ID GABR1_HUMAN Reviewed; 961 AA. AC Q9UBS5; B0UXY7; O95375; O95468; O95975; O96022; Q5STL4; Q5SUJ8; Q5SUL3; AC Q71SG6; Q86W60; Q9UQQ0; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 216. 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; Synonyms=GPRC3A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), FUNCTION, SUBCELLULAR RP LOCATION, TISSUE SPECIFICITY, AND DOMAIN. RC TISSUE=Cerebellum {ECO:0000303|PubMed:9844003}; RX PubMed=9844003; DOI=10.1073/pnas.95.25.14991; RA Kaupmann K., Schuler V., Mosbacher J., Bischoff S., Bittiger H., Heid J., RA Froestl W., Leonhard S., Pfaff T., Karschin A., Bettler B.; RT "Human gamma-aminobutyric acid type B receptors are differentially RT expressed and regulate inwardly rectifying K+ channels."; RL Proc. Natl. Acad. Sci. U.S.A. 95:14991-14996(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 1C), FUNCTION, SUBUNIT, RP INTERACTION WITH GABBR2, AND SUBCELLULAR LOCATION. RC TISSUE=Cerebellum {ECO:0000303|PubMed:9872316}; RX PubMed=9872316; DOI=10.1038/25354; RA White J.H., Wise A., Main M.J., Green A., Fraser N.J., Disney G.H., RA Barnes A.A., Emson P., Foord S.M., Marshall F.H.; RT "Heterodimerization is required for the formation of a functional GABA(B) RT receptor."; RL Nature 396:679-682(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A). RC TISSUE=Brain {ECO:0000303|Ref.3}; RA Stropp U., Raming K.; RT "Human mRNA for GABA-B1a receptor."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain {ECO:0000303|PubMed:9753614}; RX PubMed=9753614; DOI=10.1006/bbrc.1998.9296; RA Grifa A., Totaro A., Rommens J.M., Carella M., Roetto A., Borgato L., RA Zelante L., Gasparini P.; RT "GABA (gamma-amino-butyric acid) neurotransmission: identification and fine RT mapping of the human GABAB receptor gene."; RL Biochem. Biophys. Res. Commun. 250:240-245(1998). RN [5] RP NUCLEOTIDE SEQUENCE (ISOFORM 1A). RX PubMed=9798068; DOI=10.1016/s0006-3223(98)00244-3; RA Goei V.L., Choi J., Ahn J., Bowlus C.L., Raha-Chowdhury R., Gruen J.R.; RT "Human gamma-aminobutyric acid B receptor gene: complementary DNA cloning, RT expression, chromosomal location, and genomic organization."; RL Biol. Psychiatry 44:659-666(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C). RC TISSUE=Cerebellum {ECO:0000303|Ref.6}; RA Fraser N.J.; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A AND 1B), AND VARIANTS VAL-20 RP AND SER-489. RC TISSUE=Fetal brain {ECO:0000303|PubMed:9933300}; RX PubMed=9933300; DOI=10.1007/s100480050051; RA Peters H.C., Kaemmer G., Volz A., Kaupmann K., Ziegler A., Bettler B., RA Epplen J.T., Sander T., Riess O.; RT "Mapping, genomic structure, and polymorphisms of the human GABABR1 RT receptor gene: evaluation of its involvement in idiopathic generalized RT epilepsy."; RL Neurogenetics 2:47-54(1998). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A). RC TISSUE=Cerebellum {ECO:0000303|PubMed:9889352}; RX PubMed=9889352; DOI=10.1016/s0169-328x(98)00316-7; RA Makoff A.; RT "Molecular cloning of human GABABR1 and its tissue distribution."; RL Brain Res. Mol. Brain Res. 64:137-140(1999). RN [9] RP NUCLEOTIDE SEQUENCE (ISOFORM 1E), FUNCTION, SUBUNIT, INTERACTION WITH RP GABBR2, TISSUE SPECIFICITY, AND VARIANT SER-489. RC TISSUE=Prostate {ECO:0000303|PubMed:10906333}; RX PubMed=10906333; DOI=10.1074/jbc.m005333200; RA Schwarz D.A., Barry G., Eliasof S.D., Petroski R.E., Conlon P.J., RA Maki R.A.; RT "Characterization of gamma-aminobutyric acid receptor GABAB(1e), a GABAB(1) RT splice variant encoding a truncated receptor."; RL J. Biol. Chem. 275:32174-32181(2000). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-20. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B). RC TISSUE=Brain {ECO:0000303|PubMed:15489334}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [13] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [14] RP FUNCTION, AND INTERACTION WITH GABBR2. RX PubMed=10773016; RA Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr., RA Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K., Abramovitz M., RA O'Neill G.P., Ng G.Y.K.; RT "Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B)) receptors RT with truncated receptors and metabotropic glutamate receptor 4 supports the RT GABA(B) heterodimer as the functional receptor."; RL J. Pharmacol. Exp. Ther. 293:460-467(2000). RN [15] RP FUNCTION. 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 [16] RP FUNCTION, INTERACTION WITH GABBR2, TISSUE SPECIFICITY, AND DOMAIN. 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 [17] RP INTERACTION WITH JAKMIP1. 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 [18] RP FUNCTION, INTERACTION WITH GABBR2, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=15617512; DOI=10.1042/bj20041435; RA Villemure J.F., Adam L., Bevan N.J., Gearing K., Chenier S., Bouvier M.; RT "Subcellular distribution of GABA(B) receptor homo- and hetero-dimers."; RL Biochem. J. 388:47-55(2005). RN [19] RP FUNCTION, AND INTERACTION WITH GABBR2. RX PubMed=18165688; DOI=10.1074/jbc.m705202200; RA Nomura R., Suzuki Y., Kakizuka A., Jingami H.; RT "Direct detection of the interaction between recombinant soluble RT extracellular regions in the heterodimeric metabotropic gamma-aminobutyric RT acid receptor."; RL J. Biol. Chem. 283:4665-4673(2008). RN [20] RP FUNCTION, PARTIAL PROTEIN SEQUENCE, AGONIST BINDING, MUTAGENESIS OF TYR-230 RP AND TYR-234, AND INTERACTION WITH GABBR2. RX PubMed=22660477; DOI=10.1038/nn.3133; RA Geng Y., Xiong D., Mosyak L., Malito D.L., Kniazeff J., Chen Y., RA Burmakina S., Quick M., Bush M., Javitch J.A., Pin J.P., Fan Q.R.; RT "Structure and functional interaction of the extracellular domain of human RT GABA(B) receptor GBR2."; RL Nat. Neurosci. 15:970-978(2012). RN [21] {ECO:0007744|PDB:4MQE, ECO:0007744|PDB:4MQF, ECO:0007744|PDB:4MR7, ECO:0007744|PDB:4MR8, ECO:0007744|PDB:4MR9, ECO:0007744|PDB:4MRM, ECO:0007744|PDB:4MS1, ECO:0007744|PDB:4MS3, ECO:0007744|PDB:4MS4} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 165-576 IN COMPLEXES WITH GABBR2; RP AGONISTS AND ANTAGONISTS, FUNCTION, SUBUNIT, DISULFIDE BOND, GLYCOSYLATION RP AT ASN-440 AND ASN-482, AND MUTAGENESIS OF TRP-182; HIS-287; TYR-367 AND RP TRP-395. RX PubMed=24305054; DOI=10.1038/nature12725; RA Geng Y., Bush M., Mosyak L., Wang F., Fan Q.R.; RT "Structural mechanism of ligand activation in human GABA(B) receptor."; RL Nature 504:254-259(2013). RN [22] RP VARIANTS VAL-20 AND SER-489. RX PubMed=10402495; RX DOI=10.1002/(sici)1096-8628(19990820)88:4<305::aid-ajmg5>3.0.co;2-x; RA Sander T., Peters C., Kaemmer G., Samochowiec J., Zirra M., Mischke D., RA Ziegler A., Kaupmann K., Bettler B., Epplen J.T., Riess O.; RT "Association analysis of exonic variants of the gene encoding the GABAB RT receptor and idiopathic generalized epilepsy."; RL Am. J. Med. Genet. 88:305-310(1999). CC -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for CC GABA, formed by GABBR1 and GABBR2 (PubMed:9872316, PubMed:9872744, CC PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054). CC Within the heterodimeric GABA receptor, only GABBR1 seems to bind CC agonists, while GABBR2 mediates coupling to G proteins CC (PubMed:18165688). Ligand binding causes a conformation change that CC triggers signaling via guanine nucleotide-binding proteins (G proteins) CC and modulates the activity of down-stream effectors, such as adenylate CC cyclase (PubMed:10906333, PubMed:10773016, PubMed:10075644, CC PubMed:9872744, PubMed:24305054). Signaling inhibits adenylate cyclase, CC stimulates phospholipase A2, activates potassium channels, inactivates CC voltage-dependent calcium-channels and modulates inositol phospholipid CC hydrolysis (PubMed:10075644). Calcium is required for high affinity CC binding to GABA (By similarity). Plays a critical role in the fine- CC tuning of inhibitory synaptic transmission (PubMed:9844003). Pre- CC synaptic GABA receptor inhibits neurotransmitter release by down- CC regulating high-voltage activated calcium channels, whereas CC 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:9844003, PubMed:9872316, PubMed:10075644, PubMed:9872744, CC PubMed:22660477). Not only implicated in synaptic inhibition but also CC in hippocampal long-term potentiation, slow wave sleep, muscle CC relaxation and antinociception (Probable). Activated by (-)-baclofen, CC cgp27492 and blocked by phaclofen (PubMed:9844003, PubMed:9872316, CC PubMed:24305054). {ECO:0000250|UniProtKB:Q9Z0U4, CC ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10773016, CC ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:15617512, CC ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, CC ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9844003, CC ECO:0000269|PubMed:9872316, ECO:0000269|PubMed:9872744, ECO:0000305}. CC -!- FUNCTION: Isoform 1E may regulate the formation of functional CC GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could CC explain the observation that certain small molecule ligands exhibit CC differential affinity for central versus peripheral sites. CC -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872316, CC PubMed:10773016, PubMed:9872744, PubMed:15617512, PubMed:18165688, CC PubMed:22660477, PubMed:24305054). Homodimers may form, but are CC inactive (PubMed:9872316, PubMed:15617512). Isoform 1E (without C- CC terminal intracellular domain) is unable to dimerize via a coiled-coil CC interaction with GABBR2 (PubMed:10906333). Interacts (via C-terminus) CC with ATF4 (via leucine zipper domain) (By similarity). Interacts with CC JAKMIP1 (PubMed:14718537). {ECO:0000250|UniProtKB:Q9Z0U4, CC ECO:0000269|PubMed:10773016, ECO:0000269|PubMed:10906333, CC ECO:0000269|PubMed:14718537, ECO:0000269|PubMed:15617512, CC ECO:0000269|PubMed:18165688, ECO:0000269|PubMed:22660477, CC ECO:0000269|PubMed:24305054, ECO:0000269|PubMed:9872316, CC ECO:0000269|PubMed:9872744}. CC -!- INTERACTION: CC Q9UBS5; O75899: GABBR2; NbExp=4; IntAct=EBI-724156, EBI-715469; CC Q9UBS5; O15354: GPR37; NbExp=2; IntAct=EBI-724156, EBI-15639515; CC Q9UBS5; P61244: MAX; NbExp=3; IntAct=EBI-724156, EBI-751711; CC Q9UBS5; P16333: NCK1; NbExp=3; IntAct=EBI-724156, EBI-389883; CC Q9UBS5; P46459: NSF; NbExp=3; IntAct=EBI-724156, EBI-712251; CC Q9UBS5-2; O75899: GABBR2; NbExp=6; IntAct=EBI-16084001, EBI-715469; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15617512}; CC Multi-pass membrane protein {ECO:0000305}. Postsynaptic cell membrane CC {ECO:0000250|UniProtKB:Q9Z0U4}; Multi-pass membrane protein CC {ECO:0000305}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:Q9Z0U4}. Note=Colocalizes with ATF4 in CC hippocampal neuron dendritic membranes (By similarity). Coexpression of CC GABBR1 and GABBR2 is required for GABBR1 maturation and transport to CC the plasma membrane (PubMed:15617512). {ECO:0000250|UniProtKB:Q9Z0U4, CC ECO:0000269|PubMed:15617512}. CC -!- SUBCELLULAR LOCATION: [Isoform 1E]: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Isoforms corresponding to the full receptor are essentially CC found in the central nervous system (CNS).; CC Name=1A; CC IsoId=Q9UBS5-1; Sequence=Displayed; CC Name=1B; CC IsoId=Q9UBS5-2; Sequence=VSP_002037; CC Name=1C; CC IsoId=Q9UBS5-3; Sequence=VSP_002038; CC Name=1D; CC IsoId=Q9UBS5-4; Sequence=VSP_002040; CC Name=1E; Synonyms=Truncated; CC IsoId=Q9UBS5-5; Sequence=VSP_002039; CC -!- TISSUE SPECIFICITY: Highly expressed in brain (PubMed:9844003, CC PubMed:9753614, PubMed:9872744). Weakly expressed in heart, small CC intestine and uterus. Isoform 1A: Mainly expressed in granular cell and CC molecular layer (PubMed:9844003). Isoform 1B: Mainly expressed in CC Purkinje cells (PubMed:9844003). Isoform 1E: Predominantly expressed in CC peripheral tissues as kidney, lung, trachea, colon, small intestine, CC stomach, bone marrow, thymus and mammary gland (PubMed:10906333). CC {ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:9753614, CC ECO:0000269|PubMed:9844003, ECO:0000269|PubMed:9872744}. CC -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region CC mediate heterodimeric interaction with GABBR2 (PubMed:9872744). The CC linker region between the transmembrane domain 3 (TM3) and the CC transmembrane domain 4 (TM4) probably plays a role in the specificity CC for G-protein coupling (PubMed:9844003). {ECO:0000305|PubMed:9844003, CC ECO:0000305|PubMed:9872744}. CC -!- MISCELLANEOUS: [Isoform 1E]: Major isoform in almost all peripheral CC tissues, although containing a premature stop codon in the mRNA and CC thus being a potential target for nonsense-mediated mRNA decay. May act CC as an antagonist of GABA-B receptors, being able to disrupt the normal CC association between isoform 1A and GABBR2. CC {ECO:0000269|PubMed:10906333}. 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; AJ225028; CAA12359.1; -; mRNA. DR EMBL; AJ225029; CAA12360.1; -; mRNA. DR EMBL; AJ012185; CAA09939.1; -; mRNA. DR EMBL; AJ012186; CAA09940.1; -; mRNA. DR EMBL; AF099148; AAC98508.1; -; mRNA. DR EMBL; Y11044; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AJ012187; CAA09941.1; -; mRNA. DR EMBL; AJ010170; CAA09031.1; -; Genomic_DNA. DR EMBL; AJ010171; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010172; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010173; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010174; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010175; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010176; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010177; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010178; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010179; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010180; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010181; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010182; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010183; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010184; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010185; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010186; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010187; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010188; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010189; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010190; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ010191; CAA09031.1; JOINED; Genomic_DNA. DR EMBL; AJ012288; CAA09980.1; -; mRNA. DR EMBL; AF301005; AAG23962.1; -; mRNA. DR EMBL; AL031983; CAA21453.1; -; Genomic_DNA. DR EMBL; AL031983; CAA21454.1; -; Genomic_DNA. DR EMBL; AL645936; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX000688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR388210; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759766; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759870; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788300; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936483; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03205.1; -; Genomic_DNA. DR EMBL; CH471081; EAX03210.1; -; Genomic_DNA. DR EMBL; BC042598; AAH42598.1; -; mRNA. DR EMBL; BC050532; AAH50532.2; -; mRNA. DR CCDS; CCDS4663.1; -. [Q9UBS5-1] DR CCDS; CCDS4664.1; -. [Q9UBS5-3] DR CCDS; CCDS4665.1; -. [Q9UBS5-2] DR PIR; JE0356; JE0356. DR RefSeq; NP_001305982.1; NM_001319053.1. DR RefSeq; NP_001461.1; NM_001470.3. [Q9UBS5-1] DR RefSeq; NP_068703.1; NM_021903.2. [Q9UBS5-2] DR RefSeq; NP_068704.2; NM_021904.3. [Q9UBS5-3] DR PDB; 4MQE; X-ray; 2.35 A; A=165-576. DR PDB; 4MQF; X-ray; 2.22 A; A=165-576. DR PDB; 4MR7; X-ray; 2.15 A; A=165-576. DR PDB; 4MR8; X-ray; 2.15 A; A=165-576. DR PDB; 4MR9; X-ray; 2.35 A; A=165-576. DR PDB; 4MRM; X-ray; 2.86 A; A=165-576. DR PDB; 4MS1; X-ray; 2.25 A; A=165-576. DR PDB; 4MS3; X-ray; 2.50 A; A=165-576. DR PDB; 4MS4; X-ray; 1.90 A; A=165-576. DR PDB; 4PAS; X-ray; 1.62 A; A=879-919. DR PDB; 6HKC; NMR; -; A=26-98. DR PDB; 6UO8; EM; 3.63 A; A=165-919. DR PDB; 6UO9; EM; 4.80 A; A=165-919. DR PDB; 6UOA; EM; 6.30 A; A=165-919. DR PDB; 6VJM; EM; 3.97 A; A=165-919. DR PDB; 6W2X; EM; 3.60 A; A=153-961. DR PDB; 6W2Y; EM; 3.20 A; A/B=153-961. DR PDB; 6WIV; EM; 3.30 A; A=153-919. DR PDB; 7C7Q; EM; 3.00 A; A=15-862. DR PDB; 7C7S; EM; 2.90 A; A=15-919. DR PDB; 7CA3; EM; 4.50 A; A=165-900. DR PDB; 7CA5; EM; 7.60 A; A=165-900. DR PDB; 7CUM; EM; 3.52 A; A=165-900. DR PDB; 7EB2; EM; 3.50 A; C=15-919. DR PDBsum; 4MQE; -. DR PDBsum; 4MQF; -. DR PDBsum; 4MR7; -. DR PDBsum; 4MR8; -. DR PDBsum; 4MR9; -. DR PDBsum; 4MRM; -. DR PDBsum; 4MS1; -. DR PDBsum; 4MS3; -. DR PDBsum; 4MS4; -. DR PDBsum; 4PAS; -. DR PDBsum; 6HKC; -. DR PDBsum; 6UO8; -. DR PDBsum; 6UO9; -. DR PDBsum; 6UOA; -. DR PDBsum; 6VJM; -. DR PDBsum; 6W2X; -. DR PDBsum; 6W2Y; -. DR PDBsum; 6WIV; -. DR PDBsum; 7C7Q; -. DR PDBsum; 7C7S; -. DR PDBsum; 7CA3; -. DR PDBsum; 7CA5; -. DR PDBsum; 7CUM; -. DR PDBsum; 7EB2; -. DR AlphaFoldDB; Q9UBS5; -. DR EMDB; EMD-20822; -. DR EMDB; EMD-20823; -. DR EMDB; EMD-20824; -. DR EMDB; EMD-21219; -. DR EMDB; EMD-21533; -. DR EMDB; EMD-21534; -. DR EMDB; EMD-21685; -. DR EMDB; EMD-30300; -. DR EMDB; EMD-30301; -. DR EMDB; EMD-30323; -. DR EMDB; EMD-30324; -. DR EMDB; EMD-30472; -. DR EMDB; EMD-31049; -. DR SMR; Q9UBS5; -. DR BioGRID; 108825; 39. DR ComplexPortal; CPX-2955; GABA-B receptor complex. DR CORUM; Q9UBS5; -. DR DIP; DIP-38394N; -. DR IntAct; Q9UBS5; 16. DR MINT; Q9UBS5; -. DR STRING; 9606.ENSP00000366233; -. DR BindingDB; Q9UBS5; -. DR ChEMBL; CHEMBL2064; -. DR DrugBank; DB00659; Acamprosate. DR DrugBank; DB08891; Arbaclofen. DR DrugBank; DB08892; Arbaclofen Placarbil. DR DrugBank; DB00181; Baclofen. DR DrugBank; DB02530; gamma-Aminobutyric acid. DR DrugBank; DB12098; L-Baclofen. DR DrugBank; DB00837; Progabide. DR DrugBank; DB05010; SGS-742. DR DrugBank; DB09072; Sodium oxybate. DR DrugBank; DB01956; Taurine. DR DrugBank; DB06354; Tezampanel. DR DrugCentral; Q9UBS5; -. DR GuidetoPHARMACOLOGY; 240; -. DR GlyCosmos; Q9UBS5; 7 sites, No reported glycans. DR GlyGen; Q9UBS5; 7 sites. DR iPTMnet; Q9UBS5; -. DR PhosphoSitePlus; Q9UBS5; -. DR BioMuta; GABBR1; -. DR DMDM; 12643873; -. DR jPOST; Q9UBS5; -. DR MassIVE; Q9UBS5; -. DR PaxDb; 9606-ENSP00000366233; -. DR PeptideAtlas; Q9UBS5; -. DR ProteomicsDB; 84047; -. [Q9UBS5-1] DR ProteomicsDB; 84048; -. [Q9UBS5-2] DR ProteomicsDB; 84049; -. [Q9UBS5-3] DR ProteomicsDB; 84050; -. [Q9UBS5-4] DR ProteomicsDB; 84051; -. [Q9UBS5-5] DR ABCD; Q9UBS5; 1 sequenced antibody. DR Antibodypedia; 50418; 628 antibodies from 44 providers. DR DNASU; 2550; -. DR Ensembl; ENST00000355973.7; ENSP00000348248.3; ENSG00000204681.11. [Q9UBS5-2] DR Ensembl; ENST00000377012.9; ENSP00000366211.4; ENSG00000204681.11. [Q9UBS5-2] DR Ensembl; ENST00000377016.8; ENSP00000366215.4; ENSG00000204681.11. [Q9UBS5-3] DR Ensembl; ENST00000377034.9; ENSP00000366233.4; ENSG00000204681.11. [Q9UBS5-1] DR Ensembl; ENST00000383537.8; ENSP00000373029.4; ENSG00000206466.10. [Q9UBS5-2] DR Ensembl; ENST00000383541.8; ENSP00000373033.4; ENSG00000206466.10. [Q9UBS5-3] DR Ensembl; ENST00000383542.8; ENSP00000373034.4; ENSG00000206466.10. [Q9UBS5-1] DR Ensembl; ENST00000383543.7; ENSP00000373035.3; ENSG00000206466.10. [Q9UBS5-2] DR Ensembl; ENST00000383636.8; ENSP00000373132.4; ENSG00000206511.10. [Q9UBS5-2] DR Ensembl; ENST00000383637.8; ENSP00000373133.4; ENSG00000206511.10. [Q9UBS5-3] DR Ensembl; ENST00000383638.8; ENSP00000373134.4; ENSG00000206511.10. [Q9UBS5-1] DR Ensembl; ENST00000383639.6; ENSP00000373135.2; ENSG00000206511.10. [Q9UBS5-2] DR Ensembl; ENST00000414980.6; ENSP00000406499.2; ENSG00000232632.8. [Q9UBS5-2] DR Ensembl; ENST00000417759.5; ENSP00000391572.1; ENSG00000237112.8. [Q9UBS5-2] DR Ensembl; ENST00000419674.5; ENSP00000399861.1; ENSG00000232569.8. [Q9UBS5-3] DR Ensembl; ENST00000423604.6; ENSP00000388035.2; ENSG00000232632.8. [Q9UBS5-1] DR Ensembl; ENST00000425097.6; ENSP00000411286.2; ENSG00000237112.8. [Q9UBS5-1] DR Ensembl; ENST00000434660.6; ENSP00000412167.2; ENSG00000232632.8. [Q9UBS5-3] DR Ensembl; ENST00000438094.5; ENSP00000406285.1; ENSG00000232632.8. [Q9UBS5-2] DR Ensembl; ENST00000439457.5; ENSP00000406066.1; ENSG00000232569.8. [Q9UBS5-1] DR Ensembl; ENST00000443440.6; ENSP00000399318.2; ENSG00000237112.8. [Q9UBS5-3] DR Ensembl; ENST00000446436.6; ENSP00000394528.2; ENSG00000237112.8. [Q9UBS5-2] DR Ensembl; ENST00000448754.5; ENSP00000405709.1; ENSG00000237051.8. [Q9UBS5-2] DR Ensembl; ENST00000449163.5; ENSP00000411263.1; ENSG00000232569.8. [Q9UBS5-2] DR Ensembl; ENST00000452300.6; ENSP00000408938.2; ENSG00000232569.8. [Q9UBS5-2] DR Ensembl; ENST00000458612.6; ENSP00000416903.2; ENSG00000237051.8. [Q9UBS5-2] DR Ensembl; ENST00000462632.6; ENSP00000419755.2; ENSG00000204681.11. [Q9UBS5-1] DR Ensembl; ENST00000494877.5; ENSP00000419061.1; ENSG00000204681.11. [Q9UBS5-5] DR Ensembl; ENST00000546913.2; ENSP00000448999.1; ENSG00000232569.8. [Q9UBS5-1] DR Ensembl; ENST00000547410.5; ENSP00000448531.1; ENSG00000232569.8. [Q9UBS5-5] DR Ensembl; ENST00000548767.2; ENSP00000446983.1; ENSG00000232632.8. [Q9UBS5-5] DR Ensembl; ENST00000551140.2; ENSP00000448654.1; ENSG00000237112.8. [Q9UBS5-5] DR Ensembl; ENST00000551423.2; ENSP00000449342.1; ENSG00000206511.10. [Q9UBS5-5] DR Ensembl; ENST00000552399.2; ENSP00000449449.1; ENSG00000206466.10. [Q9UBS5-5] DR Ensembl; ENST00000706533.1; ENSP00000516435.1; ENSG00000204681.11. [Q9UBS5-1] DR GeneID; 2550; -. DR KEGG; hsa:2550; -. DR MANE-Select; ENST00000377034.9; ENSP00000366233.4; NM_001470.4; NP_001461.1. DR UCSC; uc003nmp.5; human. [Q9UBS5-1] DR AGR; HGNC:4070; -. DR CTD; 2550; -. DR DisGeNET; 2550; -. DR GeneCards; GABBR1; -. DR HGNC; HGNC:4070; GABBR1. DR HPA; ENSG00000204681; Tissue enriched (brain). DR MalaCards; GABBR1; -. DR MIM; 603540; gene. DR neXtProt; NX_Q9UBS5; -. DR OpenTargets; ENSG00000204681; -. DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability. DR PharmGKB; PA28484; -. DR VEuPathDB; HostDB:ENSG00000204681; -. DR eggNOG; KOG1055; Eukaryota. DR GeneTree; ENSGT00940000157642; -. DR HOGENOM; CLU_005240_2_0_1; -. DR InParanoid; Q9UBS5; -. DR OMA; WAGGEAC; -. DR OrthoDB; 2970339at2759; -. DR PhylomeDB; Q9UBS5; -. DR TreeFam; TF313965; -. DR PathwayCommons; Q9UBS5; -. DR Reactome; R-HSA-1296041; Activation of G protein gated Potassium channels. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR Reactome; R-HSA-420499; Class C/3 (Metabotropic glutamate/pheromone receptors). DR Reactome; R-HSA-977444; GABA B receptor activation. DR Reactome; R-HSA-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits. DR SignaLink; Q9UBS5; -. DR SIGNOR; Q9UBS5; -. DR BioGRID-ORCS; 2550; 23 hits in 1166 CRISPR screens. DR ChiTaRS; GABBR1; human. DR GeneWiki; GABBR1; -. DR GenomeRNAi; 2550; -. DR Pharos; Q9UBS5; Tclin. DR PRO; PR:Q9UBS5; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9UBS5; Protein. DR Bgee; ENSG00000204681; Expressed in right hemisphere of cerebellum and 128 other cell types or tissues. DR ExpressionAtlas; Q9UBS5; baseline and differential. DR GO; GO:0030673; C:axolemma; IEA:Ensembl. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:1902712; C:G protein-coupled GABA receptor complex; IPI:ComplexPortal. DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; IPI:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl. DR GO; GO:1990430; F:extracellular matrix protein binding; IEA:Ensembl. DR GO; GO:0004965; F:G protein-coupled GABA receptor activity; IDA:UniProtKB. DR GO; GO:0099579; F:G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential; IEA:Ensembl. DR GO; GO:0150047; F:G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential; IEA:Ensembl. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl. DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0033602; P:negative regulation of dopamine secretion; IEA:Ensembl. DR GO; GO:0032811; P:negative regulation of epinephrine secretion; IEA:Ensembl. DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IEA:Ensembl. DR GO; GO:0050805; P:negative regulation of synaptic transmission; IEA:Ensembl. DR GO; GO:0150099; P:neuron-glial cell signaling; ISS:ARUK-UCL. DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl. DR GO; GO:0014049; P:positive regulation of glutamate secretion; IEA:Ensembl. DR GO; GO:0060124; P:positive regulation of growth hormone secretion; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl. 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 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. DR Genevisible; Q9UBS5; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Coiled coil; Direct protein sequencing; Disulfide bond; KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein; KW Postsynaptic cell membrane; Receptor; Reference proteome; Repeat; Secreted; KW Signal; Sushi; Synapse; Transducer; Transmembrane; Transmembrane helix. FT SIGNAL 1..14 FT /evidence="ECO:0000255" FT CHAIN 15..961 FT /note="Gamma-aminobutyric acid type B receptor subunit 1" FT /id="PRO_0000012949" FT TOPO_DOM 15..591 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 592..612 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 613..631 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 632..652 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 653..667 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 668..688 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 689..710 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 711..731 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 732..768 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 769..789 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 790..804 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 805..825 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 826..833 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 834..854 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 855..961 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 30..96 FT /note="Sushi 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DOMAIN 98..159 FT /note="Sushi 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT REGION 867..892 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 888..916 FT /note="Interaction with ATF4" FT /evidence="ECO:0000250" FT REGION 909..961 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 869..925 FT /evidence="ECO:0000255" FT COMPBIAS 867..884 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 927..946 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 247 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS3" FT BINDING 247 FT /ligand="baclofen" FT /ligand_id="ChEBI:CHEBI:187893" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS4" FT BINDING 247 FT /ligand="phaclofen" FT /ligand_id="ChEBI:CHEBI:188150" FT /ligand_note="antagonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MRM" FT BINDING 270 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS3" FT BINDING 270 FT /ligand="baclofen" FT /ligand_id="ChEBI:CHEBI:187893" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS4" FT BINDING 270 FT /ligand="phaclofen" FT /ligand_id="ChEBI:CHEBI:188150" FT /ligand_note="antagonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MRM" FT BINDING 287 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS3" FT BINDING 287 FT /ligand="baclofen" FT /ligand_id="ChEBI:CHEBI:187893" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS4" FT BINDING 287 FT /ligand="phaclofen" FT /ligand_id="ChEBI:CHEBI:188150" FT /ligand_note="antagonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MRM" FT BINDING 367 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS3" FT BINDING 367 FT /ligand="baclofen" FT /ligand_id="ChEBI:CHEBI:187893" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS4" FT BINDING 466 FT /ligand="4-aminobutanoate" FT /ligand_id="ChEBI:CHEBI:59888" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS3" FT BINDING 466 FT /ligand="baclofen" FT /ligand_id="ChEBI:CHEBI:187893" FT /ligand_note="agonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MS4" FT BINDING 466 FT /ligand="phaclofen" FT /ligand_id="ChEBI:CHEBI:188150" FT /ligand_note="antagonist" FT /evidence="ECO:0000269|PubMed:24305054, FT ECO:0007744|PDB:4MR7" FT MOD_RES 873 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV18" FT MOD_RES 930 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9WV18" FT CARBOHYD 24 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 84 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 409 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 440 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24305054" FT CARBOHYD 482 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:24305054" FT CARBOHYD 502 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 514 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 100..145 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 131..157 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302" FT DISULFID 220..246 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:24305054" FT DISULFID 376..410 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302, FT ECO:0000269|PubMed:24305054" FT VAR_SEQ 1..164 FT /note="MLLLLLLAPLFLRPPGAGGAQTPNATSEGCQIIHPPWEGGIRYRGLTRDQVK FT AINFLPVDYEIEYVCRGEREVVGPKVRKCLANGSWTDMDTPSRCVRICSKSYLTLENGK FT VFLTGGDLPALDGARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH -> MG FT PGAPFARVGWPLPLLVVMAAGVAPVWASHSPHLPRPHSRVPPHPS (in isoform FT 1B)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9844003, ECO:0000303|PubMed:9872316" FT /id="VSP_002037" FT VAR_SEQ 98..159 FT /note="Missing (in isoform 1C)" FT /evidence="ECO:0000303|PubMed:9872316, ECO:0000303|Ref.6" FT /id="VSP_002038" FT VAR_SEQ 570..961 FT /note="GGSPPADQTLVIKTFRFLSQKLFISVSVLSSLGIVLAVVCLSFNIYNSHVRY FT IQNSQPNLNNLTAVGCSLALAAVFPLGLDGYHIGRNQFPFVCQARLWLLGLGFSLGYGS FT MFTKIWWVHTVFTKKEEKKEWRKTLEPWKLYATVGLLVGMDVLTLAIWQIVDPLHRTIE FT TFAKEEPKEDIDVSILPQLEHCSSRKMNTWLGIFYGYKGLLLLLGIFLAYETKSVSTEK FT INDHRAVGMAIYNVAVLCLITAPVTMILSSQQDAAFAFASLAIVFSSYITLVVLFVPKM FT RRLITRGEWQSEAQDTMKTGSSTNNNEEEKSRLLEKENRELEKIIAEKEERVSELRHQL FT QSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRVHLLYK -> VISRTHSPT FT (in isoform 1E)" FT /evidence="ECO:0000305" FT /id="VSP_002039" FT VAR_SEQ 905..961 FT /note="KEERVSELRHQLQSRQQLRSRRHPPTPPEPSGGLPRGPPEPPDRLSCDGSRV FT HLLYK -> SGGLPRGPPEPPDRLSCDGSRVHLLYK (in isoform 1D)" FT /evidence="ECO:0000305" FT /id="VSP_002040" FT VARIANT 20 FT /note="A -> V (in dbSNP:rs1805056)" FT /evidence="ECO:0000269|PubMed:10402495, FT ECO:0000269|PubMed:14574404, ECO:0000269|PubMed:9933300" FT /id="VAR_010146" FT VARIANT 489 FT /note="G -> S (in dbSNP:rs1805057)" FT /evidence="ECO:0000269|PubMed:10402495, FT ECO:0000269|PubMed:10906333, ECO:0000269|PubMed:9933300" FT /id="VAR_010147" FT VARIANT 645 FT /note="F -> L (in dbSNP:rs2076489)" FT /id="VAR_049279" FT MUTAGEN 182 FT /note="W->A: Abolishes signaling via G-proteins. Abolishes FT antagonist binding." FT /evidence="ECO:0000269|PubMed:24305054" FT MUTAGEN 230 FT /note="Y->A: Slightly decreases signaling via G-proteins." FT /evidence="ECO:0000269|PubMed:22660477" FT MUTAGEN 234 FT /note="Y->A: Decreases signaling via G-proteins." FT /evidence="ECO:0000269|PubMed:22660477" FT MUTAGEN 287 FT /note="H->A: Strongly reduces signaling via G-proteins. FT Abolishes antagonist binding." FT /evidence="ECO:0000269|PubMed:24305054" FT MUTAGEN 367 FT /note="Y->A: Strongly reduces signaling via G-proteins. No FT effect on antagonist binding." FT /evidence="ECO:0000269|PubMed:24305054" FT MUTAGEN 395 FT /note="W->A: Strongly reduces signaling via G-proteins. FT Strongly reduces antagonist binding." FT /evidence="ECO:0000269|PubMed:24305054" FT CONFLICT 2 FT /note="L -> M (in Ref. 4; Y11044)" FT /evidence="ECO:0000305" FT CONFLICT 21 FT /note="Q -> H (in Ref. 2; CAA09939/CAA09941)" FT /evidence="ECO:0000305" FT CONFLICT 93 FT /note="P -> L (in Ref. 3; AAC98508)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="V -> A (in Ref. 2; CAA09939)" FT /evidence="ECO:0000305" FT CONFLICT 322 FT /note="Missing (in Ref. 7; CAA09031)" FT /evidence="ECO:0000305" FT CONFLICT 542 FT /note="L -> P (in Ref. 4; Y11044)" FT /evidence="ECO:0000305" FT CONFLICT 691 FT /note="V -> G (in Ref. 4; Y11044)" FT /evidence="ECO:0000305" FT CONFLICT 905..934 FT /note="Missing (in Ref. 7; CAA09031)" FT /evidence="ECO:0000305" FT STRAND 37..42 FT /evidence="ECO:0007829|PDB:6HKC" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:6HKC" FT STRAND 62..67 FT /evidence="ECO:0007829|PDB:6HKC" FT TURN 68..70 FT /evidence="ECO:0007829|PDB:6HKC" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:6HKC" FT STRAND 79..81 FT /evidence="ECO:0007829|PDB:6HKC" FT STRAND 83..89 FT /evidence="ECO:0007829|PDB:6HKC" FT STRAND 168..176 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 185..200 FT /evidence="ECO:0007829|PDB:4MS4" FT TURN 203..205 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 209..217 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 222..233 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 234..237 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 247..256 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 272..275 FT /evidence="ECO:0007829|PDB:4MS4" FT TURN 277..279 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 283..287 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 290..292 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 293..303 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 308..316 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 317..332 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 336..345 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 348..356 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 361..365 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 368..381 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 385..387 FT /evidence="ECO:0007829|PDB:4MRM" FT STRAND 389..393 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 400..402 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 412..419 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 423..427 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 443..453 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 454..456 FT /evidence="ECO:0007829|PDB:7C7Q" FT HELIX 458..460 FT /evidence="ECO:0007829|PDB:4MS4" FT TURN 462..466 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 467..484 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 495..497 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 504..514 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 517..520 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 523..526 FT /evidence="ECO:0007829|PDB:4MS4" FT TURN 529..531 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 536..543 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 546..554 FT /evidence="ECO:0007829|PDB:4MS4" FT TURN 555..558 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 559..562 FT /evidence="ECO:0007829|PDB:4MS4" FT HELIX 569..571 FT /evidence="ECO:0007829|PDB:4MS4" FT STRAND 580..584 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 589..615 FT /evidence="ECO:0007829|PDB:7C7S" FT TURN 616..618 FT /evidence="ECO:0007829|PDB:7C7S" FT STRAND 619..625 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 627..648 FT /evidence="ECO:0007829|PDB:7C7S" FT TURN 651..653 FT /evidence="ECO:0007829|PDB:7C7S" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:6W2Y" FT HELIX 659..692 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 707..731 FT /evidence="ECO:0007829|PDB:7C7S" FT STRAND 735..740 FT /evidence="ECO:0007829|PDB:7C7S" FT STRAND 749..751 FT /evidence="ECO:0007829|PDB:7C7Q" FT STRAND 753..762 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 766..790 FT /evidence="ECO:0007829|PDB:7C7S" FT STRAND 797..799 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 802..825 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 826..828 FT /evidence="ECO:0007829|PDB:6W2Y" FT HELIX 830..858 FT /evidence="ECO:0007829|PDB:7C7S" FT TURN 859..861 FT /evidence="ECO:0007829|PDB:7C7S" FT HELIX 885..917 FT /evidence="ECO:0007829|PDB:4PAS" SQ SEQUENCE 961 AA; 108320 MW; 54E7349CD02B633F CRC64; MLLLLLLAPL FLRPPGAGGA QTPNATSEGC QIIHPPWEGG IRYRGLTRDQ VKAINFLPVD YEIEYVCRGE REVVGPKVRK CLANGSWTDM DTPSRCVRIC SKSYLTLENG KVFLTGGDLP ALDGARVDFR CDPDFHLVGS SRSICSQGQW STPKPHCQVN RTPHSERRAV YIGALFPMSG GWPGGQACQP AVEMALEDVN SRRDILPDYE LKLIHHDSKC DPGQATKYLY ELLYNDPIKI ILMPGCSSVS TLVAEAARMW NLIVLSYGSS SPALSNRQRF PTFFRTHPSA TLHNPTRVKL FEKWGWKKIA TIQQTTEVFT STLDDLEERV KEAGIEITFR QSFFSDPAVP VKNLKRQDAR IIVGLFYETE ARKVFCEVYK ERLFGKKYVW FLIGWYADNW FKIYDPSINC TVDEMTEAVE GHITTEIVML NPANTRSISN MTSQEFVEKL TKRLKRHPEE TGGFQEAPLA YDAIWALALA LNKTSGGGGR SGVRLEDFNY NNQTITDQIY RAMNSSSFEG VSGHVVFDAS GSRMAWTLIE QLQGGSYKKI GYYDSTKDDL SWSKTDKWIG GSPPADQTLV IKTFRFLSQK LFISVSVLSS LGIVLAVVCL SFNIYNSHVR YIQNSQPNLN NLTAVGCSLA LAAVFPLGLD GYHIGRNQFP FVCQARLWLL GLGFSLGYGS MFTKIWWVHT VFTKKEEKKE WRKTLEPWKL YATVGLLVGM DVLTLAIWQI VDPLHRTIET FAKEEPKEDI DVSILPQLEH CSSRKMNTWL GIFYGYKGLL LLLGIFLAYE TKSVSTEKIN DHRAVGMAIY NVAVLCLITA PVTMILSSQQ DAAFAFASLA IVFSSYITLV VLFVPKMRRL ITRGEWQSEA QDTMKTGSST NNNEEEKSRL LEKENRELEK IIAEKEERVS ELRHQLQSRQ QLRSRRHPPT PPEPSGGLPR GPPEPPDRLS CDGSRVHLLY K //