ID KCNT1_HUMAN Reviewed; 1230 AA. AC Q5JUK3; B3KXF7; B7ZVY4; B9EGP2; G5E9V0; Q9P2C5; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 18-JUN-2025, entry version 174. DE RecName: Full=Potassium channel subfamily T member 1; DE AltName: Full=KCa4.1; DE AltName: Full=KNa1.1; DE AltName: Full=Sodium and chloride-activated ATP-sensitive potassium channel Slo2.2 {ECO:0000303|PubMed:37494189}; GN Name=KCNT1 {ECO:0000312|HGNC:HGNC:18865}; GN Synonyms=KIAA1422, SLACK, Slo2.2 {ECO:0000303|PubMed:37494189}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1103 (ISOFORM 2), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [6] RP INTERACTION WITH FMR1. RX PubMed=20512134; DOI=10.1038/nn.2563; RA Brown M.R., Kronengold J., Gazula V.R., Chen Y., Strumbos J.G., RA Sigworth F.J., Navaratnam D., Kaczmarek L.K.; RT "Fragile X mental retardation protein controls gating of the sodium- RT activated potassium channel Slack."; RL Nat. Neurosci. 13:819-821(2010). RN [7] {ECO:0007744|PDB:8HIR, ECO:0007744|PDB:8HK6, ECO:0007744|PDB:8HKF, ECO:0007744|PDB:8HKK, ECO:0007744|PDB:8HKM, ECO:0007744|PDB:8HKQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.64 ANGSTROMS) OF 23-1230 IN COMPLEX RP WITH SODIUM AND INHIBITOR C23, FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY RP REGULATION, SUBUNIT, AND MUTAGENESIS OF MET-315; ALA-319; PHE-327; GLU-541; RP 758-CYS-CYS-759; ASN-769; TYR-777; ASP-820; ASP-865 AND 873-GLU--TYR-876. RX PubMed=37494189; DOI=10.1016/j.celrep.2023.112858; RA Zhang J., Liu S., Fan J., Yan R., Huang B., Zhou F., Yuan T., Gong J., RA Huang Z., Jiang D.; RT "Structural basis of human Slo2.2 channel gating and modulation."; RL Cell Rep. 42:112858-112858(2023). RN [8] RP VARIANTS ENFL5 GLN-379; HIS-777; ILE-877 AND CYS-909. RX PubMed=23086396; DOI=10.1038/ng.2440; RA Heron S.E., Smith K.R., Bahlo M., Nobili L., Kahana E., Licchetta L., RA Oliver K.L., Mazarib A., Afawi Z., Korczyn A., Plazzi G., Petrou S., RA Berkovic S.F., Scheffer I.E., Dibbens L.M.; RT "Missense mutations in the sodium-gated potassium channel gene KCNT1 cause RT severe autosomal dominant nocturnal frontal lobe epilepsy."; RL Nat. Genet. 44:1188-1190(2012). RN [9] RP VARIANTS DEE14 GLN-409; HIS-455; MET-741 AND THR-915, AND CHARACTERIZATION RP OF VARIANTS DEE14 GLN-409 AND THR-915. RX PubMed=23086397; DOI=10.1038/ng.2441; RA Barcia G., Fleming M.R., Deligniere A., Gazula V.R., Brown M.R., RA Langouet M., Chen H., Kronengold J., Abhyankar A., Cilio R., Nitschke P., RA Kaminska A., Boddaert N., Casanova J.L., Desguerre I., Munnich A., RA Dulac O., Kaczmarek L.K., Colleaux L., Nabbout R.; RT "De novo gain-of-function KCNT1 channel mutations cause malignant migrating RT partial seizures of infancy."; RL Nat. Genet. 44:1255-1259(2012). RN [10] RP VARIANT DEE14 SER-269. RX PubMed=24029078; DOI=10.1016/j.gene.2013.08.096; RA Ishii A., Shioda M., Okumura A., Kidokoro H., Sakauchi M., Shimada S., RA Shimizu T., Osawa M., Hirose S., Yamamoto T.; RT "A recurrent KCNT1 mutation in two sporadic cases with malignant migrating RT partial seizures in infancy."; RL Gene 531:467-471(2013). RN [11] RP VARIANTS DEE14 ILE-562 AND GLN-1088. RX PubMed=23708187; DOI=10.1038/ng.2646; RA Carvill G.L., Heavin S.B., Yendle S.C., McMahon J.M., O'Roak B.J., Cook J., RA Khan A., Dorschner M.O., Weaver M., Calvert S., Malone S., Wallace G., RA Stanley T., Bye A.M., Bleasel A., Howell K.B., Kivity S., Mackay M.T., RA Rodriguez-Casero V., Webster R., Korczyn A., Afawi Z., Zelnick N., RA Lerman-Sagie T., Lev D., Moeller R.S., Gill D., Andrade D.M., Freeman J.L., RA Sadleir L.G., Shendure J., Berkovic S.F., Scheffer I.E., Mefford H.C.; RT "Targeted resequencing in epileptic encephalopathies identifies de novo RT mutations in CHD2 and SYNGAP1."; RL Nat. Genet. 45:825-830(2013). RN [12] RP VARIANT DEE14 THR-947, AND CHARACTERIZATION OF VARIANT DEE14 THR-947. RX PubMed=24463883; DOI=10.1093/hmg/ddu030; RG WGS500 Consortium; RA Martin H.C., Kim G.E., Pagnamenta A.T., Murakami Y., Carvill G.L., RA Meyer E., Copley R.R., Rimmer A., Barcia G., Fleming M.R., Kronengold J., RA Brown M.R., Hudspith K.A., Broxholme J., Kanapin A., Cazier J.B., RA Kinoshita T., Nabbout R., Bentley D., McVean G., Heavin S., Zaiwalla Z., RA McShane T., Mefford H.C., Shears D., Stewart H., Kurian M.A., RA Scheffer I.E., Blair E., Donnelly P., Kaczmarek L.K., Taylor J.C.; RT "Clinical whole-genome sequencing in severe early-onset epilepsy reveals RT new genes and improves molecular diagnosis."; RL Hum. Mol. Genet. 23:3200-3211(2014). RN [13] RP VARIANTS DEE14 SER-269; LYS-877 AND THR-915. RX PubMed=26993267; DOI=10.1136/jmedgenet-2015-103263; RA Trump N., McTague A., Brittain H., Papandreou A., Meyer E., Ngoh A., RA Palmer R., Morrogh D., Boustred C., Hurst J.A., Jenkins L., Kurian M.A., RA Scott R.H.; RT "Improving diagnosis and broadening the phenotypes in early-onset seizure RT and severe developmental delay disorders through gene panel analysis."; RL J. Med. Genet. 53:310-317(2016). RN [14] RP VARIANTS DEE14 VAL-497 AND GLU-928. RX PubMed=27864847; DOI=10.1002/humu.23149; RG Clinical Study Group; RA Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D., RA Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S., RA Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.; RT "Diagnostic targeted resequencing in 349 patients with drug-resistant RT pediatric epilepsies identifies causative mutations in 30 different RT genes."; RL Hum. Mutat. 38:216-225(2017). CC -!- FUNCTION: Sodium-activated K(+) channel (PubMed:37494189). Acts as an CC important mediator of neuronal membrane excitability (PubMed:37494189). CC Contributes to the delayed outward currents (By similarity). Regulates CC neuronal bursting in sensory neurons (By similarity). Contributes to CC synaptic development and plasticity (By similarity). CC {ECO:0000250|UniProtKB:Q6ZPR4, ECO:0000250|UniProtKB:Q9Z258, CC ECO:0000269|PubMed:37494189}. CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:37494189}; CC -!- ACTIVITY REGULATION: Activated by high intracellular Na(+) CC (PubMed:37494189). In addition to activation by Na(+), is cooperatively CC activated by intracellular Cl(-) levels (By similarity). Inhibited by CC Zn(2+) (PubMed:37494189). Activated upon stimulation of G-protein CC coupled receptors, such as CHRM1 and GRIA1 (By similarity). CC {ECO:0000250|UniProtKB:Q9Z258, ECO:0000269|PubMed:37494189}. CC -!- SUBUNIT: Homotetramer; which constitutes the Na(+)-activated K(+) CC channel (PubMed:37494189). Interacts with KCNT2; these heterodimer CC channels differ from the homomers in their unitary conductance, kinetic CC behavior, subcellular localization, and response to activation of CC protein kinase C (By similarity). Interacts (via C-terminus) with FMR1; CC this interaction alters gating properties of KCNT1 (PubMed:20512134). CC Interacts with CRBN via its cytoplasmic C-terminus (By similarity). CC {ECO:0000250|UniProtKB:Q9Z258, ECO:0000269|PubMed:20512134, CC ECO:0000269|PubMed:37494189}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Z258}; CC Multi-pass membrane protein {ECO:0000269|PubMed:37494189}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q5JUK3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5JUK3-2; Sequence=VSP_015470, VSP_015471; CC Name=3; CC IsoId=Q5JUK3-3; Sequence=VSP_015470, VSP_015471, VSP_044476; CC Name=4; CC IsoId=Q5JUK3-4; Sequence=VSP_055700, VSP_055701, VSP_015471; CC -!- TISSUE SPECIFICITY: Highest expression in liver, brain and spinal cord. CC Lowest expression in skeletal muscle. {ECO:0000269|PubMed:10718198}. CC -!- DOMAIN: The cytoplasmic gating ring domain of the closed KCNT1 channel CC harbors multiple K(+) and Zn(2+) sites, which stabilize the channel in CC the closed conformation. Under low-Na(+) conditions, the abundant CC cytoplasmic K(+) ions stabilize the gating ring domain in a closed CC conformation. KCNT1 contains at least two Na(+)-sensitive sites in the CC RCKs domain where Na(+) binding induces expansion and rotation of the CC gating ring that opens the inner gate. {ECO:0000269|PubMed:37494189}. CC -!- DOMAIN: The cytoplasmic N-terminal domain facilitates the localization CC of heteromeric KCNT1/KCNT2 channels to the plasma membrane. CC {ECO:0000250|UniProtKB:Q9Z258}. CC -!- PTM: Phosphorylated by protein kinase C. Phosphorylation of the C- CC terminal domain increases channel activity. CC {ECO:0000250|UniProtKB:Q9Z258}. CC -!- DISEASE: Developmental and epileptic encephalopathy 14 (DEE14) CC [MIM:614959]: A rare epileptic encephalopathy of infancy that combines CC pharmacoresistant seizures with developmental delay. This severe CC neurologic disorder is characterized by onset in the first 6 months of CC life of refractory focal seizures and arrest of psychomotor CC development. Ictal EEG shows discharges that arise randomly from CC various areas of both hemispheres and migrate from one brain region to CC another. {ECO:0000269|PubMed:23086397, ECO:0000269|PubMed:23708187, CC ECO:0000269|PubMed:24029078, ECO:0000269|PubMed:24463883, CC ECO:0000269|PubMed:26993267, ECO:0000269|PubMed:27864847}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Epilepsy, nocturnal frontal lobe, 5 (ENFL5) [MIM:615005]: An CC autosomal dominant focal epilepsy syndrome characterized by childhood CC onset of clusters of motor seizures during sleep. Some patients may CC develop behavioral or psychiatric manifestations and/or intellectual CC disability. The phenotype is more severe than observed in other genetic CC forms of nocturnal frontal lobe epilepsy. CC {ECO:0000269|PubMed:23086396}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated CC (TC 1.A.1.3) subfamily. KCa4.1/KCNT1 sub-subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA92660.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK127272; BAG54469.1; -; mRNA. DR EMBL; AL158822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW88180.1; -; Genomic_DNA. DR EMBL; BC136618; AAI36619.1; -; mRNA. DR EMBL; BC171770; AAI71770.1; -; mRNA. DR EMBL; AB037843; BAA92660.1; ALT_INIT; mRNA. DR CCDS; CCDS35175.2; -. [Q5JUK3-3] DR CCDS; CCDS65188.1; -. [Q5JUK3-4] DR RefSeq; NP_001258932.1; NM_001272003.2. [Q5JUK3-4] DR RefSeq; NP_065873.2; NM_020822.3. [Q5JUK3-3] DR PDB; 8HIR; EM; 3.18 A; A/B/C/D=23-1230. DR PDB; 8HK6; EM; 2.64 A; A/B/C/D=23-1230. DR PDB; 8HKF; EM; 2.66 A; A/B/C/D=23-1230. DR PDB; 8HKK; EM; 2.84 A; A/B/C/D=23-1230. DR PDB; 8HKM; EM; 2.95 A; A/B/C/D=23-1230. DR PDB; 8HKQ; EM; 2.90 A; A/B/C/D=23-1230. DR PDBsum; 8HIR; -. DR PDBsum; 8HK6; -. DR PDBsum; 8HKF; -. DR PDBsum; 8HKK; -. DR PDBsum; 8HKM; -. DR PDBsum; 8HKQ; -. DR AlphaFoldDB; Q5JUK3; -. DR EMDB; EMD-34827; -. DR EMDB; EMD-34847; -. DR EMDB; EMD-34851; -. DR EMDB; EMD-34853; -. DR EMDB; EMD-34855; -. DR EMDB; EMD-34858; -. DR SMR; Q5JUK3; -. DR FunCoup; Q5JUK3; 677. DR IntAct; Q5JUK3; 1. DR STRING; 9606.ENSP00000360822; -. DR BindingDB; Q5JUK3; -. DR ChEMBL; CHEMBL4739688; -. DR DrugBank; DB17045; Phorbol 12-myristate 13-acetate diester. DR DrugBank; DB08837; Tetraethylammonium. DR DrugCentral; Q5JUK3; -. DR GuidetoPHARMACOLOGY; 385; -. DR GlyCosmos; Q5JUK3; 2 sites, No reported glycans. DR GlyGen; Q5JUK3; 2 sites. DR iPTMnet; Q5JUK3; -. DR PhosphoSitePlus; Q5JUK3; -. DR BioMuta; KCNT1; -. DR DMDM; 73920089; -. DR MassIVE; Q5JUK3; -. DR PaxDb; 9606-ENSP00000360822; -. DR PeptideAtlas; Q5JUK3; -. DR ProteomicsDB; 34049; -. DR ProteomicsDB; 63278; -. [Q5JUK3-1] DR ProteomicsDB; 63279; -. [Q5JUK3-2] DR ProteomicsDB; 7527; -. DR ABCD; Q5JUK3; 1 sequenced antibody. DR Antibodypedia; 32072; 174 antibodies from 26 providers. DR DNASU; 57582; -. DR Ensembl; ENST00000371757.7; ENSP00000360822.2; ENSG00000107147.14. [Q5JUK3-3] DR Ensembl; ENST00000487664.5; ENSP00000417851.2; ENSG00000107147.14. [Q5JUK3-2] DR Ensembl; ENST00000488444.6; ENSP00000419007.3; ENSG00000107147.14. [Q5JUK3-1] DR Ensembl; ENST00000628528.2; ENSP00000486374.1; ENSG00000107147.14. [Q5JUK3-4] DR GeneID; 57582; -. DR KEGG; hsa:57582; -. DR MANE-Select; ENST00000371757.7; ENSP00000360822.2; NM_020822.3; NP_065873.2. [Q5JUK3-3] DR UCSC; uc011mdq.3; human. [Q5JUK3-1] DR AGR; HGNC:18865; -. DR CTD; 57582; -. DR DisGeNET; 57582; -. DR GeneCards; KCNT1; -. DR GeneReviews; KCNT1; -. DR HGNC; HGNC:18865; KCNT1. DR HPA; ENSG00000107147; Tissue enhanced (brain, lymphoid tissue, skeletal muscle). DR MalaCards; KCNT1; -. DR MIM; 608167; gene. DR MIM; 614959; phenotype. DR MIM; 615005; phenotype. DR neXtProt; NX_Q5JUK3; -. DR OpenTargets; ENSG00000107147; -. DR Orphanet; 293181; Epilepsy of infancy with migrating focal seizures. DR Orphanet; 98784; Sleep-related hypermotor epilepsy. DR PharmGKB; PA38725; -. DR VEuPathDB; HostDB:ENSG00000107147; -. DR eggNOG; KOG3193; Eukaryota. DR GeneTree; ENSGT00940000156880; -. DR InParanoid; Q5JUK3; -. DR OMA; GMCSIEH; -. DR OrthoDB; 257992at2759; -. DR PAN-GO; Q5JUK3; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q5JUK3; -. DR TreeFam; TF314283; -. DR PathwayCommons; Q5JUK3; -. DR SignaLink; Q5JUK3; -. DR BioGRID-ORCS; 57582; 13 hits in 1142 CRISPR screens. DR ChiTaRS; KCNT1; human. DR GeneWiki; KCNT1; -. DR GenomeRNAi; 57582; -. DR Pharos; Q5JUK3; Tchem. DR PRO; PR:Q5JUK3; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q5JUK3; protein. DR Bgee; ENSG00000107147; Expressed in right hemisphere of cerebellum and 95 other cell types or tissues. DR ExpressionAtlas; Q5JUK3; baseline and differential. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005228; F:intracellular sodium-activated potassium channel activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB. DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB. DR FunFam; 3.40.50.720:FF:000011; Potassium channel subfamily T member 1; 1. DR FunFam; 3.40.50.720:FF:000034; Potassium channel subfamily T member 1; 1. DR FunFam; 1.10.287.70:FF:000069; Potassium sodium-activated channel subfamily T member 1; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2. DR InterPro; IPR003929; K_chnl_BK_asu. DR InterPro; IPR013099; K_chnl_dom. DR InterPro; IPR047871; K_chnl_Slo-like. DR InterPro; IPR003148; RCK_N. DR PANTHER; PTHR10027; CALCIUM-ACTIVATED POTASSIUM CHANNEL ALPHA CHAIN; 1. DR PANTHER; PTHR10027:SF14; POTASSIUM CHANNEL SUBFAMILY T MEMBER 1; 1. DR Pfam; PF03493; BK_channel_a; 1. DR Pfam; PF07885; Ion_trans_2; 1. DR Pfam; PF22614; Slo-like_RCK; 2. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR PROSITE; PS51201; RCK_N; 2. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell membrane; KW Disease variant; Epilepsy; Glycoprotein; Ion channel; Ion transport; KW Membrane; Metal-binding; Phosphoprotein; Potassium; Potassium channel; KW Potassium transport; Proteomics identification; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Zinc. FT CHAIN 1..1230 FT /note="Potassium channel subfamily T member 1" FT /id="PRO_0000054090" FT TOPO_DOM 1..93 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 94..126 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000269|PubMed:23086396, FT ECO:0007744|PDB:8HIR" FT TOPO_DOM 127..153 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 154..178 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000269|PubMed:23086396, FT ECO:0007744|PDB:8HIR" FT TOPO_DOM 179..192 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 193..208 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000269|PubMed:23086396, FT ECO:0007744|PDB:8HIR" FT TOPO_DOM 209..215 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 216..233 FT /note="Helical; Name=Segment S4" FT /evidence="ECO:0000269|PubMed:23086396, FT ECO:0007744|PDB:8HIR" FT TOPO_DOM 234..246 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 247..274 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000305" FT TOPO_DOM 275..281 FT /note="Extracellular" FT /evidence="ECO:0000305" FT INTRAMEM 282..302 FT /note="Pore-forming" FT /evidence="ECO:0000269|PubMed:23086396, FT ECO:0007744|PDB:8HIR" FT TOPO_DOM 303..304 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 305..338 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000269|PubMed:23086396, FT ECO:0007744|PDB:8HIR" FT TOPO_DOM 339..1230 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 352..488 FT /note="RCK N-terminal 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543" FT DOMAIN 781..921 FT /note="RCK N-terminal 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 660..689 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1048..1078 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1204..1230 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1057..1072 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1204..1219 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 296 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /ligand_note="ligand shared between homotetrameric FT partners" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 297 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /ligand_note="ligand shared between homotetrameric FT partners" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 513 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 516 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 538 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 540 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 758 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 759 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 761 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 761 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 764 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 764 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 766 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 768 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HIR" FT BINDING 769 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 771 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 771 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 777 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 778 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HK6" FT BINDING 779 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HKK" FT BINDING 787 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HK6" FT BINDING 818 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HK6" FT BINDING 820 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HK6" FT BINDING 842 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HK6" FT BINDING 865 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:37494189, FT ECO:0007744|PDB:8HK6" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 137 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..66 FT /note="MARAKLPRSPSEGKAGPGGAPAGAAAPEEPHGLSPLLPARGGGSVGSDVGQR FT LPVEDFSLDSSLSQ -> MPLPDGARTPGGVCREARGGGYTNRTFEFDDGQCAPRRPCA FT GDGALLDTAGFKMSDLDSEVLPLPPRYRFRDLLLGDPSFQNDDR (in isoform 2 FT and isoform 3)" FT /evidence="ECO:0000303|PubMed:10718198, FT ECO:0000303|PubMed:15489334" FT /id="VSP_015470" FT VAR_SEQ 1..66 FT /note="MARAKLPRSPSEGKAGPGGAPAGAAAPEEPHGLSPLLPARGGGSVGSDVGQR FT LPVEDFSLDSSLSQ -> MPLPDGARTPGGVCREARGGGYTNRTFEFDDGQCAPR (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055700" FT VAR_SEQ 266 FT /note="G -> GGCR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055701" FT VAR_SEQ 1033 FT /note="E -> EPHDLRAQ (in isoform 2, isoform 3 and isoform FT 4)" FT /evidence="ECO:0000303|PubMed:10718198, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_015471" FT VAR_SEQ 1142..1162 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044476" FT VARIANT 269 FT /note="G -> S (in DEE14; dbSNP:rs587777264)" FT /evidence="ECO:0000269|PubMed:24029078, FT ECO:0000269|PubMed:26993267" FT /id="VAR_078683" FT VARIANT 379 FT /note="R -> Q (in ENFL5; dbSNP:rs397515407)" FT /evidence="ECO:0000269|PubMed:23086396" FT /id="VAR_069311" FT VARIANT 409 FT /note="R -> Q (in DEE14; gain-of-function mutation; FT dbSNP:rs397515402)" FT /evidence="ECO:0000269|PubMed:23086397" FT /id="VAR_069312" FT VARIANT 455 FT /note="R -> H (in DEE14; dbSNP:rs397515404)" FT /evidence="ECO:0000269|PubMed:23086397" FT /id="VAR_069313" FT VARIANT 497 FT /note="M -> V (in DEE14; dbSNP:rs886041691)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078214" FT VARIANT 562 FT /note="T -> I (in DEE14; uncertain significance; FT dbSNP:rs1185192267)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078641" FT VARIANT 741 FT /note="I -> M (in DEE14; dbSNP:rs370521183)" FT /evidence="ECO:0000269|PubMed:23086397" FT /id="VAR_069314" FT VARIANT 777 FT /note="Y -> H (in ENFL5; dbSNP:rs397515406)" FT /evidence="ECO:0000269|PubMed:23086396" FT /id="VAR_069315" FT VARIANT 877 FT /note="M -> I (in ENFL5; dbSNP:rs797044544)" FT /evidence="ECO:0000269|PubMed:23086396" FT /id="VAR_069316" FT VARIANT 877 FT /note="M -> K (in DEE14; uncertain significance)" FT /evidence="ECO:0000269|PubMed:26993267" FT /id="VAR_078684" FT VARIANT 909 FT /note="R -> C (in ENFL5; dbSNP:rs397515405)" FT /evidence="ECO:0000269|PubMed:23086396" FT /id="VAR_069317" FT VARIANT 915 FT /note="A -> T (in DEE14; gain-of-function mutation; FT dbSNP:rs397515403)" FT /evidence="ECO:0000269|PubMed:23086397, FT ECO:0000269|PubMed:26993267" FT /id="VAR_069318" FT VARIANT 928 FT /note="K -> E (in DEE14; dbSNP:rs1057519544)" FT /evidence="ECO:0000269|PubMed:27864847" FT /id="VAR_078215" FT VARIANT 947 FT /note="A -> T (in DEE14; variant homolog in rat has FT increased channel activity upon positive potentials; FT dbSNP:rs1424788778)" FT /evidence="ECO:0000269|PubMed:24463883" FT /id="VAR_078685" FT VARIANT 1088 FT /note="R -> Q (in DEE14; uncertain significance; FT dbSNP:rs758311066)" FT /evidence="ECO:0000269|PubMed:23708187" FT /id="VAR_078642" FT MUTAGEN 315 FT /note="M->L: Reduced the potency of the agonist C23 by 7-8 FT fold." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 319 FT /note="A->T: Reduced the potency of the agonist C23 by 7-8 FT fold." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 327 FT /note="F->A: Reduced the potency of the agonist C23 by 28 FT fold." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 541 FT /note="E->D,N,A: Dramatically reduced the Na(+) sensitivity FT of KCNT1." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 758..759 FT /note="CC->AA: Decreased inhibition by Zn(2+)." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 769 FT /note="N->A: Reduced the Na(+) sensitivity of KCNT1." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 777 FT /note="Y->F: Reduced the Na(+) sensitivity of KCNT1." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 820 FT /note="D->N: Dramatically reduced the Na(+) sensitivity of FT KCNT1." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 865 FT /note="D->A: Dramatically reduced the Na(+) sensitivity of FT KCNT1." FT /evidence="ECO:0000269|PubMed:37494189" FT MUTAGEN 873..876 FT /note="EEDY->AAAA: Dramatically reduced the Na(+) FT sensitivity of KCNT1." FT /evidence="ECO:0000269|PubMed:37494189" FT CONFLICT 107 FT /note="T -> I (in Ref. 1; BAG54469)" FT /evidence="ECO:0000305" FT CONFLICT 498 FT /note="L -> P (in Ref. 1; BAG54469)" FT /evidence="ECO:0000305" FT CONFLICT 615 FT /note="A -> V (in Ref. 4; AAI71770)" FT /evidence="ECO:0000305" FT CONFLICT 822 FT /note="K -> E (in Ref. 1; BAG54469)" FT /evidence="ECO:0000305" FT CONFLICT 969 FT /note="M -> K (in Ref. 1; BAG54469)" FT /evidence="ECO:0000305" FT HELIX 92..117 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 126..129 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 146..149 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 155..178 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 187..189 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 193..208 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 210..212 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 219..221 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 222..234 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 248..273 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 274..278 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 282..293 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 306..337 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 354..358 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 364..374 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 378..380 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 384..388 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 395..401 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 404..407 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 410..413 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 420..425 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 426..430 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 434..436 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 445..462 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 468..474 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 475..480 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 484..489 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 490..501 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 507..514 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 522..525 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 529..537 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 541..547 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 551..553 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 554..556 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 561..571 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 575..580 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 588..590 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 602..609 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 611..613 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 615..624 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 731..733 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 748..750 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 757..760 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 761..764 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 774..777 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 783..787 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 793..802 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 809..811 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 815..821 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 825..831 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 834..841 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 847..853 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 855..857 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 858..863 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 875..879 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 880..892 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 897..904 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 907..910 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 918..932 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 938..941 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 943..946 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 949..952 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 955..962 FT /evidence="ECO:0007829|PDB:8HKM" FT TURN 963..965 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 969..977 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 987..993 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 995..997 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 1003..1013 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 1017..1026 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 1103..1116 FT /evidence="ECO:0007829|PDB:8HKM" FT HELIX 1119..1134 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 1171..1178 FT /evidence="ECO:0007829|PDB:8HKM" FT STRAND 1189..1195 FT /evidence="ECO:0007829|PDB:8HKM" SQ SEQUENCE 1230 AA; 138343 MW; 482D70015434493E CRC64; MARAKLPRSP SEGKAGPGGA PAGAAAPEEP HGLSPLLPAR GGGSVGSDVG QRLPVEDFSL DSSLSQVQVE FYVNENTFKE RLKLFFIKNQ RSSLRIRLFN FSLKLLTCLL YIVRVLLDDP ALGIGCWGCP KQNYSFNDSS SEINWAPILW VERKMTLWAI QVIVAIISFL ETMLLIYLSY KGNIWEQIFR VSFVLEMINT LPFIITIFWP PLRNLFIPVF LNCWLAKHAL ENMINDFHRA ILRTQSAMFN QVLILFCTLL CLVFTGTCGI QHLERAGENL SLLTSFYFCI VTFSTVGYGD VTPKIWPSQL LVVIMICVAL VVLPLQFEEL VYLWMERQKS GGNYSRHRAQ TEKHVVLCVS SLKIDLLMDF LNEFYAHPRL QDYYVVILCP TEMDVQVRRV LQIPLWSQRV IYLQGSALKD QDLMRAKMDN GEACFILSSR NEVDRTAADH QTILRAWAVK DFAPNCPLYV QILKPENKFH VKFADHVVCE EECKYAMLAL NCICPATSTL ITLLVHTSRG QEGQESPEQW QRMYGRCSGN EVYHIRMGDS KFFREYEGKS FTYAAFHAHK KYGVCLIGLK REDNKSILLN PGPRHILAAS DTCFYINITK EENSAFIFKQ EEKRKKRAFS GQGLHEGPAR LPVHSIIASM GTVAMDLQGT EHRPTQSGGG GGGSKLALPT ENGSGSRRPS IAPVLELADS SALLPCDLLS DQSEDEVTPS DDEGLSVVEY VKGYPPNSPY IGSSPTLCHL LPVKAPFCCL RLDKGCKHNS YEDAKAYGFK NKLIIVSAET AGNGLYNFIV PLRAYYRSRK ELNPIVLLLD NKPDHHFLEA ICCFPMVYYM EGSVDNLDSL LQCGIIYADN LVVVDKESTM SAEEDYMADA KTIVNVQTMF RLFPSLSITT ELTHPSNMRF MQFRAKDSYS LALSKLEKRE RENGSNLAFM FRLPFAAGRV FSISMLDTLL YQSFVKDYMI TITRLLLGLD TTPGSGYLCA MKITEGDLWI RTYGRLFQKL CSSSAEIPIG IYRTESHVFS TSESQISVNV EDCEDTREVK GPWGSRAGTG GSSQGRHTGG GDPAEHPLLR RKSLQWARRL SRKAPKQAGR AAAAEWISQQ RLSLYRRSER QELSELVKNR MKHLGLPTTG YEDVANLTAS DVMNRVNLGY LQDEMNDHQN TLSYVLINPP PDTRLEPSDI VYLIRSDPLA HVASSSQSRK SSCSHKLSSC NPETRDETQL //