| IED ID |
IndEnz0010001428 |
| Enzyme Type ID |
esterase001428 |
| Protein Name |
Gamma-aminobutyric acid type B receptor subunit 2
|
| Gene Name |
gbb-2 ZK180.1 |
| 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
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| Enzyme Sequence |
MSRWLSLLLFAVQAVGGYEAGEELSCKRRHGGIPLPLGVFTVQKEGFPDALPAIRTALSHVHSRSCILQGYRLEMIVKDTHCKTSQGMKALFDLIASRPRPVAILGGQCTEVNEPIAMALKYWQIVQLSYAETHAKFASSDSHELFTTFFRVVPGSRNTNMAKCKFVNHFGWKRVGTVKQNDQPRYALPHEALTTRLEHGFGVKIVHTAGVNWEQIETVGGELDELKERDVRIILVDVDEEMAATVLCAGYHRGMYGDNYVWILPGYHSDKWLNQTHDNCTVEEMREAAKNHFSVEFALTRRDVDTKIVGNTRAGDVWNEITQLDPNNTWRGYLYDGLWTLAIALSHSMGDNAEFSHHKMMEAIDNSSFQGLTGKVKFANNERLGLVDIKQWSDGQYVPFAVYDGADDEFKIIDSTTKGWSPPLDSTITERRREHISSILFLAMSLLALIGIFLALIFLLINFRYRNHRFIKMSSPNLNNIIIAGSICTFASVIMLGLDTRIVSPDVFVWLCYTKTWTLCIGFTLSFGAMFSKTWRVHSIFTNIRMDRKAIKDSKLFIILGILLFIDICVLVTWAFVSPFSYTVTELPHIPEDNIVIIPEVEKCNSSHSGVFQAVLYAVKGVLMILGCFLAWETRHVNVPALNDSKYIGTSVYCCVVMSVLGLSTSVILQERVNEMFSLASFFVIFSTTLTLCLVFVPKVIELARNPVGNEPRAYRRGLMKSVVAKTSQPMSPQPRSDSSGDLIGKAESENKLRRRYLHQKSTQLWDLVEKLRAQGDTRFLQQEWCLSSASPSSQERETSLLLRQPSSSNNREETSLTAAGPNGERSSDWPWVDPDEPSTKL |
| Enzyme Length |
842 |
| Uniprot Accession Number |
G5ECB2 |
| Absorption |
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| Active Site |
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| Activity Regulation |
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| Binding Site |
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| Calcium Binding |
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| catalytic Activity |
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| DNA Binding |
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| EC Number |
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| 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). 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-1, 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). Regulates locomotory behavior in response to GABA release by GABAergic motor neurons (PubMed:18614679, PubMed:21613582). {ECO:0000250|UniProtKB:O88871, ECO:0000269|PubMed:18614679, ECO:0000269|PubMed:21613582}. |
| Temperature Dependency |
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| PH Dependency |
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| Pathway |
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| nucleotide Binding |
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| Features |
Chain (1); Compositional bias (2); Glycosylation (5); Mutagenesis (2); Region (2); Signal peptide (1); Topological domain (8); Transmembrane (7) |
| Keywords |
Cell membrane;G-protein coupled receptor;Glycoprotein;Membrane;Receptor;Reference proteome;Signal;Transducer;Transmembrane;Transmembrane helix |
| Interact With |
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| Induction |
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| Subcellular Location |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O75899}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue |
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| Post Translational Modification |
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| Signal Peptide |
SIGNAL 1..17; /evidence=ECO:0000255 |
| Structure 3D |
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| Cross Reference PDB |
- |
| Mapped Pubmed ID |
10778742;
17164286;
19343510;
20439776;
21085631;
21177967;
21367940;
22267497;
22286215;
22347378;
22560298;
23800452;
24884423;
25487147;
6593563;
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| Motif |
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| Gene Encoded By |
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| Mass |
94,861 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
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