KCNQ5
entrez
56479
canonical
uniprot
Q9NR82
canonical
ensembl
ENSG00000185760
resolver
ensp
ENSP00000345055
resolver
ensp
ENSP00000359419
resolver
ensp
ENSP00000359425
resolver
ensp
ENSP00000485743
resolver
ensp
ENSP00000486187
resolver
genesymbol
KCNQ5
resolver
hgnc
HGNC:6299
resolver
uniprot
A6NKT6
resolver
uniprot
A6PVT6
resolver
uniprot
A8MSQ5
resolver
uniprot
B4DS33
resolver
uniprot
B5MC83
resolver
uniprot
B7ZL37
resolver
uniprot
F5GZV0
resolver
uniprot
Q17RE1
resolver
uniprot
Q5VVP3
resolver
uniprot
Q86W40
resolver
uniprot
Q9NRN0
resolver
uniprot
Q9NYA6
resolver
uniprot_entry
KCNQ5_HUMAN
resolver
uniprot_sec
A6NKT6
resolver
uniprot_sec
A6PVT6
resolver
uniprot_sec
A8MSQ5
resolver
uniprot_sec
B4DS33
resolver
uniprot_sec
B5MC83
resolver
uniprot_sec
B7ZL37
resolver
uniprot_sec
F5GZV0
resolver
uniprot_sec
Q17RE1
resolver
uniprot_sec
Q5VVP3
resolver
uniprot_sec
Q86W40
resolver
uniprot_sec
Q9NRN0
resolver
uniprot_sec
Q9NYA6
resolver
activity_regulation
ACTIVITY REGULATION: Phosphatidylinositol-4,5-bisphosphate (PIP2) is essential to activate KCNQ5 channel by inducing the coupling of the voltage-sensing domain (VSD) and the pore-forming domain (PD) (By similarity). Calcium suppresses KCNQ5 channel current through calcium-bound CALM C-terminus (PubMed:29429937). Therefore CALM acts as calcium sensor that controls channel activity (PubMed:29429937). Activated by niflumic acid and the anticonvulsant retigabine (PubMed:10816588, PubMed:11159685). Inhibited by barium, linopirdine, XE991 and tetraethylammonium (as homomer) (PubMed:10787416, PubMed:10816588, PubMed:11159685). Insensitive to tetraethylammonium in KCNQ3-KCNQ5 heteromers (PubMed:10787416, PubMed:10816588). {ECO:0000250|UniProtKB:Q92508, ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:10816588, ECO:0000269|PubMed:11159685, ECO:0000269|PubMed:29429937}.
uniprot
proteins
amino_acid_sequence
MPRHHAGGEEGGAAGLWVKSGAAAAAAGGGRLGSGMKDVESGRGRVLLNSAAARGDGLLLLGTRAATLGGGGGGLRESRRGKQGARMSLLGKPLSYTSSQSCRRNVKYRRVQNYLYNVLERPRGWAFIYHAFVFLLVFGCLILSVFSTIPEHTKLASSCLLILEFVMIVVFGLEFIIRIWSAGCCCRYRGWQGRLRFARKPFCVIDTIVLIASIAVVSAKTQGNIFATSALRSLRFLQILRMVRMDRRGGTWKLLGSVVYAHSKELITAWYIGFLVLIFSSFLVYLVEKDANKEFSTYADALWWGTITLTTIGYGDKTPLTWLGRLLSAGFALLGISFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAANLIQCVWRSYAADEKSVSIATWKPHLKALHTCSPTKKEQGEASSSQKLSFKERVRMASPRGQSIKSRQASVGDRRSPSTDITAEGSPTKVQKSWSFNDRTRFRPSLRLKSSQPKPVIDADTALGTDDVYDEKGCQCDVSVEDLTPPLKTVIRAIRIMKFHVAKRKFKETLRPYDVKDVIEQYSAGHLDMLCRIKSLQTRVDQILGKGQITSDKKSREKITAEHETTDDLSMLGRVVKVEKQVQSIESKLDCLLDIYQQVLRKGSASALALASFQIPPFECEQTSDYQSPVDSKDLSGSAQNSGCLSRSTSANISRGLQFILTPNEFSAQTFYALSPTMHSQATQVPISQSDGSAVAATNTIANQINTAPKPAAPTTLQIPPPLPAIKHLPRPETLHPNPAGLQESISDVTTCLVASKENVQVAQSNLTKDRSMRKSFDMGGETLLSVCPMVPKDLGKSLSVQNLIRSTEELNIQLSGSESSGSRGSQDFYPKWRESKLFITDEEVGPEETETDTFDAAPQPAREAAFASDSLRTGRSRSSQSICKAGESTDALSLPHVKLK
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, autosomal dominant 46 (MRD46) [MIM:617601]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD46 patients manifest developmental delay and mild to moderate intellectual disability. {ECO:0000269|PubMed:28669405}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Pore-forming subunit of the voltage-gated potassium (Kv) channel broadly expressed in brain and involved in the regulation of neuronal excitability (PubMed:10787416, PubMed:10816588, PubMed:11159685, PubMed:28669405). Associates with KCNQ3/Kv7.3 pore-forming subunit to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons (PubMed:10816588, PubMed:11159685). Contributes, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current (PubMed:10816588). Also forms a functional channel with KCNQ1/Kv7.1 subunit that may contribute to vasoconstriction and hypertension (PubMed:24855057). Channel may be selectively permeable in vitro to other cations besides potassium, in decreasing order of affinity K(+) = Rb(+) > Cs(+) > Na(+) (PubMed:10816588). Similar to the native M-channel, KCNQ3-KCNQ5 potassium channel is suppressed by activation of the muscarinic acetylcholine receptor CHRM1 (PubMed:10816588). {ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:10816588, ECO:0000269|PubMed:11159685, ECO:0000269|PubMed:24855057, ECO:0000269|PubMed:28669405}.
uniprot
proteins
mass_dalton
102179
uniprot
proteins
protein_family
KQT (TC 1.A.1.15) subfamily
uniprot
proteins
protein_family
Kv7.5/KCNQ5 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
10787416
uniprot
proteins
pubmed
10816588
uniprot
proteins
pubmed
11159685
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24855057
uniprot
proteins
pubmed
28669405
uniprot
proteins
pubmed
29429937
uniprot
proteins
sequence_length
932
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10787416, ECO:0000269|PubMed:11159685}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 126..146; /note="Helical; Name=Segment S1"; /evidence="ECO:0000255"; TRANSMEM 157..177; /note="Helical; Name=Segment S2"; /evidence="ECO:0000255"; TRANSMEM 201..221; /note="Helical; Name=Segment S3"; /evidence="ECO:0000255"; TRANSMEM 230..252; /note="Helical; Voltage-sensor; Name=Segment S4"; /evidence="ECO:0000255"; TRANSMEM 267..287; /note="Helical; Name=Segment S5"; /evidence="ECO:0000255"; TRANSMEM 326..346; /note="Helical; Name=Segment S6"; /evidence="ECO:0000255
uniprot
proteins