ID KCNT1_MOUSE Reviewed; 1224 AA. AC Q6ZPR4; B2RUK3; C0KTP6; Q8C3E7; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2005, sequence version 2. DT 02-SEP-2026, entry version 160. DE RecName: Full=Potassium channel subfamily T member 1; GN Name=Kcnt1; GN Synonyms=Kiaa1422, Slack {ECO:0000303|PubMed:18787033, GN ECO:0000303|PubMed:25609627}, Slo2.2 {ECO:0000303|PubMed:26559620}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-297. RC STRAIN=C57BL/6J; TISSUE=Head; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-1224. RC TISSUE=Brain; RX PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III. RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs RT identified by screening of terminal sequences of cDNA clones randomly RT sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [4] RP NUCLEOTIDE SEQUENCE (ISOFORM 2), AND TISSUE SPECIFICITY. RX PubMed=18787033; DOI=10.1113/jphysiol.2008.160861; RA Brown M.R., Kronengold J., Gazula V.R., Spilianakis C.G., Flavell R.A., RA von Hehn C.A., Bhattacharjee A., Kaczmarek L.K.; RT "Amino-termini isoforms of the Slack K+ channel, regulated by alternative RT promoters, differentially modulate rhythmic firing and adaptation."; RL J. Physiol. (Lond.) 586:5161-5179(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). 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] RP INTERACTION WITH KCNT2, AND SUBCELLULAR LOCATION. RX PubMed=29124216; DOI=10.1016/j.bbrep.2015.09.024; RA Rizzi S., Schwarzer C., Kremser L., Lindner H.H., Knaus H.G.; RT "Identification of potential novel interaction partners of the sodium- RT activated potassium channels Slick and Slack in mouse brain."; RL Biochem. Biophys. Rep. 4:291-298(2015). RN [8] RP FUNCTION, TRANSPORTER ACTIVITY, AND DISRUPTION PHENOTYPE. RX PubMed=26559620; DOI=10.7554/elife.10013; RA Martinez-Espinosa P.L., Wu J., Yang C., Gonzalez-Perez V., Zhou H., RA Liang H., Xia X.M., Lingle C.J.; RT "Knockout of Slo2.2 enhances itch, abolishes KNa current, and increases RT action potential firing frequency in DRG neurons."; RL Elife 4:0-0(2015). RN [9] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=25609627; DOI=10.1523/jneurosci.2423-14.2015; RA Lu R., Bausch A.E., Kallenborn-Gerhardt W., Stoetzer C., Debruin N., RA Ruth P., Geisslinger G., Leffler A., Lukowski R., Schmidtko A.; RT "Slack channels expressed in sensory neurons control neuropathic pain in RT mice."; RL J. Neurosci. 35:1125-1135(2015). RN [10] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=32081855; DOI=10.1038/s41598-020-60028-z; RA Quraishi I.H., Mercier M.R., McClure H., Couture R.L., Schwartz M.L., RA Lukowski R., Ruth P., Kaczmarek L.K.; RT "Impaired motor skill learning and altered seizure susceptibility in mice RT with loss or gain of function of the Kcnt1 gene encoding Slack (KNa1.1) RT Na+-activated K+ channels."; RL Sci. Rep. 10:3213-3213(2020). RN [11] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=34664085; DOI=10.1007/s00018-021-03953-0; RA Matt L., Pham T., Skrabak D., Hoffmann F., Eckert P., Yin J., Gisevius M., RA Ehinger R., Bausch A., Ueffing M., Boldt K., Ruth P., Lukowski R.; RT "The Na+-activated K+ channel Slack contributes to synaptic development and RT plasticity."; RL Cell. Mol. Life Sci. 78:7569-7587(2021). CC -!- FUNCTION: Sodium-activated K(+) channel (PubMed:26559620). Acts as an CC important mediator of neuronal membrane excitability (By similarity). CC Contributes to the delayed outward currents (By similarity). Regulates CC neuronal bursting in sensory neurons (PubMed:25609627, CC PubMed:26559620). Contributes to synaptic development and plasticity CC (PubMed:32081855, PubMed:34664085). {ECO:0000250|UniProtKB:Q5JUK3, CC ECO:0000250|UniProtKB:Q9Z258, ECO:0000269|PubMed:25609627, CC ECO:0000269|PubMed:26559620, ECO:0000269|PubMed:32081855, CC ECO:0000269|PubMed:34664085}. CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:26559620}; CC -!- ACTIVITY REGULATION: Activated by high intracellular Na(+) (By CC similarity). In addition to activation by Na(+), is cooperatively CC activated by intracellular Cl(-) levels (By similarity). Inhibited by CC Zn(2+) (By similarity). Activated upon stimulation of G protein-coupled CC receptors, such as CHRM1 and GRIA1 (By similarity). CC {ECO:0000250|UniProtKB:Q5JUK3, ECO:0000250|UniProtKB:Q9Z258}. CC -!- SUBUNIT: Homotetramer; which constitutes the Na(+)-activated K(+) CC channel (By similarity). 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 (By similarity). CC Interacts with CRBN via its cytoplasmic C-terminus (By similarity). CC {ECO:0000250|UniProtKB:Q5JUK3, ECO:0000250|UniProtKB:Q9Z258}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:29124216}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5JUK3}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=1; Synonyms=Slack-B {ECO:0000303|PubMed:18787033}; CC IsoId=Q6ZPR4-1; Sequence=Displayed; CC Name=2; Synonyms=Slack-A {ECO:0000303|PubMed:18787033}; CC IsoId=Q6ZPR4-2; Sequence=VSP_062459; CC -!- TISSUE SPECIFICITY: [Isoform 2]: Enriched in the brainstem and CC olfactory bulb and detected at significant levels in four different CC brain regions. {ECO:0000269|PubMed:18787033}. 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. The open KCNT1 structure contains at least two Na(+)- CC sensitive sites in the RCKs where Na(+) binding induces expansion and CC rotation of the gating ring that opens the inner gate. CC {ECO:0000250|UniProtKB:Q5JUK3}. 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 -!- DISRUPTION PHENOTYPE: Kcnt2-null mice exhibit impaired action potential CC firing in sensory neurons and increased mechanical hypersensitivity in CC neuropathic pain models (PubMed:25609627, PubMed:26559620). Deficient CC mice display impaired motor skill learning (PubMed:32081855). Kcnt2- CC null mice exhibit severely impaired synaptic function in the CC hippocampus of infant and milder deficits in adult Kcnt2-deficient mice CC (PubMed:34664085). {ECO:0000269|PubMed:25609627, CC ECO:0000269|PubMed:26559620, ECO:0000269|PubMed:32081855, CC ECO:0000269|PubMed:34664085}. 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 --------------------------------------------------------------------------- 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; BC141190; AAI41191.1; -; mRNA. DR EMBL; BC171963; AAI71963.1; -; mRNA. DR EMBL; AK086119; BAC39614.1; -; mRNA. DR EMBL; FJ628361; ACM90117.1; -; mRNA. DR EMBL; AK129355; BAC98165.1; -; mRNA. DR CCDS; CCDS50537.1; -. [Q6ZPR4-2] DR CCDS; CCDS79757.1; -. [Q6ZPR4-1] DR RefSeq; NP_001138875.1; NM_001145403.3. [Q6ZPR4-2] DR RefSeq; NP_001289280.1; NM_001302351.2. [Q6ZPR4-1] DR RefSeq; NP_780671.2; NM_175462.5. DR AlphaFoldDB; Q6ZPR4; -. DR SMR; Q6ZPR4; -. DR BioGRID; 230652; 2. DR FunCoup; Q6ZPR4; 955. DR IntAct; Q6ZPR4; 3. DR MINT; Q6ZPR4; -. DR STRING; 10090.ENSMUSP00000039058; -. DR BindingDB; Q6ZPR4; -. DR ChEMBL; CHEMBL4739694; -. DR GuidetoPHARMACOLOGY; 385; -. DR GlyCosmos; Q6ZPR4; 2 sites, No reported glycans. DR GlyGen; Q6ZPR4; 5 sites, 2 N-linked glycans (2 sites). DR iPTMnet; Q6ZPR4; -. DR PhosphoSitePlus; Q6ZPR4; -. DR PaxDb; 10090-ENSMUSP00000039058; -. DR ProteomicsDB; 268967; -. DR ProteomicsDB; 331165; -. DR ABCD; Q6ZPR4; 1 sequenced antibody. DR Antibodypedia; 32072; 178 antibodies from 28 providers. DR DNASU; 227632; -. DR Ensembl; ENSMUST00000114172.6; ENSMUSP00000109809.3; ENSMUSG00000058740.15. [Q6ZPR4-1] DR Ensembl; ENSMUST00000171268.8; ENSMUSP00000132212.2; ENSMUSG00000058740.15. [Q6ZPR4-2] DR GeneID; 227632; -. DR KEGG; mmu:227632; -. DR UCSC; uc008itq.2; mouse. [Q6ZPR4-1] DR AGR; MGI:1924627; -. DR CTD; 57582; -. DR MGI; MGI:1924627; Kcnt1. DR VEuPathDB; HostDB:ENSMUSG00000058740; -. DR eggNOG; KOG3193; Eukaryota. DR GeneTree; ENSGT00940000156880; -. DR InParanoid; Q6ZPR4; -. DR OrthoDB; 257992at2759; -. DR BioGRID-ORCS; 227632; 3 hits in 77 CRISPR screens. DR PRO; PR:Q6ZPR4; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q6ZPR4; protein. DR Bgee; ENSMUSG00000058740; Expressed in cerebellar cortex and 115 other cell types or tissues. DR ExpressionAtlas; Q6ZPR4; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098839; C:postsynaptic density membrane; IDA:SynGO. DR GO; GO:0070089; F:chloride-activated potassium channel activity; ISO:GO_Central. DR GO; GO:0005228; F:intracellular sodium-activated potassium channel activity; ISO:GO_Central. DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISS:UniProtKB. DR GO; GO:0005267; F:potassium channel activity; ISO:GO_Central. DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB. DR GO; GO:0006813; P:potassium ion transport; ISO:GO_Central. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IDA:SynGO. 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 Alternative promoter usage; Calcium; Cell membrane; Glycoprotein; KW Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein; KW Potassium; Potassium channel; Potassium transport; Reference proteome; KW Sodium; Transmembrane; Transmembrane helix; Transport; Zinc. FT CHAIN 1..1224 FT /note="Potassium channel subfamily T member 1" FT /id="PRO_0000054091" FT TOPO_DOM 1..79 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 80..112 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 113..139 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 140..164 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 165..178 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 179..194 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 195..201 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 202..219 FT /note="Helical; Name=Segment S4" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 220..232 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 233..260 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 261..267 FT /note="Extracellular" FT /evidence="ECO:0000305" FT INTRAMEM 268..288 FT /note="Pore-forming" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 289..290 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 291..324 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT TOPO_DOM 325..1224 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT DOMAIN 338..474 FT /note="RCK N-terminal 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00543" FT DOMAIN 767..907 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 644..675 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1038..1066 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1198..1224 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 13..27 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 663..673 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1045..1055 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1198..1215 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 282 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:0000250|UniProtKB:Q5JUK3" FT BINDING 283 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:0000250|UniProtKB:Q5JUK3" FT BINDING 499 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 502 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 524 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 526 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 744 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 745 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 747 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 747 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 750 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 750 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 752 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 754 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 755 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 757 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 757 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 763 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="3" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 764 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 765 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 773 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 804 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 806 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 828 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT BINDING 851 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:Q5JUK3" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 2..52 FT /note="ARAKLPRSPSEGKAGPGDTPAGAAAPEEPHGLSPLLPARGGGSVGSDVGQR FT -> NDLDTEVLPLPPRYRFRDLLLGDQPFPNDDRLHVEDFSLDSSLSQ (in FT isoform 2)" FT /id="VSP_062459" SQ SEQUENCE 1224 AA; 138106 MW; 7F343893D70E506B CRC64; MARAKLPRSP SEGKAGPGDT PAGAAAPEEP HGLSPLLPAR GGGSVGSDVG QRVQVEFYVN ENTFKERLKL FFIKNQRSSL RIRLFNFSLK LLTCLLYIVR VLLDNPDQGI GCWGCTKYNY TFNGSSSEFH WAPILWVERK MALWVIQVIV ATISFLETML IIYLSYKGNI WEQIFHVSFV LEMINTLPFI ITVFWPPLRN LFIPVFLNCW LAKHALENMI NDFHRAILRT QSAMFNQVLI LFCTLLCLVF TGTCGIQHLE RAGGNLNLLT SFYFCIVTFS TVGFGDVTPK IWPSQLLVVI LICVTLVVLP LQFEELVYLW MERQKSGGNY SRHRARTEKH VVLCVSSLKI DLLMDFLNEF YAHPRLQDYY VVILCPSEMD VQVRRVLQIP LWSQRVIYLQ GSALKDQDLM RAKMDNGEAC FILSSRNEVD RTAADHQTIL RAWAVKDFAP NCPLYVQILK PENKFHVKFA DHVVCEEECK YAMLALNCIC PATSTLITLL VHTSRGQEGQ ESPEQWQRTY GRCSGNEVYH IRMGDSKFFR EYEGKSFTYA AFHAHKKYGV CLIGLKREEN KSILLNPGPR HILAASDTCF YINITKEENS AFIFKQEEKQ KRRGLAGQAL YEGPSRLPVH SIIASMGTVA MDLQNTDCRP SQGGSGGDGT KLTLPTENGS GSRRPSIAPV LELADSSALL PCDLLSDQSE DEVTPSDDEG LSVVEYVKGY PPNSPYIGSS PTLCHLLPVK APFCCLRLDK GCKHNSYEDA KAYGFKNKLI IVSAETAGNG LYNFIVPLRA YYRSRRELNP IVLLLDNKPD HHFLEAICCF PMVYYMEGSV DNLDSLLQCG IIYADNLVVV DKESTMSAEE DYMADAKTIV NVQTMFRLFP SLSITTELTH PSNMRFMQFR AKDSYSLALS KLEKQERENG SNLAFMFRLP FAAGRVFSIS MLDTLLYQSF VKDYMITITR LLLGLDTTPG SGYLCAMKVT EDDLWIRTYG RLFQKLCSSS AEIPIGIYRT ECHVFSEPHD VRAQSQISVN MEDCEDTREA KGPWGTRAAS GSGSTHGRHG GSADPVEHPL LRRKSLQWAR KLSRKSTKQA GKAPVATDWI TQQRLSLYRR SERQELSELV KNRMKHLGLP TTGYEDVANL TASDVMNRVN LGYLQDEMND HHQNTLSYVL INPPPDTRLE PNDIVYLIRS DPLAHVASSS QSRKSSCSNK LSSCNPETRD ETQL //