GABR1_RAT
ID GABR1_RAT Reviewed; 991 AA.
AC Q9Z0U4; O08620; O08621; Q9Z0F9; Q9Z308;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Gamma-aminobutyric acid type B receptor subunit 1;
DE Short=GABA-B receptor 1;
DE Short=GABA-B-R1;
DE Short=GABA-BR1;
DE Short=GABABR1;
DE Short=Gb1;
DE Flags: Precursor;
GN Name=Gabbr1;
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] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=RICO;
RC TISSUE=Brain cortex, and Cerebellum {ECO:0000303|PubMed:9069281};
RX PubMed=9069281; DOI=10.1038/386239a0;
RA Kaupmann K., Huggel K., Heid J., Flor P.J., Bischoff S., Mickel S.J.,
RA McMaster G., Angst C., Bittiger H., Froestl W., Bettler B.;
RT "Expression cloning of GABA(B) receptors uncovers similarity to
RT metabotropic glutamate receptors.";
RL Nature 386:239-246(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1C AND 1D), AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum {ECO:0000303|PubMed:9875211};
RX PubMed=9875211; DOI=10.1006/bbrc.1998.9706;
RA Isomoto S., Kaibara M., Sakurai-Yamashita Y., Nagayama Y., Uezono Y.,
RA Yano K., Taniyama K.;
RT "Cloning and tissue distribution of novel splice variants of the rat GABAB
RT receptor.";
RL Biochem. Biophys. Res. Commun. 253:10-15(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1E), ALTERNATIVE SPLICING
RP (ISOFORM 1E), FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Hippocampus {ECO:0000303|PubMed:10457184};
RX PubMed=10457184; DOI=10.1046/j.1460-9568.1999.00704.x;
RA Pfaff T., Malitschek B., Kaupmann K., Prezeau L., Pin J.-P., Bettler B.,
RA Karschin A.;
RT "Alternative splicing generates a novel isoform of the rat metabotropic
RT GABA(B)R1 receptor.";
RL Eur. J. Neurosci. 11:2874-2882(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND FUNCTION.
RC TISSUE=Brain {ECO:0000303|PubMed:10075644};
RX PubMed=10075644; DOI=10.1074/jbc.274.12.7607;
RA Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R.,
RA Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P.,
RA Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F.,
RA Bonner T.I., O'Neill G.P.;
RT "Identification of a GABAB receptor subunit, gb2, required for functional
RT GABAB receptor activity.";
RL J. Biol. Chem. 274:7607-7610(1999).
RN [5]
RP FUNCTION, INTERACTION WITH GABBR2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Hypothalamus {ECO:0000303|PubMed:9872315};
RX PubMed=9872315; DOI=10.1038/25348;
RA Jones K.A., Borowsky B., Tamm J.A., Craig D.A., Durkin M.M., Dai M.,
RA Yao W.-J., Johnson M., Gunwaldsen C.A., Huang L.-Y., Tang C., Shen Q.,
RA Salon J.A., Morse K., Laz T., Smith K.E., Nagarathnam D., Noble S.A.,
RA Branchek T.A., Gerald C.;
RT "GABA(B) receptors function as a heteromeric assembly of the subunits
RT GABA(B)R1 and GABA(B)R2.";
RL Nature 396:674-679(1998).
RN [6]
RP FUNCTION, INTERACTION WITH GABBR2, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain cortex, and Cerebellum {ECO:0000303|PubMed:9872317};
RX PubMed=9872317; DOI=10.1038/25360;
RA Kaupmann K., Malitschek B., Schuler V., Heid J., Froestl W., Beck P.,
RA Mosbacher J., Bischoff S., Kulik A., Shigemoto R., Karschin A., Bettler B.;
RT "GABA-B receptor subtypes assemble into functional heteromeric complexes.";
RL Nature 396:683-687(1998).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=10658574; DOI=10.1016/s0968-0896(99)00214-x;
RA Belley M., Sullivan R., Reeves A., Evans J.F., O'Neill G.P., Ng G.Y.K.;
RT "Synthesis of the nanomolar photoaffinity GABA(B) receptor ligand CGP 71872
RT reveals diversity in the tissue distribution of GABA(B) receptor forms.";
RL Bioorg. Med. Chem. 7:2697-2704(1999).
RN [8]
RP FUNCTION, INTERACTION WITH GABBR2, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9872744; DOI=10.1126/science.283.5398.74;
RA Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.;
RT "Role of heteromer formation in GABAB receptor function.";
RL Science 283:74-77(1999).
RN [9]
RP TISSUE SPECIFICITY.
RC TISSUE=Brain cortex {ECO:0000303|PubMed:10727622};
RX PubMed=10727622; DOI=10.1016/s0006-8993(00)01958-2;
RA Clark J.A., Mezey E., Lam A.S., Bonner T.I.;
RT "Distribution of the GABA(B) receptor subunit gb2 in rat CNS.";
RL Brain Res. 860:41-52(2000).
RN [10]
RP FUNCTION, INTERACTION WITH ATF4, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10924501; DOI=10.1074/jbc.m002727200;
RA Nehring R.B., Horikawa H.P.M., El Far O., Kneussel M., Brandstatter J.H.,
RA Stamm S., Wischmeyer E., Betz H., Karschin A.;
RT "The metabotropic GABAB receptor directly interacts with the activating
RT transcription factor 4.";
RL J. Biol. Chem. 275:35185-35191(2000).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF SER-247; SER-268 AND SER-269.
RX PubMed=10692480; DOI=10.1124/mol.57.3.419;
RA Galvez T., Urwyler S., Prezeau L., Mosbacher J., Joly C., Malitschek B.,
RA Heid J., Brabet I., Froestl W., Bettler B., Kaupmann K., Pin J.-P.;
RT "Ca(2+) requirement for high-affinity gamma-aminobutyric acid (GABA)
RT binding at GABA(B) receptors: involvement of serine 269 of the GABA(B)R1
RT subunit.";
RL Mol. Pharmacol. 57:419-426(2000).
RN [12]
RP INTERACTION WITH JAKMIP1, AND SUBCELLULAR LOCATION.
RX PubMed=14718537; DOI=10.1074/jbc.m311737200;
RA Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT "Marlin-1, a novel RNA-binding protein associates with GABA receptors.";
RL J. Biol. Chem. 279:13934-13943(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-960, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [14]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83 AND ASN-439, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [15]
RP STRUCTURE BY NMR OF 96-159, AND DISULFIDE BONDS.
RX PubMed=15304491; DOI=10.1074/jbc.m406540200;
RA Blein S., Ginham R., Uhrin D., Smith B.O., Soares D.C., Veltel S.,
RA McIlhinney R.A., White J.H., Barlow P.N.;
RT "Structural analysis of the complement control protein (CCP) modules of
RT GABA(B) receptor 1a: only one of the two CCP modules is compactly folded.";
RL J. Biol. Chem. 279:48292-48306(2004).
CC -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC GABA, formed by GABBR1 and GABBR2 (PubMed:9872315, PubMed:9872317,
CC PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1
CC seems to bind agonists, while GABBR2 mediates coupling to G proteins
CC (PubMed:9872317, PubMed:10658574). Ligand binding causes a conformation
CC change that triggers signaling via guanine nucleotide-binding proteins
CC (G proteins) and modulates the activity of down-stream effectors, such
CC as adenylate cyclase (PubMed:10075644, PubMed:9872315, PubMed:9872744,
CC PubMed:10924501). Signaling inhibits adenylate cyclase, stimulates
CC phospholipase A2, activates potassium channels, inactivates voltage-
CC dependent calcium-channels and modulates inositol phospholipid
CC hydrolysis (PubMed:9069281, PubMed:10457184, PubMed:9872315,
CC PubMed:9872744, PubMed:10924501, PubMed:10692480). Calcium is required
CC for high affinity binding to GABA (PubMed:10692480). Plays a critical
CC role in the fine-tuning of inhibitory synaptic transmission
CC (PubMed:9872744). Pre-synaptic GABA receptor inhibits neurotransmitter
CC release by down-regulating high-voltage activated calcium channels,
CC whereas postsynaptic GABA receptor decreases neuronal excitability by
CC activating a prominent inwardly rectifying potassium (Kir) conductance
CC that underlies the late inhibitory postsynaptic potentials
CC (PubMed:9872744, PubMed:10924501, PubMed:10692480). Not only implicated
CC in synaptic inhibition but also in hippocampal long-term potentiation,
CC slow wave sleep, muscle relaxation and antinociception (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBS5, ECO:0000269|PubMed:10075644,
CC ECO:0000269|PubMed:10457184, ECO:0000269|PubMed:10658574,
CC ECO:0000269|PubMed:10692480, ECO:0000269|PubMed:10924501,
CC ECO:0000269|PubMed:9069281, ECO:0000269|PubMed:9872315,
CC ECO:0000269|PubMed:9872744}.
CC -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872315,
CC PubMed:9872317, PubMed:9872744). Homodimers may form, but are inactive
CC (PubMed:9872317). Interacts (via C-terminus) with ATF4 (via leucine
CC zipper domain) (PubMed:10924501). Interacts with JAKMIP1
CC (PubMed:14718537). {ECO:0000269|PubMed:10924501,
CC ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:9872315,
CC ECO:0000269|PubMed:9872317, ECO:0000269|PubMed:9872744}.
CC -!- INTERACTION:
CC Q9Z0U4; O88871: Gabbr2; NbExp=8; IntAct=EBI-7090268, EBI-7090239;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10457184,
CC ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:9069281,
CC ECO:0000269|PubMed:9872315}; Multi-pass membrane protein {ECO:0000305}.
CC Postsynaptic cell membrane {ECO:0000269|PubMed:10924501}; Multi-pass
CC membrane protein {ECO:0000305}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10924501, ECO:0000269|PubMed:9872317}. Perikaryon
CC {ECO:0000269|PubMed:14718537}. Note=Coexpression of GABBR1 and GABBR2
CC is required for GABBR1 maturation and transport to the plasma membrane
CC (PubMed:10457184). Colocalizes with ATF4 in hippocampal neuron
CC dendritic membranes (PubMed:10924501). {ECO:0000269|PubMed:10924501,
CC ECO:0000305|PubMed:10457184}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1E {ECO:0000312|RGD:621537}; Synonyms=1C
CC {ECO:0000303|PubMed:10457184};
CC IsoId=Q9Z0U4-1; Sequence=Displayed;
CC Name=1A;
CC IsoId=Q9Z0U4-2; Sequence=VSP_002045;
CC Name=1B;
CC IsoId=Q9Z0U4-3; Sequence=VSP_002044, VSP_002045;
CC Name=1C;
CC IsoId=Q9Z0U4-4; Sequence=VSP_002044;
CC Name=1D;
CC IsoId=Q9Z0U4-5; Sequence=VSP_002044, VSP_002045, VSP_002046;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in tissues including the
CC forebrain, cerebellum, eye, atrium, ventricle, lung, stomach, small
CC intestine, colon, liver, spleen, kidney, urinary bladder and skeletal
CC muscle (PubMed:9875211). Expressed at low levels in testis, and more
CC highly in brain regions (PubMed:9069281). Expression is high the brain
CC regions including cerebral cortical layers, with higher expression in
CC VIb than in the II-V layers, pyramidal CA1-CA3 cell layers and granular
CC cell layers of the hippocampus, granular cell layers of the dentate
CC gyrus, including the caudate, putamen, nucleus accumbens and olfactory
CC tubercle, the granular layer cell layers of the medial habenula, in the
CC cerebellum, predominantly in Purkinje cells, and in the granule cell
CC layer (PubMed:9069281, PubMed:9872315 PubMed:9872744, PubMed:10727622).
CC Also expressed in areas of the brain including the medial geniculate
CC nucleus, substantia nigra, pars compacta, the ventral tegmental area,
CC and in several thalamic, amygdaloid and hypothalamic nuclei, such as
CC the arcuate nucleus of the hypothalamus and mammilary bodies of the
CC hypothalamus (PubMed:9069281, PubMed:9872744). Expressed in the
CC amacrine cell of the retina (PubMed:10924501). Isoform 1A: Expressed in
CC the brain, spinal cord, stomach, testis, adrenal gland, pituitary,
CC spleen and prostate (PubMed:10658574). Isoform 1B: Expressed in the
CC brain, spinal cord, stomach, testis, kidney and liver
CC (PubMed:10658574). Expressed in Isoform 1C: Ubiquitously expressed
CC (PubMed:9875211). Isoform 1D: Expressed in the forebrain, cerebellum,
CC eye, kidney and urinary bladder (PubMed:9875211). Isoform 1E:
CC Ubiquitously expressed with high expression the pyramidal CA1-CA3 cell
CC layers of the hippocampus, the granule cell layers of the dentate gyrus
CC and olfactory tubercle, the whole cortex, and Purkinje cells of the
CC cerebellum (PubMed:10457184). Moderate expression in the granule cell
CC layer of the cerebellum (PubMed:10457184).
CC {ECO:0000269|PubMed:10457184, ECO:0000269|PubMed:10658574,
CC ECO:0000269|PubMed:10727622, ECO:0000269|PubMed:10924501,
CC ECO:0000269|PubMed:9069281, ECO:0000269|PubMed:9872315,
CC ECO:0000269|PubMed:9872744, ECO:0000269|PubMed:9875211}.
CC -!- DEVELOPMENTAL STAGE: At E17 during embryonic development, highly
CC expressed in brain regions including the striatum, olfactory bulb,
CC septal nuclei, lateral habenula, pyramidal CA1-CA2 cell layers of the
CC hippocampus and in the neuroepithelial cells of the ventricular zone.
CC On the day of birth, expressed in the regions of the brain including
CC hippocampus, thalamic nuclei, cortex and cerebellum.
CC {ECO:0000269|PubMed:9872744}.
CC -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC mediate heterodimeric interaction with GABBR2. The linker region
CC between the transmembrane domain 3 (TM3) and the transmembrane domain 4
CC (TM4) probably plays a role in the specificity for G-protein coupling.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC receptor subfamily. {ECO:0000305}.
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DR EMBL; Y10369; CAA71398.1; -; mRNA.
DR EMBL; Y10370; CAA71399.1; -; mRNA.
DR EMBL; AB016160; BAA34708.1; -; mRNA.
DR EMBL; AB016161; BAA34709.1; -; mRNA.
DR EMBL; AF110797; AAD19656.1; -; Genomic_DNA.
DR EMBL; AF110796; AAD19656.1; JOINED; Genomic_DNA.
DR EMBL; AF110797; AAD19657.1; -; Genomic_DNA.
DR EMBL; AF110796; AAD19657.1; JOINED; Genomic_DNA.
DR EMBL; AF110797; AAD19658.1; -; Genomic_DNA.
DR EMBL; AF110796; AAD19658.1; JOINED; Genomic_DNA.
DR EMBL; AF110797; AAD19659.1; -; Genomic_DNA.
DR EMBL; AF110796; AAD19659.1; JOINED; Genomic_DNA.
DR RefSeq; NP_112290.2; NM_031028.3. [Q9Z0U4-2]
DR RefSeq; XP_006255941.1; XM_006255879.3. [Q9Z0U4-1]
DR PDB; 1SRZ; NMR; -; A=96-159.
DR PDB; 1SS2; NMR; -; A=96-159.
DR PDBsum; 1SRZ; -.
DR PDBsum; 1SS2; -.
DR AlphaFoldDB; Q9Z0U4; -.
DR BMRB; Q9Z0U4; -.
DR SMR; Q9Z0U4; -.
DR BioGRID; 249557; 2.
DR ComplexPortal; CPX-404; GABA-B receptor complex.
DR CORUM; Q9Z0U4; -.
DR IntAct; Q9Z0U4; 2.
DR MINT; Q9Z0U4; -.
DR STRING; 10116.ENSRNOP00000047788; -.
DR BindingDB; Q9Z0U4; -.
DR ChEMBL; CHEMBL2753; -.
DR DrugCentral; Q9Z0U4; -.
DR GuidetoPHARMACOLOGY; 240; -.
DR GlyGen; Q9Z0U4; 7 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; Q9Z0U4; -.
DR PhosphoSitePlus; Q9Z0U4; -.
DR PaxDb; Q9Z0U4; -.
DR PRIDE; Q9Z0U4; -.
DR ABCD; Q9Z0U4; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000085050; ENSRNOP00000075181; ENSRNOG00000000774. [Q9Z0U4-1]
DR Ensembl; ENSRNOT00000088396; ENSRNOP00000072226; ENSRNOG00000000774. [Q9Z0U4-3]
DR Ensembl; ENSRNOT00000090936; ENSRNOP00000071413; ENSRNOG00000000774. [Q9Z0U4-2]
DR GeneID; 81657; -.
DR KEGG; rno:81657; -.
DR UCSC; RGD:621537; rat. [Q9Z0U4-1]
DR CTD; 2550; -.
DR RGD; 621537; Gabbr1.
DR eggNOG; KOG1055; Eukaryota.
DR GeneTree; ENSGT00940000157642; -.
DR InParanoid; Q9Z0U4; -.
DR OrthoDB; 590810at2759; -.
DR PhylomeDB; Q9Z0U4; -.
DR TreeFam; TF313965; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-RNO-977444; GABA B receptor activation.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR EvolutionaryTrace; Q9Z0U4; -.
DR PRO; PR:Q9Z0U4; -.
DR Proteomes; UP000002494; Chromosome 20.
DR Bgee; ENSRNOG00000000774; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; Q9Z0U4; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:1902712; C:G protein-coupled GABA receptor complex; IPI:ComplexPortal.
DR GO; GO:0038037; C:G protein-coupled receptor dimeric complex; ISO:RGD.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; ISS:UniProtKB.
DR GO; GO:1902710; C:GABA receptor complex; IDA:CAFA.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:CAFA.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0097060; C:synaptic membrane; IDA:CAFA.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:1990430; F:extracellular matrix protein binding; IMP:CAFA.
DR GO; GO:0004965; F:G protein-coupled GABA receptor activity; IDA:RGD.
DR GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; ISO:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:ComplexPortal.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0033602; P:negative regulation of dopamine secretion; IDA:RGD.
DR GO; GO:0032811; P:negative regulation of epinephrine secretion; IMP:RGD.
DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IMP:RGD.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IDA:RGD.
DR GO; GO:0150099; P:neuron-glial cell signaling; IGI:ARUK-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IMP:RGD.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; IMP:RGD.
DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:RGD.
DR GO; GO:0014048; P:regulation of glutamate secretion; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IC:ComplexPortal.
DR CDD; cd15291; 7tmC_GABA-B-R1; 1.
DR CDD; cd00033; CCP; 1.
DR DisProt; DP00463; -.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR002455; GPCR3_GABA-B.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR002456; GPCR_3_GABA_rcpt_B1.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR10519; PTHR10519; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 2.
DR SUPFAM; SSF53822; SSF53822; 1.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Transducer; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..991
FT /note="Gamma-aminobutyric acid type B receptor subunit 1"
FT /id="PRO_0000012951"
FT TOPO_DOM 17..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..666
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 667..687
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 688..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..797
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 798..818
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 819..834
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..855
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..863
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 864..884
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 885..991
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..95
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 97..158
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT REGION 897..922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..946
FT /note="Interaction with ATF4"
FT /evidence="ECO:0000269|PubMed:10924501"
FT REGION 939..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 901..955
FT /evidence="ECO:0000255"
FT COMPBIAS 897..914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 269
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 286
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 366
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT BINDING 465
FT /ligand="4-aminobutanoate"
FT /ligand_id="ChEBI:CHEBI:59888"
FT /ligand_note="agonist"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS5"
FT MOD_RES 903
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV18"
FT MOD_RES 960
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:15304491"
FT DISULFID 130..156
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302,
FT ECO:0000269|PubMed:15304491"
FT DISULFID 219..245
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 375..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT VAR_SEQ 1..163
FT /note="MLLLLLVPLFLRPLGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVKA
FT INFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGKV
FT FLTGGDLPALDGARVEFRCDPDFHLVGSSRSVCSQGQWSTPKPHCQVNRTPH -> MGP
FT GGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRPHPRVPPHPS (in isoform
FT 1B, isoform 1C and isoform 1D)"
FT /evidence="ECO:0000303|PubMed:9069281,
FT ECO:0000303|PubMed:9875211"
FT /id="VSP_002044"
FT VAR_SEQ 771..801
FT /note="Missing (in isoform 1A, isoform 1B and isoform 1D)"
FT /evidence="ECO:0000303|PubMed:10075644,
FT ECO:0000303|PubMed:9069281, ECO:0000303|PubMed:9875211"
FT /id="VSP_002045"
FT VAR_SEQ 935..991
FT /note="KEERVSELRHQLQSRQQLRSRRHPPTPPDPSGGLPRGPSEPPDRLSCDGSRV
FT HLLYK -> VCGDKQPGPPVSEGGLPVVGPSIEV (in isoform 1D)"
FT /evidence="ECO:0000303|PubMed:9875211"
FT /id="VSP_002046"
FT MUTAGEN 247
FT /note="S->A: No change in the affinity for GABA."
FT /evidence="ECO:0000269|PubMed:10692480"
FT MUTAGEN 268
FT /note="S->A: No change in the affinity for GABA."
FT /evidence="ECO:0000269|PubMed:10692480"
FT MUTAGEN 269
FT /note="S->A: Decrease in the affinity for GABA."
FT /evidence="ECO:0000269|PubMed:10692480"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:1SRZ"
FT HELIX 101..104
FT /evidence="ECO:0007829|PDB:1SRZ"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:1SRZ"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:1SRZ"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1SRZ"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1SRZ"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1SRZ"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:1SRZ"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1SRZ"
SQ SEQUENCE 991 AA; 111534 MW; 012CD293D4B444A2 CRC64;
MLLLLLVPLF LRPLGAGGAQ TPNATSEGCQ IIHPPWEGGI RYRGLTRDQV KAINFLPVDY
EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS KSYLTLENGK VFLTGGDLPA
LDGARVEFRC DPDFHLVGSS RSVCSQGQWS TPKPHCQVNR TPHSERRAVY IGALFPMSGG
WPGGQACQPA VEMALEDVNS RRDILPDYEL KLIHHDSKCD PGQATKYLYE LLYNDPIKII
LMPGCSSVST LVAEAARMWN LIVLSYGSSS PALSNRQRFP TFFRTHPSAT LHNPTRVKLF
EKWGWKKIAT IQQTTEVFTS TLDDLEERVK EAGIEITFRQ SFFSDPAVPV KNLKRQDARI
IVGLFYETEA RKVFCEVYKE RLFGKKYVWF LIGWYADNWF KTYDPSINCT VEEMTEAVEG
HITTEIVMLN PANTRSISNM TSQEFVEKLT KRLKRHPEET GGFQEAPLAY DAIWALALAL
NKTSGGGGRS GVRLEDFNYN NQTITDQIYR AMNSSSFEGV SGHVVFDASG SRMAWTLIEQ
LQGGSYKKIG YYDSTKDDLS WSKTDKWIGG SPPADQTLVI KTFRFLSQKL FISVSVLSSL
GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG YHIGRSQFPF
VCQARLWLLG LGFSLGYGSM FTKIWWVHTV FTKKEEKKEW RKTLEPWKLY ATVGLLVGMD
VLTLAIWQIV DPLHRTIETF AKEEPKEDID VSILPQLEHC SSKKMNTWLG ELWSFAVSSD
VQRRATVGGD SPICVWPAPE SIFYGYKGLL LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY
NVAVLCLITA PVTMILSSQQ DAAFAFASLA IVFSSYITLV VLFVPKMRRL ITRGEWQSET
QDTMKTGSST NNNEEEKSRL LEKENRELEK IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT
PPDPSGGLPR GPSEPPDRLS CDGSRVHLLY K
