GBRB1_RAT
ID GBRB1_RAT Reviewed; 474 AA.
AC P15431;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 184.
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; Synonyms=Gabrb-1;
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].
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], AND FUNCTION.
RX PubMed=1977069; DOI=10.1016/0169-328x(90)90017-8;
RA Malherbe P., Draguhn A., Multhaup G., Beyreuther K., Mohler H.;
RT "GABAA-receptor expressed from rat brain alpha- and beta-subunit cDNAs
RT displays potentiation by benzodiazepine receptor ligands.";
RL Brain Res. Mol. Brain Res. 8:199-208(1990).
RN [3]
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).
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
CC histamine. 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:0000269|PubMed:18281286, ECO:0000269|PubMed:1977069}.
CC -!- SUBUNIT: Binds UBQLN1. 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 (By similarity). Heteropentamer, formed
CC by a combination of alpha, beta, gamma, delta and rho chains.
CC {ECO:0000250, ECO:0000269|PubMed:18281286}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:18281286}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18281286}. Cell membrane
CC {ECO:0000269|PubMed:18281286}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18281286}.
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; X15466; CAA33493.1; -; mRNA.
DR PIR; S04464; B60039.
DR RefSeq; NP_037088.1; NM_012956.1.
DR PDB; 6DW0; EM; 3.80 A; B/E=1-333, B/E=440-474.
DR PDB; 6DW1; EM; 3.10 A; B/E=1-333, B/E=440-474.
DR PDBsum; 6DW0; -.
DR PDBsum; 6DW1; -.
DR AlphaFoldDB; P15431; -.
DR SMR; P15431; -.
DR CORUM; P15431; -.
DR IntAct; P15431; 2.
DR STRING; 10116.ENSRNOP00000003170; -.
DR ChEMBL; CHEMBL1907607; -.
DR DrugCentral; P15431; -.
DR TCDB; 1.A.9.5.1; the neurotransmitter receptor, cys loop, ligand-gated ion channel (lic) family.
DR GlyGen; P15431; 3 sites.
DR iPTMnet; P15431; -.
DR PhosphoSitePlus; P15431; -.
DR PaxDb; P15431; -.
DR PRIDE; P15431; -.
DR ABCD; P15431; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000003170; ENSRNOP00000003170; ENSRNOG00000002327.
DR GeneID; 25450; -.
DR KEGG; rno:25450; -.
DR UCSC; RGD:2649; rat.
DR CTD; 2560; -.
DR RGD; 2649; Gabrb1.
DR eggNOG; KOG3643; Eukaryota.
DR GeneTree; ENSGT00940000154245; -.
DR HOGENOM; CLU_010920_0_2_1; -.
DR InParanoid; P15431; -.
DR OMA; QTYMPSN; -.
DR OrthoDB; 480926at2759; -.
DR PhylomeDB; P15431; -.
DR TreeFam; TF315453; -.
DR Reactome; R-RNO-977443; GABA receptor activation.
DR PRO; PR:P15431; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000002327; Expressed in Ammon's horn and 2 other tissues.
DR Genevisible; P15431; 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:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:1902711; C:GABA-A receptor complex; IMP:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005253; F:anion channel activity; IDA:RGD.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0050811; F:GABA receptor binding; IPI:RGD.
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:0015276; F:ligand-gated ion channel activity; IMP: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; IDA:SynGO.
DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB.
DR GO; GO:0021954; P:central nervous system neuron development; IEP: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:0006821; P:chloride transport; TAS:RGD.
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; IMP:UniProtKB.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0042698; P:ovulation cycle; IEP:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0032570; P:response to progesterone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IDA:RGD.
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 3D-structure; Cell membrane; Chloride; Chloride channel; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Ligand-gated ion channel;
KW Membrane; Postsynaptic cell membrane; Receptor; Reference proteome; Signal;
KW Synapse; 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_0000000458"
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"
FT CONFLICT 420
FT /note="R -> Q (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="R -> P (in Ref. 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6DW1"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 61..71
FT /evidence="ECO:0007829|PDB:6DW1"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 81..93
FT /evidence="ECO:0007829|PDB:6DW1"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:6DW1"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 145..160
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6DW1"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:6DW1"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:6DW1"
FT STRAND 229..239
FT /evidence="ECO:0007829|PDB:6DW1"
SQ SEQUENCE 474 AA; 54072 MW; 986277FDBD66377A CRC64;
MWTVQNRESL GLLSFPVMVA MVCCAHSSNE 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 ASKQDQSANE KNKLEMNKVQ
VDAHGNILLS TLEIRNETSG SEVLTGVSDP KATMYSYDSA SIQYRKPLSS REGFGRGLDR
HGVPGKGRIR RRASQLKVKI PDLTDVNSID KWSRMFFPIT FSLFNVVYWL YYVH
