GBRB1_BOVIN
ID GBRB1_BOVIN Reviewed; 474 AA.
AC P08220;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 160.
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 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], FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RC TISSUE=Brain;
RX PubMed=3037384; DOI=10.1038/328221a0;
RA Schofield P.R., Darlison M.G., Fujita N., Burt D.R., Stephenson F.A.,
RA Rodriguez H., Rhee L.M., Ramachandran J., Reale V., Glencorse T.A.,
RA Seeburg P.H., Barnard E.A.;
RT "Sequence and functional expression of the GABA A receptor shows a ligand-
RT gated receptor super-family.";
RL Nature 328:221-227(1987).
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:3037384}.
CC -!- SUBUNIT: 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). Heteropentamer, formed by a
CC combination of alpha, beta, gamma, delta and rho chains. {ECO:0000250,
CC ECO:0000269|PubMed:3037384}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:3037384}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:3037384}. Cell membrane
CC {ECO:0000269|PubMed:3037384}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:3037384}.
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; X05718; CAA29190.1; -; mRNA.
DR PIR; B27142; B27142.
DR RefSeq; NP_776969.1; NM_174544.2.
DR AlphaFoldDB; P08220; -.
DR SMR; P08220; -.
DR STRING; 9913.ENSBTAP00000023711; -.
DR BindingDB; P08220; -.
DR ChEMBL; CHEMBL4680049; -.
DR DrugCentral; P08220; -.
DR PaxDb; P08220; -.
DR PRIDE; P08220; -.
DR Ensembl; ENSBTAT00000023711; ENSBTAP00000023711; ENSBTAG00000017837.
DR GeneID; 282239; -.
DR KEGG; bta:282239; -.
DR CTD; 2560; -.
DR VEuPathDB; HostDB:ENSBTAG00000017837; -.
DR VGNC; VGNC:29196; GABRB1.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154245; -.
DR HOGENOM; CLU_010920_1_4_1; -.
DR InParanoid; P08220; -.
DR OMA; QTYMPSN; -.
DR OrthoDB; 480926at2759; -.
DR TreeFam; TF315453; -.
DR Reactome; R-BTA-977443; GABA receptor activation.
DR PRO; PR:P08220; -.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000017837; Expressed in occipital lobe and 37 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
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: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; 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; 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; IBA:GO_Central.
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: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; 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_0000000455"
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; 54130 MW; 001AE6F7ACEC74C0 CRC64;
MWTVQNRESL GLLSFPVMIA MVCCAHSANE 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 AGKQDQSANE KNKLEMNKVQ
VDAHGNILLS TLEIRNETSG SEVLTGVGDP KTTMYSYDSA SIQYRKPMSS REGYGRALDR
HGAHSKGRIR RRASQLKVKI PDLTDVNSID KWSRMFFPIT FSLFNVVYWL YYVH
