ID   KCNV1_HUMAN             Reviewed;         500 AA.
AC   Q6PIU1; Q9UHJ4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   10-JUN-2026, entry version 169.
DE   RecName: Full=Potassium voltage-gated channel subfamily V member 1;
DE   AltName: Full=Neuronal potassium channel alpha subunit HNKA;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv8.1;
GN   Name=KCNV1;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH KCNB1; KCNB2; KCNC4 AND KCND1.
RX   PubMed=8670833; DOI=10.1002/j.1460-2075.1996.tb00697.x;
RA   Hugnot J.-P., Salinas M., Lesage F., Guillemare E., de Weille J.,
RA   Heurteaux C., Mattei M.-G., Lazdunski M.;
RT   "Kv8.1, a new neuronal potassium channel subunit with specific inhibitory
RT   properties towards Shab and Shaw channels.";
RL   EMBO J. 15:3322-3331(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   PubMed=12383276; DOI=10.1046/j.1528-1157.43.s.9.7.x;
RA   Sano A., Mikami M., Nakamura M., Ueno S., Tanabe H., Kaneko S.;
RT   "Positional candidate approach for the gene responsible for benign adult
RT   familial myoclonic epilepsy.";
RL   Epilepsia 43:26-31(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Xia J.-H., Zheng D., Tang X.-X., Yu K.-P., Tan S.;
RT   "Molecular cloning of human neuronal potassium channel alpha subunit
RT   (HNKA).";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-22.
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCNB1 AND KCNB2.
RX   PubMed=9079713; DOI=10.1074/jbc.272.13.8774;
RA   Salinas M., de Weille J., Guillemare E., Lazdunski M., Hugnot J.-P.;
RT   "Modes of regulation of shab K+ channel activity by the Kv8.1 subunit.";
RL   J. Biol. Chem. 272:8774-8780(1997).
CC   -!- FUNCTION: Potassium channel subunit that does not form functional
CC       channels by itself. Modulates KCNB1 and KCNB2 channel activity by
CC       shifting the threshold for inactivation to more negative values and by
CC       slowing the rate of inactivation. Can down-regulate the channel
CC       activity of KCNB1, KCNB2, KCNC4 and KCND1, possibly by trapping them in
CC       intracellular membranes. {ECO:0000269|PubMed:8670833,
CC       ECO:0000269|PubMed:9079713}.
CC   -!- SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Interacts with KCNC4 and
CC       KCND1. {ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:9079713}.
CC   -!- INTERACTION:
CC       Q6PIU1; Q02410: APBA1; NbExp=2; IntAct=EBI-11667684, EBI-368690;
CC       Q6PIU1; Q99767: APBA2; NbExp=2; IntAct=EBI-11667684, EBI-81711;
CC       Q6PIU1; Q92796: DLG3; NbExp=3; IntAct=EBI-11667684, EBI-80440;
CC       Q6PIU1; P78352: DLG4; NbExp=3; IntAct=EBI-11667684, EBI-80389;
CC       Q6PIU1; Q68DX3: FRMPD2; NbExp=3; IntAct=EBI-11667684, EBI-53993476;
CC       Q6PIU1; A4D2P6: GRID2IP; NbExp=2; IntAct=EBI-11667684, EBI-15893226;
CC       Q6PIU1; Q9Y3R0: GRIP1; NbExp=5; IntAct=EBI-11667684, EBI-5349621;
CC       Q6PIU1; Q9C0E4: GRIP2; NbExp=5; IntAct=EBI-11667684, EBI-949557;
CC       Q6PIU1; Q14005: IL16; NbExp=3; IntAct=EBI-11667684, EBI-2831580;
CC       Q6PIU1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11667684, EBI-739832;
CC       Q6PIU1; Q96QZ7: MAGI1; NbExp=2; IntAct=EBI-11667684, EBI-924464;
CC       Q6PIU1; Q86UL8: MAGI2; NbExp=5; IntAct=EBI-11667684, EBI-311035;
CC       Q6PIU1; O75970: MPDZ; NbExp=3; IntAct=EBI-11667684, EBI-821405;
CC       Q6PIU1; Q86UT5: NHERF4; NbExp=2; IntAct=EBI-11667684, EBI-8744528;
CC       Q6PIU1; Q8NI35: PATJ; NbExp=8; IntAct=EBI-11667684, EBI-724390;
CC       Q6PIU1; Q5T2W1: PDZK1; NbExp=3; IntAct=EBI-11667684, EBI-349819;
CC       Q6PIU1; Q14160: SCRIB; NbExp=3; IntAct=EBI-11667684, EBI-357345;
CC       Q6PIU1; Q07157: TJP1; NbExp=2; IntAct=EBI-11667684, EBI-79553;
CC       Q6PIU1; Q9P202: WHRN; NbExp=3; IntAct=EBI-11667684, EBI-310886;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8670833,
CC       ECO:0000269|PubMed:9079713}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:9079713}. Note=Has to
CC       be associated with another potassium channel subunit to get inserted in
CC       the plasma membrane. Remains intracellular in the absence of KCNB2.
CC   -!- TISSUE SPECIFICITY: Detected in brain. {ECO:0000269|PubMed:12383276}.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at every
CC       third position. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. V (TC 1.A.1.2)
CC       subfamily. Kv8.1/KCNV1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AB032013; BAA92316.1; -; Genomic_DNA.
DR   EMBL; AF167082; AAD48031.2; -; mRNA.
DR   EMBL; BC028739; AAH28739.1; -; mRNA.
DR   CCDS; CCDS6314.1; -.
DR   RefSeq; NP_055194.1; NM_014379.4.
DR   AlphaFoldDB; Q6PIU1; -.
DR   SMR; Q6PIU1; -.
DR   BioGRID; 117954; 36.
DR   CORUM; Q6PIU1; -.
DR   FunCoup; Q6PIU1; 32.
DR   IntAct; Q6PIU1; 86.
DR   MINT; Q6PIU1; -.
DR   STRING; 9606.ENSP00000435954; -.
DR   ChEMBL; CHEMBL2362996; -.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB01110; Miconazole.
DR   DrugBank; DB01069; Promethazine.
DR   DrugCentral; Q6PIU1; -.
DR   PhosphoSitePlus; Q6PIU1; -.
DR   BioMuta; KCNV1; -.
DR   DMDM; 160013825; -.
DR   jPOST; Q6PIU1; -.
DR   MassIVE; Q6PIU1; -.
DR   PaxDb; 9606-ENSP00000435954; -.
DR   PeptideAtlas; Q6PIU1; -.
DR   ProteomicsDB; 67176; -.
DR   Antibodypedia; 26632; 128 antibodies from 20 providers.
DR   DNASU; 27012; -.
DR   Ensembl; ENST00000297404.1; ENSP00000297404.1; ENSG00000164794.9.
DR   Ensembl; ENST00000524391.6; ENSP00000435954.1; ENSG00000164794.9.
DR   GeneID; 27012; -.
DR   KEGG; hsa:27012; -.
DR   MANE-Select; ENST00000524391.6; ENSP00000435954.1; NM_014379.4; NP_055194.1.
DR   UCSC; uc003ynr.5; human.
DR   AGR; HGNC:18861; -.
DR   ClinPGx; PA38721; -.
DR   CTD; 27012; -.
DR   DisGeNET; 27012; -.
DR   GeneCards; KCNV1; -.
DR   HGNC; HGNC:18861; KCNV1.
DR   HPA; ENSG00000164794; Tissue enriched (brain).
DR   MIM; 608164; gene.
DR   OpenTargets; ENSG00000164794; -.
DR   VEuPathDB; HostDB:ENSG00000164794; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000159740; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; Q6PIU1; -.
DR   OMA; SGGDEFW; -.
DR   OrthoDB; 296522at2759; -.
DR   PAN-GO; Q6PIU1; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6PIU1; -.
DR   PathwayCommons; Q6PIU1; -.
DR   Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR   SignaLink; Q6PIU1; -.
DR   Agora; ENSG00000164794; -.
DR   BioGRID-ORCS; 27012; 4 hits in 1141 CRISPR screens.
DR   ChiTaRS; KCNV1; human.
DR   GeneWiki; KCNV1; -.
DR   GenomeRNAi; 27012; -.
DR   Pharos; Q6PIU1; Tclin.
DR   PRO; PR:Q6PIU1; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q6PIU1; protein.
DR   Bgee; ENSG00000164794; Expressed in buccal mucosa cell and 47 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR   GO; GO:0008200; F:ion channel inhibitor activity; TAS:ProtInc.
DR   GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
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:0006813; P:potassium ion transport; TAS:ProtInc.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   FunFam; 1.10.287.70:FF:000005; potassium voltage-gated channel subfamily G member 1; 1.
DR   FunFam; 1.20.120.350:FF:000044; Potassium voltage-gated channel subfamily V member 1; 1.
DR   FunFam; 3.30.710.10:FF:000067; Potassium voltage-gated channel subfamily V member 1; 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; IPR003970; K_chnl_volt-dep_Kv8.1.
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:SF38; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY V MEMBER 1; 1.
DR   PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01493; KV8CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
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   Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Proteomics identification;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN           1..500
FT                   /note="Potassium voltage-gated channel subfamily V member
FT                   1"
FT                   /id="PRO_0000308350"
FT   TOPO_DOM        1..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..238
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        260..276
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        310..331
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        332..345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..500
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          168..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           392..397
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        168..181
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         22
FT                   /note="D -> G (in dbSNP:rs17852611)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_036804"
SQ   SEQUENCE   500 AA;  56304 MW;  C229E21ABC869C73 CRC64;
     MPSSGRALLD SPLDSGSLTS LDSSVFCSEG EGEPLALGDC FTVNVGGSRF VLSQQALSCF
     PHTRLGKLAV VVASYRRPGA LAAVPSPLEL CDDANPVDNE YFFDRSSQAF RYVLHYYRTG
     RLHVMEQLCA LSFLQEIQYW GIDELSIDSC CRDRYFRRKE LSETLDFKKD TEDQESQHES
     EQDFSQGPCP TVRQKLWNIL EKPGSSTAAR IFGVISIIFV VVSIINMALM SAELSWLDLQ
     LLEILEYVCI SWFTGEFVLR FLCVRDRCRF LRKVPNIIDL LAILPFYITL LVESLSGSQT
     TQELENVGRI VQVLRLLRAL RMLKLGRHST GLRSLGMTIT QCYEEVGLLL LFLSVGISIF
     STVEYFAEQS IPDTTFTSVP CAWWWATTSM TTVGYGDIRP DTTTGKIVAF MCILSGILVL
     ALPIAIINDR FSACYFTLKL KEAAVRQREA LKKLTKNIAT DSYISVNLRD VYARSIMEML
     RLKGRERAST RSSGGDDFWF
//