Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Potassium voltage-gated channel subfamily A member 4

Gene

Kcna4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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:8020965). 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 (By similarity). 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:8020965). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (By similarity).By similarity1 Publication

GO - Molecular functioni

  1. potassium ion binding Source: InterPro
  2. voltage-gated potassium channel activity Source: UniProtKB

GO - Biological processi

  1. potassium ion transmembrane transport Source: UniProtKB
  2. protein homooligomerization Source: InterPro
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_287159. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 4
Alternative name(s):
Voltage-gated potassium channel subunit Kv1.4
Gene namesi
Name:Kcna4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:96661. Kcna4.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein Curated. Cell projectionaxon By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 305305CytoplasmicBy similarityAdd
BLAST
Transmembranei306 – 32722Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini328 – 37144ExtracellularBy similarityAdd
BLAST
Transmembranei372 – 39322Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini394 – 40411CytoplasmicBy similarityAdd
BLAST
Transmembranei405 – 42521Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini426 – 44015ExtracellularBy similarityAdd
BLAST
Transmembranei441 – 46121Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini462 – 47615CytoplasmicBy similarityAdd
BLAST
Transmembranei477 – 49822Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini499 – 51214ExtracellularBy similarityAdd
BLAST
Intramembranei513 – 52412Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei525 – 5328By similarity
Topological domaini533 – 5397ExtracellularBy similarity
Transmembranei540 – 56829Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini569 – 65486CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  1. axon Source: UniProtKB
  2. integral component of membrane Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
  4. membrane Source: MGI
  5. voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 654654Potassium voltage-gated channel subfamily A member 4PRO_0000053982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi353 – 3531N-linked (GlcNAc...)Sequence Analysis
Modified residuei600 – 6001Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ61423.
PRIDEiQ61423.

PTM databases

PhosphoSiteiQ61423.

Expressioni

Gene expression databases

BgeeiQ61423.
GenevestigatoriQ61423.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi200879. 1 interaction.
IntActiQ61423. 1 interaction.
MINTiMINT-1780501.
STRINGi10090.ENSMUSP00000106689.

Structurei

3D structure databases

ProteinModelPortaliQ61423.
SMRiQ61423. Positions 1-75, 176-572.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni463 – 47614S4-S5 linkerBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi525 – 5306Selectivity filterBy similarity
Motifi652 – 6543PDZ-bindingBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi38 – 5013Poly-AlaAdd
BLAST
Compositional biasi62 – 654Poly-His
Compositional biasi83 – 897Poly-Arg
Compositional biasi123 – 13715Poly-GluAdd
BLAST
Compositional biasi162 – 1665Poly-Gly
Compositional biasi434 – 4374Poly-Gln

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.By similarity
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.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiQ61423.
KOiK04877.
OMAiKKAHHRQ.
OrthoDBiEOG7M0NRD.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
1.20.5.600. 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.
IPR020467. K_chnl_volt-dep_Kv1.4.
IPR012897. K_chnl_volt-dep_Kv1.4_TID.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF07941. K_channel_TID. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01511. KV14CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

Q61423-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA
60 70 80 90 100
VEGTGGSGGG PHHHHQTRGA YSSHDPQGSR GSRRRRRQRT EKKKLHHRQS
110 120 130 140 150
SFPHCSDLMP SGSEEKILRE LSEEEEDEEE EEEEEEEGRF YYSEEDHGDG
160 170 180 190 200
CSYTDLLPQD DGGGGGYSSV RYSDCCERVV INVSGLRFET QMKTLAQFPE
210 220 230 240 250
TLLGDPEKRT QYFDPLRNEY FFDRNRPSFD AILYYYQSGG RLKRPVNVPF
260 270 280 290 300
DIFTEEVKFY QLGEEALLKF REDEGFVREE EDRALPENEF KKQIWLLFEY
310 320 330 340 350
PESSSPARGI AIVSVLVILI SIVIFCLETL PEFRDDRDLI MALSAGGHSR
360 370 380 390 400
LLNDTSAPHL ENSGHTIFND PFFIVETVCI VWFSFEFVVR CFACPSQALF
410 420 430 440 450
FKNIMNIIDI VSILPYFITL GTDLAQQQGG GNGQQQQAMS FAILRIIRLV
460 470 480 490 500
RVFRIFKLSR HSKGLQILGH TLRASMRELG LLIFFLFIGV ILFSSAVYFA
510 520 530 540 550
EADEPTTHFQ SIPDAFWWAV VTMTTVGYGD MKPITVGGKI VGSLCAIAGV
560 570 580 590 600
LTIALPVPVI VSNFNYFYHR ETENEEQTQL TQNAVSCPYL PSNLLKKFRS
610 620 630 640 650
STSSSLGDKS EYLEMEEGVK ESLCGKEEKC QGKGDESETD KNNCSNAKAV

ETDV
Length:654
Mass (Da):73,470
Last modified:July 26, 2011 - v2
Checksum:i9322A3DC9CBA2AC4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601D → E in AAB60668 (PubMed:8020965).Curated
Sequence conflicti395 – 3951P → T in AAB60668 (PubMed:8020965).Curated
Sequence conflicti636 – 6361E → D in AAB60668 (PubMed:8020965).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03723 Genomic DNA. Translation: AAB60668.1.
AK036112 mRNA. Translation: BAC29309.1.
BX293548 Genomic DNA. Translation: CAM23761.1.
CH466519 Genomic DNA. Translation: EDL27774.1.
BC109014 mRNA. Translation: AAI09015.1.
CCDSiCCDS16505.1.
PIRiS09045.
RefSeqiNP_067250.2. NM_021275.4.
XP_006498875.1. XM_006498812.2.
UniGeneiMm.142718.

Genome annotation databases

EnsembliENSMUST00000037012; ENSMUSP00000037958; ENSMUSG00000042604.
GeneIDi16492.
KEGGimmu:16492.
UCSCiuc008llu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03723 Genomic DNA. Translation: AAB60668.1.
AK036112 mRNA. Translation: BAC29309.1.
BX293548 Genomic DNA. Translation: CAM23761.1.
CH466519 Genomic DNA. Translation: EDL27774.1.
BC109014 mRNA. Translation: AAI09015.1.
CCDSiCCDS16505.1.
PIRiS09045.
RefSeqiNP_067250.2. NM_021275.4.
XP_006498875.1. XM_006498812.2.
UniGeneiMm.142718.

3D structure databases

ProteinModelPortaliQ61423.
SMRiQ61423. Positions 1-75, 176-572.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200879. 1 interaction.
IntActiQ61423. 1 interaction.
MINTiMINT-1780501.
STRINGi10090.ENSMUSP00000106689.

Chemistry

GuidetoPHARMACOLOGYi541.

PTM databases

PhosphoSiteiQ61423.

Proteomic databases

PaxDbiQ61423.
PRIDEiQ61423.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037012; ENSMUSP00000037958; ENSMUSG00000042604.
GeneIDi16492.
KEGGimmu:16492.
UCSCiuc008llu.2. mouse.

Organism-specific databases

CTDi3739.
MGIiMGI:96661. Kcna4.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiQ61423.
KOiK04877.
OMAiKKAHHRQ.
OrthoDBiEOG7M0NRD.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_287159. Voltage gated Potassium channels.

Miscellaneous databases

NextBioi289795.
PROiQ61423.
SOURCEiSearch...

Gene expression databases

BgeeiQ61423.
GenevestigatoriQ61423.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
1.20.5.600. 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.
IPR020467. K_chnl_volt-dep_Kv1.4.
IPR012897. K_chnl_volt-dep_Kv1.4_TID.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF07941. K_channel_TID. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01511. KV14CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic organization, nucleotide sequence, biophysical properties, and localization of the voltage-gated K+ channel gene KCNA4/Kv1.4 to mouse chromosome 2/human 11p14 and mapping of KCNC1/Kv3.1 to mouse 7/human 11p14.3-p15.2 and KCNA1/Kv1.1 to human 12p13."
    Wymore R.S., Korenberg J.R., Kinoshita K.D., Aiyar J., Coyne C., Chen X.N., Hustad C.M., Copeland N.G., Gutman G.A., Jenkins N.A., Chandy K.G.
    Genomics 20:191-202(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: AKR.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.

Entry informationi

Entry nameiKCNA4_MOUSE
AccessioniPrimary (citable) accession number: Q61423
Secondary accession number(s): Q8CBF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 14, 1998
Last sequence update: July 26, 2011
Last modified: March 31, 2015
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.