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Protein

Potassium voltage-gated channel subfamily A member 10

Gene

KCNA10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient. The channel activity is up-regulated by cAMP.1 Publication

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: GO_Central
  2. intracellular cyclic nucleotide activated cation channel activity Source: ProtInc

GO - Biological processi

  1. potassium ion transmembrane transport Source: GO_Central
  2. potassium ion transport Source: ProtInc
  3. protein homooligomerization Source: InterPro
  4. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 10
Alternative name(s):
Voltage-gated potassium channel subunit Kv1.8
Gene namesi
Name:KCNA10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6219. KCNA10.

Subcellular locationi

Membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei218 – 23821Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei271 – 29222Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei303 – 32321Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei339 – 35820Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei375 – 39521Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Transmembranei436 – 45621Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: GO_Central
  2. plasma membrane Source: Reactome
  3. voltage-gated potassium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Potassium voltage-gated channel subfamily A member 10PRO_0000308275Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
Lipidationi293 – 2931S-palmitoyl cysteineSequence Analysis
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PaxDbiQ16322.
PRIDEiQ16322.

Expressioni

Tissue specificityi

Detected in kidney, in proximal tubules, glomerular endothelium, in vascular endothelium and in smooth muscle cells.1 Publication

Gene expression databases

CleanExiHS_KCNA10.
ExpressionAtlasiQ16322. differential.
GenevestigatoriQ16322.

Organism-specific databases

HPAiCAB022564.
HPA015061.

Interactioni

Subunit structurei

Homotetramer. Interacts with KCN4B/POMP. Interaction with KCN4B/POMP is necessary for the modulation of channel activity by cAMP.1 Publication

Protein-protein interaction databases

BioGridi109946. 1 interaction.
STRINGi9606.ENSP00000358786.

Structurei

3D structure databases

SMRiQ16322. Positions 86-468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 4266Selectivity filterBy similarity

Domaini

The N-terminus may be important in determining the rate of inactivation of the channel while the tail may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.
The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiQ16322.
KOiK04881.
OMAiKQNIPGE.
OrthoDBiEOG7M0NRD.
PhylomeDBiQ16322.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

Q16322-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVCGWKEME VALVNFDNSD EIQEEPGYAT DFDSTSPKGR PGGSSFSNGK
60 70 80 90 100
ILISESTNHE TAFSKLPGDY ADPPGPEPVV LNEGNQRVII NIAGLRFETQ
110 120 130 140 150
LRTLSQFPET LLGDREKRMQ FFDSMRNEYF FDRNRPSFDG ILYYYQSGGK
160 170 180 190 200
IRRPANVPID IFADEISFYE LGSEAMDQFR EDEGFIKDPE TLLPTNDIHR
210 220 230 240 250
QFWLLFEYPE SSSAARAVAV VSVLVVVISI TIFCLETLPE FREDRELKVV
260 270 280 290 300
RDPNLNMSKT VLSQTMFTDP FFMVESTCIV WFTFELVLRF VVCPSKTDFF
310 320 330 340 350
RNIMNIIDII SIIPYFATLI TELVQETEPS AQQNMSLAIL RIIRLVRVFR
360 370 380 390 400
IFKLSRHSKG LQILGQTLKA SMRELGLLIF FLFIGVILFS SAVYFAEVDE
410 420 430 440 450
PESHFSSIPD GFWWAVVTMT TVGYGDMCPT TPGGKIVGTL CAIAGVLTIA
460 470 480 490 500
LPVPVIVSNF NYFYHRETEN EEKQNIPGEI ERILNSVGSR MGSTDSLNKT
510
NGGCSTEKSR K
Length:511
Mass (Da):57,785
Last modified:November 1, 1998 - v2
Checksum:i1B09B1CD68745F29
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti200 – 2001R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036778
Natural varianti220 – 2201V → M.
Corresponds to variant rs34970857 [ dbSNP | Ensembl ].
VAR_036779
Natural varianti258 – 2581S → N.
Corresponds to variant rs3748729 [ dbSNP | Ensembl ].
VAR_036780

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96110 Genomic DNA. Translation: AAC51333.1.
AL358215 Genomic DNA. Translation: CAH74103.1.
CH471122 Genomic DNA. Translation: EAW56454.1.
BC074990 mRNA. Translation: AAH74990.1.
CCDSiCCDS826.1.
RefSeqiNP_005540.1. NM_005549.2.
UniGeneiHs.248140.
Hs.622910.

Genome annotation databases

EnsembliENST00000369771; ENSP00000358786; ENSG00000143105.
GeneIDi3744.
KEGGihsa:3744.
UCSCiuc001dzt.1. human.

Polymorphism databases

DMDMi74739879.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U96110 Genomic DNA. Translation: AAC51333.1.
AL358215 Genomic DNA. Translation: CAH74103.1.
CH471122 Genomic DNA. Translation: EAW56454.1.
BC074990 mRNA. Translation: AAH74990.1.
CCDSiCCDS826.1.
RefSeqiNP_005540.1. NM_005549.2.
UniGeneiHs.248140.
Hs.622910.

3D structure databases

SMRiQ16322. Positions 86-468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109946. 1 interaction.
STRINGi9606.ENSP00000358786.

Chemistry

ChEMBLiCHEMBL2362996.
DrugBankiDB06637. Dalfampridine.
GuidetoPHARMACOLOGYi545.

Polymorphism databases

DMDMi74739879.

Proteomic databases

PaxDbiQ16322.
PRIDEiQ16322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369771; ENSP00000358786; ENSG00000143105.
GeneIDi3744.
KEGGihsa:3744.
UCSCiuc001dzt.1. human.

Organism-specific databases

CTDi3744.
GeneCardsiGC01M111059.
H-InvDBHIX0200074.
HGNCiHGNC:6219. KCNA10.
HPAiCAB022564.
HPA015061.
MIMi602420. gene.
neXtProtiNX_Q16322.
PharmGKBiPA30020.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiQ16322.
KOiK04881.
OMAiKQNIPGE.
OrthoDBiEOG7M0NRD.
PhylomeDBiQ16322.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

GeneWikiiKCNA10.
GenomeRNAii3744.
NextBioi14651.
PROiQ16322.
SOURCEiSearch...

Gene expression databases

CleanExiHS_KCNA10.
ExpressionAtlasiQ16322. differential.
GenevestigatoriQ16322.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003972. K_chnl_volt-dep_Kv1.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic localization of the human gene for KCNA10, a cGMP-activated K channel."
    Orias M., Bray-Ward P., Curran M.E., Keating M.T., Desir G.V.
    Genomics 42:33-37(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  5. "KCNA10: a novel ion channel functionally related to both voltage-gated potassium and CNG cation channels."
    Lang R., Lee G., Liu W., Tian S., Rafi H., Orias M., Segal A.S., Desir G.V.
    Am. J. Physiol. 278:F1013-F1021(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Regulation of the voltage-gated K+ channel KCNA10 by KCNA4B, a novel beta-subunit."
    Tian S., Liu W., Wu Y., Rafi H., Segal A.S., Desir G.V.
    Am. J. Physiol. 283:F142-F149(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POMP, REGULATION BY CAMP.
  7. "Expression of KCNA10, a voltage-gated K channel, in glomerular endothelium and at the apical membrane of the renal proximal tubule."
    Yao X., Tian S., Chan H.-Y., Biemesderfer D., Desir G.V.
    J. Am. Soc. Nephrol. 13:2831-2839(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-200.

Entry informationi

Entry nameiKCA10_HUMAN
AccessioniPrimary (citable) accession number: Q16322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: November 1, 1998
Last modified: April 1, 2015
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.