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 27-MAR-2024, entry version 197. 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, CC PubMed:10727622). Also expressed in areas of the brain including the CC medial geniculate nucleus, substantia nigra, pars compacta, the ventral CC tegmental area, and in several thalamic, amygdaloid and hypothalamic CC nuclei, such as the arcuate nucleus of the hypothalamus and mammilary CC bodies of the hypothalamus (PubMed:9069281, PubMed:9872744). Expressed CC in the amacrine cell of the retina (PubMed:10924501). Isoform 1A: CC Expressed in the brain, spinal cord, stomach, testis, adrenal gland, CC pituitary, spleen and prostate (PubMed:10658574). Isoform 1B: Expressed CC in the 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 17 dpc 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9Z0U4; 7 sites, 2 glycans. DR GlyGen; Q9Z0U4; 7 sites, 2 N-linked glycans (2 sites). DR iPTMnet; Q9Z0U4; -. DR PhosphoSitePlus; Q9Z0U4; -. DR PaxDb; 10116-ENSRNOP00000047788; -. DR ABCD; Q9Z0U4; 1 sequenced antibody. DR Ensembl; ENSRNOT00000085050.2; ENSRNOP00000075181.2; ENSRNOG00000000774.9. [Q9Z0U4-1] DR Ensembl; ENSRNOT00000088396.2; ENSRNOP00000072226.1; ENSRNOG00000000774.9. [Q9Z0U4-3] DR Ensembl; ENSRNOT00000090936.2; ENSRNOP00000071413.2; ENSRNOG00000000774.9. [Q9Z0U4-2] DR Ensembl; ENSRNOT00055015250; ENSRNOP00055012209; ENSRNOG00055009006. [Q9Z0U4-1] DR Ensembl; ENSRNOT00060005505; ENSRNOP00060004025; ENSRNOG00060003245. [Q9Z0U4-1] DR Ensembl; ENSRNOT00065046663; ENSRNOP00065038265; ENSRNOG00065026733. [Q9Z0U4-1] DR GeneID; 81657; -. DR KEGG; rno:81657; -. DR UCSC; RGD:621537; rat. [Q9Z0U4-1] DR AGR; RGD:621537; -. DR CTD; 2550; -. DR RGD; 621537; Gabbr1. DR eggNOG; KOG1055; Eukaryota. DR GeneTree; ENSGT00940000157642; -. DR InParanoid; Q9Z0U4; -. DR OMA; WAGGEAC; -. DR OrthoDB; 2970339at2759; -. 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 cell types or tissues. DR ExpressionAtlas; Q9Z0U4; baseline and differential. 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:0016020; C:membrane; ISO:RGD. DR GO; GO:0031966; C:mitochondrial membrane; IDA:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:CAFA. DR GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO. DR GO; GO:0098793; C:presynapse; ISO:RGD. DR GO; GO:0042734; C:presynaptic membrane; IDA:SynGO. 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:0150047; F:G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential; ISO:RGD. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:CAFA. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD. DR GO; GO:0099565; P:chemical synaptic transmission, postsynaptic; ISO:RGD. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:ComplexPortal. 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:0060078; P:regulation of postsynaptic membrane potential; ISO: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; NAS:ComplexPortal. DR CDD; cd15291; 7tmC_GABA-B-R1; 1. DR CDD; cd00033; CCP; 1. DR CDD; cd06366; PBP1_GABAb_receptor; 1. DR DisProt; DP00463; -. DR Gene3D; 3.40.50.2300; -; 2. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. 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; GABA-B RECEPTOR; 1. DR PANTHER; PTHR10519:SF76; GAMMA-AMINOBUTYRIC ACID TYPE B RECEPTOR SUBUNIT 1; 1. DR Pfam; PF00003; 7tm_3; 1. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00084; Sushi; 1. DR PRINTS; PR01177; GABAB1RECPTR. DR PRINTS; PR01176; GABABRECEPTR. DR SMART; SM00032; CCP; 2. DR SUPFAM; SSF57535; Complement control module/SCR domain; 2. DR SUPFAM; SSF53822; Periplasmic binding protein-like I; 1. 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 //