0000250|UniProtKB:P63138, ECO:0000269|PubMed:2548852}.
CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines (By
CC similarity). Allosterically activated by the anesthetic etomidate
CC (PubMed:17093081). Inhibited by the antagonist bicuculline (By
CC similarity). {ECO:0000250|UniProtKB:P47870,
CC ECO:0000269|PubMed:17093081}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains (PubMed:2548852). 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, ECO:0000269|PubMed:2548852}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P63137}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:17093081,
CC ECO:0000269|PubMed:2548852}; Multi-pass membrane protein {ECO:0000255}.
CC Cytoplasmic vesicle membrane {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 AlphaFoldDB; P0C2W5; -.
DR SMR; P0C2W5; -.
DR InParanoid; P0C2W5; -.
DR OrthoDB; 480926at2759; -.
DR Proteomes; UP000009136; Unplaced.
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:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
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: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:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
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: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; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL <1..23
FT /evidence="ECO:0000269|PubMed:17093081"
FT CHAIN 24..472
FT /note="Gamma-aminobutyric acid receptor subunit beta-2"
FT /id="PRO_0000286328"
FT TOPO_DOM 24..239
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..329
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 330..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 451..471
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 287..308
FT /note="Etomidate binding; allosteric effector"
FT /evidence="ECO:0000269|PubMed:17093081"
FT MOD_RES 401
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P63137"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 158..172
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 472 AA; 54451 MW; 9D79CAF59EC36B32 CRC64;
RVRKKDYFGI WSFPLIIAAV CAQSVNDPSN MSLVKETVDR LLKGYDIRLR PDFGGPPVAV
GMNIDIASID MVSEVNMDYT LTMYFQQAWR DKRLSYNVIP LNLTLDNRVA DQLWVPDTYF
LNDKKSFVHG VTVKNRMIRL HPDGTVLYGL RITTTTACMM DLRRYPLDEQ NCTLEIESYG
YTTDDIEFYW RGDDNAVTGV TKIELPQFSI VDYKLITKKV VFSTGSYPRL SLSFKLKRNI
GYFILQTYMP SILITILSWV SFWINYDASA ARVALGITTV LTMTTINTHL RETLPKIPYV
KAIDMYLMGC FVFVFMALLE YALVNYIFFG RGPQRQKKAA EKAASANNEK MRLDVNKMDP
HENILLSTLE IKNEMATSEA VMGLGDPRST MLAYDASSIQ YRKAGLPRHS FWRNALERHV
AQKKSRLRER ASQLKITIPD LTDVNAIDRW SRIFFPVVFS FFNIVYWLYY VN
