| IED ID | IndEnz0002006565 |
| Enzyme Type ID | protease006565 |
| Protein Name |
Potassium voltage-gated channel subfamily KQT member 2 KQT-like 2 Neuroblastoma-specific potassium channel subunit alpha KvLQT2 Voltage-gated potassium channel subunit Kv7.2 |
| Gene Name | KCNQ2 |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRGWAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASIAVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWWGLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCRGPLCGCCPGRSSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESDTDSDLCTPCGPPPRSATGEGPFGDVGWAGPRK |
| Enzyme Length | 872 |
| Uniprot Accession Number | O43526 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Associates with KCNQ3 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2/KCNQ3 current is blocked by linopirdine and XE991, and activated by the anticonvulsant retigabine (PubMed:9836639, PubMed:11572947, PubMed:14534157, PubMed:12742592, PubMed:17872363). As the native M-channel, the potassium channel composed of KCNQ2 and KCNQ3 is also suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (PubMed:10684873). {ECO:0000269|PubMed:10684873, ECO:0000269|PubMed:11572947, ECO:0000269|PubMed:12742592, ECO:0000269|PubMed:14534157, ECO:0000269|PubMed:17872363, ECO:0000269|PubMed:25740509, ECO:0000269|PubMed:9836639}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (7); Beta strand (2); Chain (1); Compositional bias (1); Helix (3); Intramembrane (1); Modified residue (11); Motif (1); Mutagenesis (5); Natural variant (42); Region (7); Sequence conflict (2); Topological domain (8); Transmembrane (6) |
| Keywords | 3D-structure;Alternative splicing;Cell membrane;Disease variant;Epilepsy;Ion channel;Ion transport;Membrane;Mental retardation;Phosphoprotein;Potassium;Potassium channel;Potassium transport;Reference proteome;Transmembrane;Transmembrane helix;Transport;Ubl conjugation;Voltage-gated channel |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10788442, ECO:0000269|PubMed:9836639}; Multi-pass membrane protein {ECO:0000255}. |
| Modified Residue | MOD_RES 52; /note=Phosphoserine; by PKA; /evidence=ECO:0000269|PubMed:9872318; MOD_RES 217; /note=Phosphothreonine; /evidence=ECO:0000269|PubMed:16319223; MOD_RES 466; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Z351; MOD_RES 468; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Z351; MOD_RES 472; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Z351; MOD_RES 476; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Z351; MOD_RES 478; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9Z351; MOD_RES 507; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O88943; MOD_RES 672; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O88943; MOD_RES 801; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O88943; MOD_RES 803; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:O88943 |
| Post Translational Modification | PTM: KCNQ2/KCNQ3 heteromeric current can be increased by intracellular cyclic AMP, an effect that depends on phosphorylation of Ser-52 in the N-terminal region. {ECO:0000269|PubMed:16319223, ECO:0000269|PubMed:9872318}.; PTM: KCNQ2/KCNQ3 are ubiquitinated by NEDD4L. Ubiquitination leads to protein degradation (Probable). Degradation induced by NEDD4L is inhibited by USP36 (PubMed:27445338). {ECO:0000269|PubMed:27445338, ECO:0000305|PubMed:27445338}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (2); Electron microscopy (6); X-ray crystallography (1) |
| Cross Reference PDB | 5J03; 6FEG; 6FEH; 7CR0; 7CR1; 7CR2; 7CR3; 7CR4; 7CR7; |
| Mapped Pubmed ID | 11427698; 11470829; 11724816; 11726784; 12395102; 12458027; 12524525; 12640002; 12832524; 12847176; 14985406; 15030501; 15178210; 15304482; 15483133; 15596769; 16169070; 16235065; 16260777; 16464983; 16525039; 16691402; 16721610; 16990515; 17044971; 17382933; 17475800; 17724161; 17993630; 18006581; 18089837; 18166285; 18246739; 18353052; 18448631; 18545987; 18625963; 19112491; 19464834; 19494108; 19559753; 19818940; 20119593; 20393197; 21156207; 21231794; 21723881; 21913284; 21937445; 21976501; 21980481; 22169383; 22275249; 22334706; 22447848; 22884718; 23002961; 23065794; 23203804; 23209695; 23290024; 23440208; 23621294; 23692823; 24107868; 24318194; 24371303; 24375629; 24489773; 24599470; 24687876; 24843134; 25041603; 25052858; 25385787; 25880994; 25959266; 25998125; 26007637; 26148514; 26627826; 27030113; 27535030; 27607834; 27861786; 28038823; 28133863; 28139826; 28372301; 28399683; 28602030; 28856943; 29058190; 29067685; 29338302; 29463698; 29474891; 30126342; 30146722; 30885609; 31102386; 31152295; 31199083; 31418850; 32179837; 32276107; 32319632; 32580997; 32770121; 32863083; 32884139; 32917465; 33616268; 33681646; 33754465; 33962768; 34650221; 34711204; 9278538; |
| Motif | MOTIF 277..282; /note=Selectivity filter; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 95,848 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |