Kcnt1
entrez
60444
canonical
uniprot
Q9Z258
canonical
ensembl
ENSRNOG00000017283
resolver
ensp
ENSRNOP00000023542
resolver
ensp
ENSRNOP00000058487
resolver
ensp
ENSRNOP00000089937
resolver
ensp
ENSRNOP00000096324
resolver
ensp
ENSRNOP00000103835
resolver
enst
ENSRNOT00000061773
resolver
enst
ENSRNOT00000110074
resolver
genesymbol
Kcnt1
resolver
genesymbol_syn
Slack
resolver
uniprot
A0A8I6ALJ8
resolver
uniprot
D3ZNI9
resolver
uniprot
F1LSG1
resolver
uniprot
Q5D6C6
resolver
uniprot_entry
A0A8I6ALJ8_RAT
resolver
uniprot_entry
D3ZNI9_RAT
resolver
uniprot_entry
KCNT1_RAT
resolver
uniprot_sec
F1LSG1
resolver
uniprot_sec
Q5D6C6
resolver
activity_regulation
ACTIVITY REGULATION: Activated by high intracellular Na(+) level (PubMed:12628167, PubMed:14684870, PubMed:36898835). In addition to activation by Na(+), is cooperatively activated by intracellular Cl(-) levels (PubMed:12628167, PubMed:36898835). Activated upon stimulation of G protein-coupled receptors, such as CHRM1 and GRIA1 (PubMed:16687497). {ECO:0000269|PubMed:12628167, ECO:0000269|PubMed:14684870, ECO:0000269|PubMed:16687497, ECO:0000269|PubMed:36898835}.
uniprot
proteins
amino_acid_sequence
MARAKLPRSPSEGKAGPGDTPAGSAAPEEPHGLSPLLPTRGGGSVGSDVGQRLHVEDFSLDSSLSQVQVEFYVNENTFKERLKLFFIKNQRSSLRIRLFNFSLKLLTCLLYIVRVLLDNPDQGIGCWGCTKYNYTFNGSSSEFHWAPILWVERKMALWVIQVIVATISFLETMLLIYLSYKGNIWEQIFHVSFVLEMINTLPFIITVFWPPLRNLFIPVFLNCWLAKHALENMINDFHRAILRTQSAMFNQVLILFCTLLCLVFTGTCGIQHLERAGGNLNLLTSFYFCIVTFSTVGFGDVTPKIWPSQLLVVILICVTLVVLPLQFEELVYLWMERQKSGGNYSRHRARTEKHVVLCVSSLKIDLLMDFLNEFYAHPRLQDYYVVILCPSEMDVQVRRVLQIPLWSQRVIYLQGSALKDQDLMRAKMDNGEACFILSSRNEVDRTAADHQTILRAWAVKDFAPNCPLYVQILKPENKFHVKFADHVVCEEECKYAMLALNCICPATSTLITLLVHTSRGQEGQESPEQWQRMYGRCSGNEVYHIRMGDSKFFREYEGKSFTYAAFHAHKKYGVCLIGLKREENKSILLNPGPRHILAASDTCFYINITKEENSAFIFKQEEKQKRRGLAGQALYEGPSRLPVHSIIASMGTVAMDLQNTDCRPSQGGSGGGGGKLTLPTENGSGSRRPSIAPVLELADSSALLPCDLLSDQSEDEVTPSDDEGLSVVEYVKGYPPNSPYIGSSPTLCHLLPVKAPFCCLRLDKGCKHNSYEDAKAYGFKNKLIIVSAETAGNGLYNFIVPLRAYYRSRRELNPIVLLLDNKPDHHFLEAICCFPMVYYMEGSVDNLDSLLQCGIIYADNLVVVDKESTMSAEEDYMADAKTIVNVQTMFRLFPSLSITTELTHPSNMRFMQFRAKDSYSLALSKLEKQERENGSNLAFMFRLPFAAGRVFSISMLDTLLYQSFVKDYMITITRLLLGLDTTPGSGYLCAMKVTEDDLWIRTYGRLFQKLCSSSAEIPIGIYRTECHVFSSEPHDLRAQSQISVNMEDCEDTREAKGPWGTRAASGGGSTHGRHGGSADPVEHPLLRRKSLQWARKLSRKSSKQAGKAPMTTDWITQQRLSLYRRSERQELSELVKNRMKHLGLPTTGYEDVANLTASDVMNRVNLGYLQDEMNDHHQNTLSYVLINPPPDTRLEPNDIVYLIRSDPLAHVTSSSQSRKSSCSNKLSSCNPETRDETQL
uniprot
proteins
function
FUNCTION: Sodium-activated K(+) channel (PubMed:12628167, PubMed:14684870, PubMed:16687497, PubMed:24463883, PubMed:36898835). Acts as an important mediator of neuronal membrane excitability (By similarity). Contributes to the delayed outward currents (PubMed:10196543, PubMed:19412167). Regulates neuronal bursting in sensory neurons (PubMed:16687497, PubMed:18787033). Contributes to synaptic development and plasticity (By similarity). {ECO:0000250|UniProtKB:Q5JUK3, ECO:0000250|UniProtKB:Q6ZPR4, ECO:0000269|PubMed:10196543, ECO:0000269|PubMed:12628167, ECO:0000269|PubMed:14684870, ECO:0000269|PubMed:16687497, ECO:0000269|PubMed:18787033, ECO:0000269|PubMed:19412167, ECO:0000269|PubMed:24463883, ECO:0000269|PubMed:36898835}.
uniprot
proteins
mass_dalton
139788
uniprot
proteins
mutagenesis
MUTAGEN 335; /note="M->A: Shows channel activity even in the absence of cytosolic Na(+)."; /evidence="ECO:0000269|PubMed:36898835"; MUTAGEN 373; /note="E->Q: Does not elicit any current. Completely abolishes Na(+) sensitivity. Does not affect membrane localization."; /evidence="ECO:0000269|PubMed:36898835"; MUTAGEN 379; /note="R->Q: Completely abolishes Cl(-) sensitivity."; /evidence="ECO:0000269|PubMed:36898835"; MUTAGEN 409; /note="R->Q: Generates currents that resembles wild-type in terms of voltage dependence and kinetic behavior but has 2- to 3-fold higher amplitude compared to wild-type. The mutation shows to cause constitutive activation of the channel, mimicking the effects of phosphorylation of the C-terminal domain by PRKCA activation."; /evidence="ECO:0000269|PubMed:23086397"; MUTAGEN 915; /note="A->T: Generates currents that resembles wild-type in terms of voltage dependence and kinetic behavior but has 2- to 3-fold higher amplitude compared to wild-type. The mutation shows to cause constitutive activation of the channel, mimicking the effects of phosphorylation of the C-terminal domain by PRKCA activation."; /evidence="ECO:0000269|PubMed:23086397"; MUTAGEN 947; /note="A->T: Increases channel activity upon positive potentials. The mutation corresponds to probable disease-associated variant in humans."; /evidence="ECO:0000269|PubMed:24463883
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by protein kinase C. Phosphorylation of the C-terminal domain increases channel activity. {ECO:0000269|PubMed:16687497}.
uniprot
proteins
protein_family
Calcium-activated (TC 1.A.1.3) subfamily
uniprot
proteins
protein_family
KCa4.1/KCNT1 sub-subfamily
uniprot
proteins
protein_family
Potassium channel family
uniprot
proteins
pubmed
10196543
uniprot
proteins
pubmed
12442315
uniprot
proteins
pubmed
12628167
uniprot
proteins
pubmed
14684870
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16045448
uniprot
proteins
pubmed
16687497
uniprot
proteins
pubmed
18787033
uniprot
proteins
pubmed
19403831
uniprot
proteins
pubmed
19412167
uniprot
proteins
pubmed
20512134
uniprot
proteins
pubmed
23086397
uniprot
proteins
pubmed
24463883
uniprot
proteins
pubmed
36898835
uniprot
proteins
sequence_length
1239
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12442315, ECO:0000269|PubMed:16045448, ECO:0000269|PubMed:36898835}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5JUK3}.
uniprot
proteins
transmembrane_region
TRANSMEM 94..126; /note="Helical; Name=Segment S1"; /evidence="ECO:0000250|UniProtKB:Q5JUK3"; TRANSMEM 154..178; /note="Helical; Name=Segment S2"; /evidence="ECO:0000250|UniProtKB:Q5JUK3"; TRANSMEM 193..208; /note="Helical; Name=Segment S3"; /evidence="ECO:0000250|UniProtKB:Q5JUK3"; TRANSMEM 216..233; /note="Helical; Name=Segment S4"; /evidence="ECO:0000250|UniProtKB:Q5JUK3"; TRANSMEM 247..274; /note="Helical; Name=Segment S5"; /evidence="ECO:0000250|UniProtKB:Q5JUK3"; TRANSMEM 305..338; /note="Helical; Name=Segment S6"; /evidence="ECO:0000250|UniProtKB:Q5JUK3
uniprot
proteins