ID KCND1_HUMAN Reviewed; 647 AA. AC Q9NSA2; A6NEF1; B2RCG0; O75671; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 07-NOV-2003, sequence version 2. DT 04-NOV-2026, entry version 196. DE RecName: Full=A-type voltage-gated potassium channel KCND1 {ECO:0000305}; DE AltName: Full=Potassium voltage-gated channel subfamily D member 1 {ECO:0000305}; DE AltName: Full=Shal-type potassium channel KCND1 {ECO:0000303|Ref.2}; DE AltName: Full=Voltage-gated potassium channel subunit Kv4.1; GN Name=KCND1 {ECO:0000312|HGNC:HGNC:6237}; 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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE RP SPECIFICITY. RC TISSUE=Embryonic kidney; RX PubMed=10729221; DOI=10.1006/geno.2000.6117; RA Isbrandt D., Leicher T., Waldschuetz R., Zhu X.-R., Luhmann U., Michel U., RA Sauter K., Pongs O.; RT "Gene structures and expression profiles of three human KCND (Kv4) RT potassium channels mediating A-type currents I(TO) and I(SA)."; RL Genomics 64:144-154(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Heart; RA Makita N., Shirai N., Sawa H., Sasaki K., Nagashima K., Yoshida M.C., RA Kitabatake A.; RT "Homo sapiens mRNA for shal-type potassium channel KCND1 (Kv4.1)."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., RA Meindl A.; RT "Transcription map in Xp11.23."; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Cerebellum; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [8] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=15454437; DOI=10.1529/biophysj.104.042358; RA Jerng H.H., Qian Y., Pfaffinger P.J.; RT "Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase RT 10 (DPP10)."; RL Biophys. J. 87:2380-2396(2004). CC -!- FUNCTION: A-type voltage-gated potassium channel that mediates CC transmembrane potassium transport in excitable membranes in the brain CC (PubMed:15454437). Mediates A-type current I(SA) in suprachiasmatic CC nucleus (SCN) neurons. Exhibits a low-threshold A-type current with a CC hyperpolarized steady-state inactivation midpoint and the recovery CC process was steeply voltage-dependent, with recovery being markedly CC faster at more negative potentials. May regulates repetitive firing CC rates in the suprachiasmatic nucleus (SCN) neurons and circadian CC rhythms in neuronal excitability and behavior. Contributes to the CC regulation of the circadian rhythm of action potential firing in CC suprachiasmatic nucleus neurons, which regulates the circadian rhythm CC of locomotor activity. The regulatory subunit KCNIP1 modulates the CC kinetics of channel inactivation, increases the current amplitudes and CC accelerates recovery from inactivation, shifts activation in a CC depolarizing direction (By similarity). The regulatory subunit DPP10 CC decreases the voltage sensitivity of the inactivation channel gating CC (PubMed:15454437). {ECO:0000250|UniProtKB:Q03719, CC ECO:0000269|PubMed:15454437}. CC -!- CATALYTIC ACTIVITY: CC Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:15454437}; CC -!- SUBUNIT: Component of heteromultimeric potassium channels. Identified CC in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, CC KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10. {ECO:0000250|UniProtKB:Q03719}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NZV8}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NZV8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NSA2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NSA2-2; Sequence=VSP_057040; CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, in CC particular in cerebellum and thalamus; detected at lower levels in the CC other parts of the brain. {ECO:0000269|PubMed:10729221}. CC -!- DOMAIN: The transmembrane segment S4 functions as a voltage-sensor and CC is characterized by a series of positively charged amino acids at every CC third position. Channel opening and closing is effected by a CC conformation change that affects the position and orientation of the CC voltage-sensor paddle formed by S3 and S4 within the membrane. A CC transmembrane electric field that is positive inside would push the CC positively charged S4 segment outwards, thereby opening the pore, while CC a field that is negative inside would pull the S4 segment inwards and CC close the pore. Changes in the position and orientation of S4 are then CC transmitted to the activation gate formed by the inner helix bundle via CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. CC -!- DOMAIN: The zinc binding sites in the N-terminal domain are important CC for tetramerization and assembly of a functional channel complex (By CC similarity). Most likely, the channel undergoes closed-state CC inactivation, where a subtle conformation change would render the CC protein less sensitive to activation (By similarity). CC {ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9NZV8}. CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) CC (TC 1.A.1.2) subfamily. Kv4.1/KCND1 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; AF166003; AAF65516.1; -; mRNA. DR EMBL; AF166006; AAF65617.1; -; Genomic_DNA. DR EMBL; AF166004; AAF65617.1; JOINED; Genomic_DNA. DR EMBL; AF166005; AAF65617.1; JOINED; Genomic_DNA. DR EMBL; AB021865; BAA96454.1; -; mRNA. DR EMBL; AJ005898; CAA06755.1; -; mRNA. DR EMBL; AK094431; BAG52865.1; -; mRNA. DR EMBL; AK315092; BAG37557.1; -; mRNA. DR EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471224; EAW50720.1; -; Genomic_DNA. DR EMBL; CH471224; EAW50721.1; -; Genomic_DNA. DR EMBL; BC045659; AAH45659.1; -; mRNA. DR CCDS; CCDS14314.1; -. [Q9NSA2-1] DR RefSeq; NP_004970.3; NM_004979.6. [Q9NSA2-1] DR AlphaFoldDB; Q9NSA2; -. DR SMR; Q9NSA2; -. DR BioGRID; 109952; 2. DR FunCoup; Q9NSA2; 20. DR IntAct; Q9NSA2; 1. DR STRING; 9606.ENSP00000218176; -. DR ChEMBL; CHEMBL2362996; -. DR DrugBank; DB06637; Dalfampridine. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01069; Promethazine. DR DrugCentral; Q9NSA2; -. DR GuidetoPHARMACOLOGY; 552; -. DR TCDB; 1.A.1.2.28; the voltage-gated ion channel (vic) superfamily. DR GlyCosmos; Q9NSA2; 2 sites, No reported glycans. DR GlyGen; Q9NSA2; 2 sites. DR iPTMnet; Q9NSA2; -. DR PhosphoSitePlus; Q9NSA2; -. DR BioMuta; KCND1; -. DR DMDM; 38258256; -. DR jPOST; Q9NSA2; -. DR MassIVE; Q9NSA2; -. DR PaxDb; 9606-ENSP00000218176; -. DR PeptideAtlas; Q9NSA2; -. DR ProteomicsDB; 82521; -. [Q9NSA2-1] DR ProteomicsDB; 980; -. DR Antibodypedia; 370; 304 antibodies from 33 providers. DR DNASU; 3750; -. DR Ensembl; ENST00000218176.4; ENSP00000218176.3; ENSG00000102057.12. [Q9NSA2-1] DR Ensembl; ENST00000376477.6; ENSP00000365660.1; ENSG00000102057.12. [Q9NSA2-2] DR Ensembl; ENST00000710081.1; ENSP00000518043.1; ENSG00000292214.1. [Q9NSA2-2] DR Ensembl; ENST00000710082.1; ENSP00000518044.1; ENSG00000292214.1. [Q9NSA2-1] DR GeneID; 3750; -. DR KEGG; hsa:3750; -. DR MANE-Select; ENST00000218176.4; ENSP00000218176.3; NM_004979.6; NP_004970.3. DR UCSC; uc004dlw.1; human. [Q9NSA2-1] DR AGR; HGNC:6237; -. DR ClinPGx; PA30029; -. DR CTD; 3750; -. DR DisGeNET; 3750; -. DR GeneCards; KCND1; -. DR HGNC; HGNC:6237; KCND1. DR HPA; ENSG00000102057; Tissue enhanced (brain). DR MIM; 300281; gene. DR OpenTargets; ENSG00000102057; -. DR VEuPathDB; HostDB:ENSG00000102057; -. DR eggNOG; KOG4390; Eukaryota. DR GeneTree; ENSGT00940000162057; -. DR HOGENOM; CLU_070236_0_0_1; -. DR InParanoid; Q9NSA2; -. DR OMA; AAFWYXY; -. DR OrthoDB; 433309at2759; -. DR PAN-GO; Q9NSA2; 7 GO annotations based on evolutionary models. DR PhylomeDB; Q9NSA2; -. DR PathwayCommons; Q9NSA2; -. DR Reactome; R-HSA-1296072; Voltage gated Potassium channels. DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels. DR SignaLink; Q9NSA2; -. DR Agora; ENSG00000102057; -. DR BioGRID-ORCS; 3750; 8 hits in 783 CRISPR screens. DR ChiTaRS; KCND1; human. DR GeneWiki; KCND1; -. DR GenomeRNAi; 3750; -. DR Pharos; Q9NSA2; Tclin. DR PRO; PR:Q9NSA2; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9NSA2; protein. DR Bgee; ENSG00000102057; Expressed in primordial germ cell in gonad and 94 other cell types or tissues. DR ExpressionAtlas; Q9NSA2; baseline and differential. DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central. DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IDA:UniProtKB. DR GO; GO:0001508; P:action potential; IBA:GO_Central. DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR FunFam; 1.20.120.350:FF:000016; Potassium voltage-gated channel subfamily D member 3; 1. DR FunFam; 3.30.710.10:FF:000004; Potassium voltage-gated channel subfamily D member 3; 1. DR FunFam; 1.10.287.70:FF:000028; potassium voltage-gated channel subfamily D member 3; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR003968; K_chnl_volt-dep_Kv. DR InterPro; IPR003975; K_chnl_volt-dep_Kv4. DR InterPro; IPR004054; K_chnl_volt-dep_Kv4.1. DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C. DR InterPro; IPR021645; Shal-type_N. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR003131; T1-type_BTB. DR InterPro; IPR028325; VG_K_chnl. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR11537:SF174; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 1; 1. DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF11879; DUF3399; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF11601; Shal-type; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01516; KV41CHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR PRINTS; PR01497; SHALCHANNEL. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Glycoprotein; Ion channel; KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Potassium; KW Potassium channel; Potassium transport; Proteomics identification; KW Reference proteome; Transmembrane; Transmembrane helix; Transport; KW Voltage-gated channel; Zinc. FT CHAIN 1..647 FT /note="A-type voltage-gated potassium channel KCND1" FT /id="PRO_0000054061" FT TOPO_DOM 1..183 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 184..205 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 206..230 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 231..252 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 253..263 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 264..284 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 285..287 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 288..308 FT /note="Helical; Voltage-sensor; Name=Segment S4" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 309..323 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 324..345 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 346..359 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT INTRAMEM 360..371 FT /note="Helical; Name=Pore helix" FT /evidence="ECO:0000250|UniProtKB:P63142" FT INTRAMEM 372..379 FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 380..386 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 387..415 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 416..647 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT REGION 2..20 FT /note="Interaction with KCNIP1, KCNIP2, and other family FT members" FT /evidence="ECO:0000250|UniProtKB:Q63881" FT REGION 144..163 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 310..323 FT /note="S4-S5 linker" FT /evidence="ECO:0000250|UniProtKB:P63142" FT REGION 474..489 FT /note="Required for dendritic targeting" FT /evidence="ECO:0000250|UniProtKB:Q63881" FT REGION 506..531 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 601..634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 372..377 FT /note="Selectivity filter" FT /evidence="ECO:0000250|UniProtKB:P63142" FT COMPBIAS 506..524 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 104 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q63881" FT BINDING 131 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q63881" FT BINDING 132 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000250|UniProtKB:Q63881" FT MOD_RES 458 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q03719" FT MOD_RES 555 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q62897" FT CARBOHYD 352 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 355 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 1..377 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057040" FT CONFLICT 358 FT /note="S -> N (in Ref. 2; BAA96454)" FT /evidence="ECO:0000305" FT CONFLICT 406 FT /note="V -> I (in Ref. 2; BAA96454)" FT /evidence="ECO:0000305" SQ SEQUENCE 647 AA; 71330 MW; 8672C299CDB7C5AA CRC64; MAAGLATWLP FARAAAVGWL PLAQQPLPPA PGVKASRGDE VLVVNVSGRR FETWKNTLDR YPDTLLGSSE KEFFYDADSG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGDGP ALPAGSSLRQ RLWRAFENPH TSTAALVFYY VTGFFIAVSV IANVVETIPC RGSARRSSRE QPCGERFPQA FFCMDTACVL IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLL VPKNDDVSGA FVTLRVFRVF RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TNKTNFTSIP AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGGLEDSGS GEEQALCVRN RSAFEQQHHH LLHCLEKTTC HEFTDELTFS EALGAVSPGG RTSRSTSVSS QPVGPGSLLS SCCPRRAKRR AIRLANSTAS VSRGSMQELD MLAGLRRSHA PQSRSSLNAK PHDSLDLNCD SRDFVAAIIS IPTPPANTPD ESQPSSPGGG GRAGSTLRNS SLGTPCLFPE TVKISSL //