Detail Information for IndEnz0010001427
IED ID IndEnz0010001427
Enzyme Type ID esterase001427
Protein Name Gamma-aminobutyric acid type B receptor subunit 1
Gene Name gbb-1 Y41G9A.4
Organism Caenorhabditis elegans
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Protostomia Ecdysozoa Nematoda (roundworms) Chromadorea Rhabditida Rhabditina Rhabditomorpha Rhabditoidea Rhabditidae Peloderinae Caenorhabditis Caenorhabditis elegans
Enzyme Sequence MFVRSSWLLLWGTIVWASAEPVTLHIGGTFPMESGSGGWAGGEACLPAVEMALKDVNSRLDILPGYVLNMTNHNSQCQPGLAMQQLYDFLYKPPTKLMLLTGCSPVTTVIAEAAPVWKLVVLSYGGSSPALSNRNRFPTLFRTHPSANMQNPTRIHIMEKFKWKRFTILMSVEEVFVTTAKDLEAIARKKGIKVDRQSFYGDPTDAMKTLQRQDARIIVGLFYVTEARKVLCQAYHHGLYGRRYVWFFIGWYADTWYIPPPEEHLNCTAEQMTEAAEYHFTTESVMLSRDNIPAISEMTGMQFQQRLTQYFQKDTANVGGFPEAPLAYDAVWALALAFNCTRNNLPSHIRLENFTYDNKVIADTLFQCVKNTSFRGVSGKVMFSDSGDRIARTQIEQMQGGKYKIMGYYDTTSGDLEWYNKEQWLNGKGPPPDSTVIKKHAMTVSNEFYYPTILFAVLGIAACVFIYLFTQKHHERLIIFQSQPECNNILLIGCSLCLFSLFLIGLPSDDISISESLFPLLCHARVTILLFGFTFAYGSMFAKVWIVHRMGATENQQLASRQKDEEENTPWEGIRTLISTMVGRQALMRKSSGQAYGALLEKRNTVLNQPISSSKFYVIVAALTAVDVFVCFVWVLIDPLHLTEQKFPLFTPADSEEDEMIMPVLQQCQSNQQEVWIGIIMGFKCLLLVFGTFLSYETRNLKLRFINDSRFVGLAIYNVAVMTLVTAPVVTLLIHGKVDANFAFISLTVLICTYISVGLIYGPKIRHIIKVPPSADEIQLNGNVGPGVMSKVDQKRYDMLKKENETLQIQIEEKERKIHECKERLEELTKNSETEDMNAQLLCENDKQIADENLTYSTATTLTTTIPLIDLQNGNHPGQIYENDNDDDGSSTSSDEILL
Enzyme Length 899
Uniprot Accession Number H2L0Q3
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Component of a heterodimeric G-protein coupled receptor for GABA, formed by gbb-1 and gbb-2 (By similarity). Within the heterodimeric GABA receptor, only gbb-1 seems to bind agonists, while gbb-2 mediates coupling to G proteins (By similarity). 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 (By similarity). Signaling inhibits adenylate cyclase, stimulates phospholipase A2, activates potassium channels, inactivates voltage-dependent calcium-channels and modulates inositol phospholipid hydrolysis (By similarity). Calcium is required for high affinity binding to GABA (By similarity). Plays a critical role in the fine-tuning of inhibitory synaptic transmission (By similarity). 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 (By similarity). Along with gbb-2, may couple to the G(o)-alpha G-protein goa-1 to negatively regulate cholinergic receptor activity in the presence of high levels of acetylcholine in ventral cord motor neurons (PubMed:18614679). As acetylcholine depolarizes body wall muscles, modulation of acetylcholine levels most likely results in the control of locomotory behavior (PubMed:18614679). Acts in neurons to regulate lifespan, and this may be through G-protein-egl-8/PLC-beta signaling to the transcription factor daf-16/FOXO (PubMed:26537867). {ECO:0000250|UniProtKB:Q9UBS5, ECO:0000250|UniProtKB:Q9Z0U4, ECO:0000269|PubMed:18614679, ECO:0000269|PubMed:26537867}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Alternative sequence (4); Chain (1); Coiled coil (1); Glycosylation (5); Region (1); Signal peptide (1); Topological domain (8); Transmembrane (7)
Keywords Alternative splicing;Cell membrane;Coiled coil;G-protein coupled receptor;Glycoprotein;Membrane;Receptor;Reference proteome;Signal;Transducer;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UBS5}; Multi-pass membrane protein {ECO:0000255}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID 10778742; 11381264; 21177967; 22267497; 22286215; 22560298; 23800452; 24884423; 25487147; 27138642; 6593563;
Motif
Gene Encoded By
Mass 101,531
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda