KCA10_HUMAN
ID KCA10_HUMAN Reviewed; 511 AA.
AC Q16322;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 10;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.8;
GN Name=KCNA10;
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].
RX PubMed=9177773; DOI=10.1006/geno.1997.4712;
RA Orias M., Bray-Ward P., Curran M.E., Keating M.T., Desir G.V.;
RT "Genomic localization of the human gene for KCNA10, a cGMP-activated K
RT channel.";
RL Genomics 42:33-37(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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].
RC TISSUE=Lung;
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, AND SUBCELLULAR LOCATION.
RX PubMed=10836990; DOI=10.1152/ajprenal.2000.278.6.f1013;
RA Lang R., Lee G., Liu W., Tian S., Rafi H., Orias M., Segal A.S.,
RA Desir G.V.;
RT "KCNA10: a novel ion channel functionally related to both voltage-gated
RT potassium and CNG cation channels.";
RL Am. J. Physiol. 278:F1013-F1021(2000).
RN [6]
RP INTERACTION WITH POMP, AND REGULATION BY CAMP.
RX PubMed=12060596; DOI=10.1152/ajprenal.00258.2001;
RA Tian S., Liu W., Wu Y., Rafi H., Segal A.S., Desir G.V.;
RT "Regulation of the voltage-gated K+ channel KCNA10 by KCNA4B, a novel beta-
RT subunit.";
RL Am. J. Physiol. 283:F142-F149(2002).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=12444201; DOI=10.1097/01.asn.0000036866.37886.c5;
RA Yao X., Tian S., Chan H.-Y., Biemesderfer D., Desir G.V.;
RT "Expression of KCNA10, a voltage-gated K channel, in glomerular endothelium
RT and at the apical membrane of the renal proximal tubule.";
RL J. Am. Soc. Nephrol. 13:2831-2839(2002).
RN [8]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-200.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Mediates voltage-dependent potassium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a potassium-selective channel through which potassium ions may
CC pass in accordance with their electrochemical gradient. The channel
CC activity is up-regulated by cAMP. {ECO:0000269|PubMed:10836990}.
CC -!- SUBUNIT: Homotetramer. Interacts with KCN4B/POMP. Interaction with
CC KCN4B/POMP is necessary for the modulation of channel activity by cAMP.
CC {ECO:0000269|PubMed:12060596}.
CC -!- INTERACTION:
CC Q16322; Q9UPQ8: DOLK; NbExp=5; IntAct=EBI-12265328, EBI-8645574;
CC Q16322; Q09470: KCNA1; NbExp=3; IntAct=EBI-12265328, EBI-8286599;
CC Q16322; P21145: MAL; NbExp=3; IntAct=EBI-12265328, EBI-3932027;
CC Q16322; O43765: SGTA; NbExp=3; IntAct=EBI-12265328, EBI-347996;
CC Q16322; P55061: TMBIM6; NbExp=3; IntAct=EBI-12265328, EBI-1045825;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10836990}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:10836990}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, in proximal tubules, glomerular
CC endothelium, in vascular endothelium and in smooth muscle cells.
CC {ECO:0000269|PubMed:12444201}.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments.
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.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.8/KCNA10 sub-subfamily. {ECO:0000305}.
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DR EMBL; U96110; AAC51333.1; -; Genomic_DNA.
DR EMBL; AL358215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471122; EAW56454.1; -; Genomic_DNA.
DR EMBL; BC074990; AAH74990.1; -; mRNA.
DR CCDS; CCDS826.1; -.
DR RefSeq; NP_005540.1; NM_005549.2.
DR AlphaFoldDB; Q16322; -.
DR SMR; Q16322; -.
DR BioGRID; 109946; 23.
DR IntAct; Q16322; 21.
DR STRING; 9606.ENSP00000358786; -.
DR ChEMBL; CHEMBL2363001; -.
DR DrugBank; DB06637; Dalfampridine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q16322; -.
DR GuidetoPHARMACOLOGY; 545; -.
DR GlyGen; Q16322; 3 sites.
DR iPTMnet; Q16322; -.
DR PhosphoSitePlus; Q16322; -.
DR BioMuta; KCNA10; -.
DR DMDM; 74739879; -.
DR EPD; Q16322; -.
DR jPOST; Q16322; -.
DR MassIVE; Q16322; -.
DR MaxQB; Q16322; -.
DR PaxDb; Q16322; -.
DR PeptideAtlas; Q16322; -.
DR PRIDE; Q16322; -.
DR ProteomicsDB; 60854; -.
DR Antibodypedia; 20099; 88 antibodies from 22 providers.
DR DNASU; 3744; -.
DR Ensembl; ENST00000369771.4; ENSP00000358786.2; ENSG00000143105.7.
DR GeneID; 3744; -.
DR KEGG; hsa:3744; -.
DR MANE-Select; ENST00000369771.4; ENSP00000358786.2; NM_005549.2; NP_005540.1.
DR UCSC; uc001dzt.2; human.
DR CTD; 3744; -.
DR DisGeNET; 3744; -.
DR GeneCards; KCNA10; -.
DR HGNC; HGNC:6219; KCNA10.
DR HPA; ENSG00000143105; Not detected.
DR MIM; 602420; gene.
DR neXtProt; NX_Q16322; -.
DR OpenTargets; ENSG00000143105; -.
DR PharmGKB; PA30020; -.
DR VEuPathDB; HostDB:ENSG00000143105; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000159534; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; Q16322; -.
DR OMA; TACIAWF; -.
DR OrthoDB; 80538at2759; -.
DR PhylomeDB; Q16322; -.
DR TreeFam; TF313103; -.
DR PathwayCommons; Q16322; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; Q16322; -.
DR BioGRID-ORCS; 3744; 108 hits in 1061 CRISPR screens.
DR GeneWiki; KCNA10; -.
DR GenomeRNAi; 3744; -.
DR Pharos; Q16322; Tclin.
DR PRO; PR:Q16322; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q16322; protein.
DR Bgee; ENSG00000143105; Expressed in stomach and 3 other tissues.
DR Genevisible; Q16322; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005221; F:intracellular cyclic nucleotide activated cation channel activity; TAS:ProtInc.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
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; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..511
FT /note="Potassium voltage-gated channel subfamily A member
FT 10"
FT /id="PRO_0000308275"
FT TRANSMEM 218..238
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..292
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..358
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 22..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..426
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 489..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 293
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 498
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 200
FT /note="R -> H (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs755748044)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036778"
FT VARIANT 220
FT /note="V -> M (in dbSNP:rs34970857)"
FT /id="VAR_036779"
FT VARIANT 258
FT /note="S -> N (in dbSNP:rs3748729)"
FT /id="VAR_036780"
SQ SEQUENCE 511 AA; 57785 MW; 1B09B1CD68745F29 CRC64;
MDVCGWKEME VALVNFDNSD EIQEEPGYAT DFDSTSPKGR PGGSSFSNGK ILISESTNHE
TAFSKLPGDY ADPPGPEPVV LNEGNQRVII NIAGLRFETQ LRTLSQFPET LLGDREKRMQ
FFDSMRNEYF FDRNRPSFDG ILYYYQSGGK IRRPANVPID IFADEISFYE LGSEAMDQFR
EDEGFIKDPE TLLPTNDIHR QFWLLFEYPE SSSAARAVAV VSVLVVVISI TIFCLETLPE
FREDRELKVV RDPNLNMSKT VLSQTMFTDP FFMVESTCIV WFTFELVLRF VVCPSKTDFF
RNIMNIIDII SIIPYFATLI TELVQETEPS AQQNMSLAIL RIIRLVRVFR IFKLSRHSKG
LQILGQTLKA SMRELGLLIF FLFIGVILFS SAVYFAEVDE PESHFSSIPD GFWWAVVTMT
TVGYGDMCPT TPGGKIVGTL CAIAGVLTIA LPVPVIVSNF NYFYHRETEN EEKQNIPGEI
ERILNSVGSR MGSTDSLNKT NGGCSTEKSR K
