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Within the heterodimeric GABA receptor, only GABBR1 seems to bind agonists, while GABBR2 mediates coupling to G proteins (PubMed:18165688). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:10075644, PubMed:10773016, PubMed:10906333, PubMed:24305054, PubMed:9872744). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (PubMed:10075644). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (PubMed:9844003). Pre-synaptic GABA receptor inhibits neurotransmitter release by down-regulating high-voltage activated calcium channels, whereas postsynaptic GABA receptor decreases neuronal excitability by activating a prominent inwardly rectifying potassium (Kir) conductance that underlies the late inhibitory postsynaptic potentials (PubMed:10075644, PubMed:22660477, PubMed:9844003, PubMed:9872316, PubMed:9872744). Not only implicated in synaptic inhibition but also in hippocampal long-term potentiation, slow wave sleep, muscle relaxation and antinociception (Probable). Activated by (-)-baclofen, cgp27492 and blocked by phaclofen (PubMed:24305054, PubMed:9844003, PubMed:9872316)"}],"commentType":"FUNCTION"},{"texts":[{"value":"Isoform 1E may regulate the formation of functional GABBR1/GABBR2 heterodimers by competing for GABBR2 binding. This could explain the observation that certain small molecule ligands exhibit differential affinity for central versus peripheral sites"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Z0U4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10773016"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10906333"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14718537"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15617512"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18165688"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22660477"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24305054"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9872316"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9872744"}],"value":"Heterodimer of GABBR1 and GABBR2 (PubMed:10773016, PubMed:15617512, PubMed:18165688, PubMed:22660477, PubMed:24305054, PubMed:9872316, PubMed:9872744). Homodimers may form, but are inactive (PubMed:15617512, PubMed:9872316). Isoform 1E (without C-terminal intracellular domain) is unable to dimerize via a coiled-coil interaction with GABBR2 (PubMed:10906333). Interacts (via C-terminus) with ATF4 (via leucine zipper domain) (By similarity). Interacts with JAKMIP1 (PubMed:14718537)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q9UBS5","intActId":"EBI-724156"},"interactantTwo":{"uniProtKBAccession":"O75899","geneName":"GABBR2","intActId":"EBI-715469"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UBS5","intActId":"EBI-724156"},"interactantTwo":{"uniProtKBAccession":"O15354","geneName":"GPR37","intActId":"EBI-15639515"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UBS5","intActId":"EBI-724156"},"interactantTwo":{"uniProtKBAccession":"P61244","geneName":"MAX","intActId":"EBI-751711"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UBS5","intActId":"EBI-724156"},"interactantTwo":{"uniProtKBAccession":"P16333","geneName":"NCK1","intActId":"EBI-389883"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UBS5","intActId":"EBI-724156"},"interactantTwo":{"uniProtKBAccession":"P46459","geneName":"NSF","intActId":"EBI-712251"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q9UBS5-2","intActId":"EBI-16084001"},"interactantTwo":{"uniProtKBAccession":"O75899","geneName":"GABBR2","intActId":"EBI-715469"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000012949","intActId":"EBI-67110347"},"interactantTwo":{"uniProtKBAccession":"O60894","geneName":"RAMP1","intActId":"EBI-962893"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000012949","intActId":"EBI-67110347"},"interactantTwo":{"uniProtKBAccession":"O60895","geneName":"RAMP2","intActId":"EBI-9009040"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"chainId":"PRO_0000012949","intActId":"EBI-67110347"},"interactantTwo":{"uniProtKBAccession":"O60896","geneName":"RAMP3","intActId":"EBI-720447"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Z0U4"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15617512"}],"value":"Colocalizes with ATF4 in hippocampal neuron dendritic membranes (By similarity). 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Weakly expressed in heart, small intestine and uterus. Isoform 1A: Mainly expressed in granular cell and molecular layer (PubMed:9844003). Isoform 1B: Mainly expressed in Purkinje cells (PubMed:9844003). Isoform 1E: Predominantly expressed in peripheral tissues as kidney, lung, trachea, colon, small intestine, stomach, bone marrow, thymus and mammary gland (PubMed:10906333)"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9844003"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9872744"}],"value":"Alpha-helical parts of the C-terminal intracellular region mediate heterodimeric interaction with GABBR2 (PubMed:9872744). 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