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Potassium voltage-gated channel subfamily A member 4 (HPCN2) (Voltage-gated K( ) channel HuKII) (Voltage-gated potassium channel HBK4) (Voltage-gated potassium channel HK1) (Voltage-gated potassium channel subunit Kv1.4)

 KCNA4_HUMAN             Reviewed;         653 AA.
P22459;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
30-NOV-2010, sequence version 2.
18-JUL-2018, entry version 172.
RecName: Full=Potassium voltage-gated channel subfamily A member 4;
AltName: Full=HPCN2;
AltName: Full=Voltage-gated K(+) channel HuKII {ECO:0000303|PubMed:19912772};
AltName: Full=Voltage-gated potassium channel HBK4;
AltName: Full=Voltage-gated potassium channel HK1 {ECO:0000303|PubMed:2001794};
AltName: Full=Voltage-gated potassium channel subunit Kv1.4;
Name=KCNA4; Synonyms=KCNA4L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Skeletal muscle;
PubMed=2263489; DOI=10.1093/nar/18.23.7160;
Philipson L.H., Schaefer K., Lamendola J., Bell G.I., Steiner D.F.;
"Sequence of a human fetal skeletal muscle potassium channel cDNA
related to RCK4.";
Nucleic Acids Res. 18:7160-7160(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Heart;
PubMed=2001794;
Tamkun M.M., Knoth K.M., Walbridge J.A., Kroemer H., Roden D.M.,
Glover D.M.;
"Molecular cloning and characterization of two voltage-gated K+
channel cDNAs from human ventricle.";
FASEB J. 5:331-337(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
TISSUE=Brain;
PubMed=19912772; DOI=10.1016/1044-7431(90)90004-N;
Ramaswami M., Gautam M., Kamb A., Rudy B., Tanouye M.A., Mathew M.K.;
"Human potassium channel genes: molecular cloning and functional
expression.";
Mol. Cell. Neurosci. 1:214-223(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=8495559; DOI=10.1161/01.RES.72.6.1326;
Po S., Roberds S., Snyders D.J., Tamkun M.M., Bennett P.B.;
"Heteromultimeric assembly of human potassium channels. Molecular
basis of a transient outward current?";
Circ. Res. 72:1326-1336(1993).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=17156368; DOI=10.1111/j.1460-9568.2006.05186.x;
Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.;
"Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast
inactivation properties of the human potassium channels Kv1.4-
1.1/Kvbeta1.1 and Kv1.4-1.1/Kvbeta1.2.";
Eur. J. Neurosci. 24:3073-3083(2006).
[7]
INTERACTION WITH KCNRG, AND SUBCELLULAR LOCATION.
PubMed=19968958; DOI=10.1016/j.bbrc.2009.11.143;
Usman H., Mathew M.K.;
"Potassium channel regulator KCNRG regulates surface expression of
Shaker-type potassium channels.";
Biochem. Biophys. Res. Commun. 391:1301-1305(2010).
[8]
STRUCTURE BY NMR OF 1-37.
PubMed=9000078; DOI=10.1038/385272a0;
Antz C., Geyer M., Fakler B., Schott M.K., Guy H.R., Frank R.,
Ruppersberg J.P., Kalbitzer H.R.;
"NMR structure of inactivation gates from mammalian voltage-dependent
potassium channels.";
Nature 385:272-275(1997).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes. Forms
tetrameric potassium-selective channels through which potassium
ions pass in accordance with their electrochemical gradient. The
channel alternates between opened and closed conformations in
response to the voltage difference across the membrane
(PubMed:19912772, PubMed:8495559). Can form functional
homotetrameric channels and heterotetrameric channels that contain
variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly
other family members as well; channel properties depend on the
type of alpha subunits that are part of the channel
(PubMed:8495559). Channel properties are modulated by cytoplasmic
beta subunits that regulate the subcellular location of the alpha
subunits and promote rapid inactivation. In vivo, membranes
probably contain a mixture of heteromeric potassium channel
complexes, making it difficult to assign currents observed in
intact tissues to any particular potassium channel family member.
Homotetrameric KCNA4 forms a potassium channel that opens in
response to membrane depolarization, followed by rapid spontaneous
channel closure (PubMed:19912772, PubMed:8495559). Likewise, a
heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid
inactivation (PubMed:17156368). {ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:8495559}.
-!- ENZYME REGULATION: Inhibited by 4-aminopyridine (4-AP), but not by
tetraethylammonium (TEA) and charybdotoxin (CTX).
{ECO:0000269|PubMed:19912772}.
-!- SUBUNIT: Homotetramer and heterotetramer of potassium channel
proteins (By similarity). Interacts with KCNAB1 and KCNAB2 (By
similarity). Binds PDZ domains of DLG1, DLG2 and DLG4 (By
similarity). Interacts with SIGMAR1 (By similarity). Detected in a
complex with KCNA1 (By similarity). Interacts with KCNA2 (By
similarity). Part of a complex containing KCNA1, KCNAB1 and LGI1
(By similarity). Interacts (via cytoplasmic N-terminal domain)
with KCNRG (PubMed:19968958). {ECO:0000250|UniProtKB:P15385}.
-!- INTERACTION:
P35609:ACTN2; NbExp=2; IntAct=EBI-631235, EBI-77797;
Q62936:Dlg3 (xeno); NbExp=4; IntAct=EBI-631235, EBI-349596;
P78352:DLG4; NbExp=2; IntAct=EBI-631235, EBI-80389;
P31016:Dlg4 (xeno); NbExp=3; IntAct=EBI-631235, EBI-375655;
P21673:SAT1; NbExp=3; IntAct=EBI-631235, EBI-711613;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:19968958,
ECO:0000269|PubMed:8495559}; Multi-pass membrane protein
{ECO:0000255}. Cell projection, axon
{ECO:0000250|UniProtKB:P15385}.
-!- TISSUE SPECIFICITY: Detected in heart ventricle.
{ECO:0000269|PubMed:2001794}.
-!- DOMAIN: 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. {ECO:0000250|UniProtKB:Q28527}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
(TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M55514; AAA60034.1; -; mRNA.
EMBL; M60450; AAA61275.1; -; mRNA.
EMBL; L02751; AAA36140.1; -; mRNA.
EMBL; AC124657; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS41629.1; -.
PIR; A39922; A39922.
RefSeq; NP_002224.1; NM_002233.3.
UniGene; Hs.592002; -.
ProteinModelPortal; P22459; -.
SMR; P22459; -.
BioGrid; 109942; 18.
IntAct; P22459; 7.
MINT; P22459; -.
STRING; 9606.ENSP00000328511; -.
BindingDB; P22459; -.
ChEMBL; CHEMBL4205; -.
DrugBank; DB02299; Arginineamide.
DrugBank; DB06637; Dalfampridine.
iPTMnet; P22459; -.
PhosphoSitePlus; P22459; -.
BioMuta; KCNA4; -.
DMDM; 313104127; -.
PaxDb; P22459; -.
PeptideAtlas; P22459; -.
PRIDE; P22459; -.
ProteomicsDB; 53992; -.
DNASU; 3739; -.
Ensembl; ENST00000328224; ENSP00000328511; ENSG00000182255.
GeneID; 3739; -.
KEGG; hsa:3739; -.
UCSC; uc001msk.4; human.
CTD; 3739; -.
DisGeNET; 3739; -.
EuPathDB; HostDB:ENSG00000182255.6; -.
GeneCards; KCNA4; -.
H-InvDB; HIX0036152; -.
HGNC; HGNC:6222; KCNA4.
HPA; CAB001977; -.
HPA; HPA016422; -.
MIM; 176266; gene.
neXtProt; NX_P22459; -.
OpenTargets; ENSG00000182255; -.
PharmGKB; PA207; -.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
InParanoid; P22459; -.
KO; K04877; -.
OMA; RQRPEKK; -.
OrthoDB; EOG091G10NU; -.
PhylomeDB; P22459; -.
TreeFam; TF313103; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
GeneWiki; KCNA4; -.
GenomeRNAi; 3739; -.
PRO; PR:P22459; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000182255; -.
CleanEx; HS_KCNA4; -.
Genevisible; P22459; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008076; C:voltage-gated potassium channel complex; IMP:UniProtKB.
GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 1.20.120.350; -; 1.
Gene3D; 1.20.5.600; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR020467; K_chnl_volt-dep_Kv1.4.
InterPro; IPR012897; K_chnl_volt-dep_Kv1.4_TID.
InterPro; IPR037065; K_chnl_volt-dep_Kv1.4_TID_sf.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF07941; K_channel_TID; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01511; KV14CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome; Glycoprotein;
Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 653 Potassium voltage-gated channel subfamily
A member 4.
/FTId=PRO_0000053981.
TOPO_DOM 1 304 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 305 326 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 327 370 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 371 392 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 393 403 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 404 424 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 425 439 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 440 460 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 461 475 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 476 497 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 498 511 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 512 523 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 524 531 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 532 538 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 539 567 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 568 653 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 462 475 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 524 529 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 651 653 PDZ-binding. {ECO:0000250}.
COMPBIAS 62 65 Poly-His.
COMPBIAS 123 137 Poly-Glu.
COMPBIAS 162 165 Poly-Gly.
COMPBIAS 433 436 Poly-Gln.
MOD_RES 90 90 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:Q61423}.
MOD_RES 599 599 Phosphoserine; by PKA. {ECO:0000255}.
CARBOHYD 352 352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 38 38 A -> R (in Ref. 1; AAA60034).
{ECO:0000305}.
CONFLICT 42 42 A -> R (in Ref. 1; AAA60034).
{ECO:0000305}.
CONFLICT 84 88 RRRRQ -> EEEAT (in Ref. 1; AAA60034).
{ECO:0000305}.
CONFLICT 304 304 S -> D (in Ref. 1; AAA60034).
{ECO:0000305}.
CONFLICT 542 542 S -> V (in Ref. 1; AAA60034).
{ECO:0000305}.
CONFLICT 631 631 G -> A (in Ref. 1; AAA60034).
{ECO:0000305}.
SEQUENCE 653 AA; 73257 MW; 5E511DB704CCA013 CRC64;
MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGSGGSGGG
SHHHHQSRGA CTSHDPQSSR GSRRRRRQRS EKKKAHYRQS SFPHCSDLMP SGSEEKILRE
LSEEEEDEEE EEEEEEEGRF YYSEDDHGDE CSYTDLLPQD EGGGGYSSVR YSDCCERVVI
NVSGLRFETQ MKTLAQFPET LLGDPEKRTQ YFDPLRNEYF FDRNRPSFDA ILYYYQSGGR
LKRPVNVPFD IFTEEVKFYQ LGEEALLKFR EDEGFVREEE DRALPENEFK KQIWLLFEYP
ESSSPARGIA IVSVLVILIS IVIFCLETLP EFRDDRDLVM ALSAGGHGGL LNDTSAPHLE
NSGHTIFNDP FFIVETVCIV WFSFEFVVRC FACPSQALFF KNIMNIIDIV SILPYFITLG
TDLAQQQGGG NGQQQQAMSF AILRIIRLVR VFRIFKLSRH SKGLQILGHT LRASMRELGL
LIFFLFIGVI LFSSAVYFAE ADEPTTHFQS IPDAFWWAVV TMTTVGYGDM KPITVGGKIV
GSLCAIAGVL TIALPVPVIV SNFNYFYHRE TENEEQTQLT QNAVSCPYLP SNLLKKFRSS
TSSSLGDKSE YLEMEEGVKE SLCAKEEKCQ GKGDDSETDK NNCSNAKAVE TDV


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