Q61423 (KCNA4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Potassium voltage-gated channel subfamily A member 4

Alternative name(s):
Voltage-gated potassium channel subunit Kv1.4

Gene names

Name:

Kcna4

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	654 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates the 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.
Subunit structure	Heterotetramer of potassium channel proteins. Binds PDZ domains of DLG1, DLG2 and DLG4. Interacts with SIGMAR1 By similarity. Part of a complex containing KCNA1, KCNAB1 and LGI1 By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
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. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
Sequence similarities	Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane Inferred from direct assay PubMed 18603586. Source: MGI voltage-gated potassium channel complex Inferred from electronic annotation. Source: InterPro
Molecular_function	potassium ion binding Inferred from electronic annotation. Source: InterPro voltage-gated potassium channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 654	654	Potassium voltage-gated channel subfamily A member 4		PRO_0000053982
Regions
	Transmembrane	309 – 327	19	Helical; Name=Segment S1; Potential
	Transmembrane	372 – 393	22	Helical; Name=Segment S2; Potential
	Transmembrane	405 – 425	21	Helical; Name=Segment S3; Potential
	Transmembrane	444 – 462	19	Helical; Voltage-sensor; Name=Segment S4; Potential
	Transmembrane	479 – 498	20	Helical; Name=Segment S5; Potential
	Transmembrane	540 – 562	23	Helical; Name=Segment S6; Potential
	Motif	525 – 530	6	Selectivity filter By similarity
	Motif	652 – 654	3	PDZ-binding By similarity
	Compositional bias	38 – 50	13	Poly-Ala
	Compositional bias	62 – 65	4	Poly-His
	Compositional bias	83 – 89	7	Poly-Arg
	Compositional bias	123 – 137	15	Poly-Glu
	Compositional bias	162 – 166	5	Poly-Gly
	Compositional bias	434 – 437	4	Poly-Gln
Amino acid modifications
	Modified residue	122	1	Phosphoserine Ref.6
	Modified residue	600	1	Phosphoserine; by PKA Potential
	Glycosylation	182	1	N-linked (GlcNAc...) Potential
	Glycosylation	353	1	N-linked (GlcNAc...) Potential
	Glycosylation	643	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	160	1	D → E in AAB60668. Ref.1
	Sequence conflict	395	1	P → T in AAB60668. Ref.1
	Sequence conflict	636	1	E → D in AAB60668. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q61423 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 9322A3DC9CBA2AC4	FASTA	654	73,470
	10 20 30 40 50 60 MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGTGGSGGG 70 80 90 100 110 120 PHHHHQTRGA YSSHDPQGSR GSRRRRRQRT EKKKLHHRQS SFPHCSDLMP SGSEEKILRE 130 140 150 160 170 180 LSEEEEDEEE EEEEEEEGRF YYSEEDHGDG CSYTDLLPQD DGGGGGYSSV RYSDCCERVV 190 200 210 220 230 240 INVSGLRFET QMKTLAQFPE TLLGDPEKRT QYFDPLRNEY FFDRNRPSFD AILYYYQSGG 250 260 270 280 290 300 RLKRPVNVPF DIFTEEVKFY QLGEEALLKF REDEGFVREE EDRALPENEF KKQIWLLFEY 310 320 330 340 350 360 PESSSPARGI AIVSVLVILI SIVIFCLETL PEFRDDRDLI MALSAGGHSR LLNDTSAPHL 370 380 390 400 410 420 ENSGHTIFND PFFIVETVCI VWFSFEFVVR CFACPSQALF FKNIMNIIDI VSILPYFITL 430 440 450 460 470 480 GTDLAQQQGG GNGQQQQAMS FAILRIIRLV RVFRIFKLSR HSKGLQILGH TLRASMRELG 490 500 510 520 530 540 LLIFFLFIGV ILFSSAVYFA EADEPTTHFQ SIPDAFWWAV VTMTTVGYGD MKPITVGGKI 550 560 570 580 590 600 VGSLCAIAGV LTIALPVPVI VSNFNYFYHR ETENEEQTQL TQNAVSCPYL PSNLLKKFRS 610 620 630 640 650 STSSSLGDKS EYLEMEEGVK ESLCGKEEKC QGKGDESETD KNNCSNAKAV ETDV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. 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(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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 (JUL-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(2004) [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(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00121102.
PIR	S09045.
RefSeq	NP_067250.2. NM_021275.4.
UniGene	Mm.142718.
3D structure databases
ProteinModelPortal	Q61423.
SMR	Q61423. Positions 1-75, 176-572.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q61423. 1 interaction.
MINT	MINT-1780501.
STRING	10090.ENSMUSP00000106689.
PTM databases
PhosphoSite	Q61423.
Proteomic databases
PaxDb	Q61423.
PRIDE	Q61423.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000037012; ENSMUSP00000037958; ENSMUSG00000042604.
GeneID	16492.
KEGG	mmu:16492.
Organism-specific databases
CTD	3739.
MGI	MGI:96661. Kcna4.
Phylogenomic databases
eggNOG	COG1226.
GeneTree	ENSGT00560000076957.
HOGENOM	HOG000231015.
HOVERGEN	HBG052230.
InParanoid	Q8CBF8.
KO	K04877.
OMA	DPQSGRG.
OrthoDB	EOG4QRH3T.
Gene expression databases
Bgee	Q61423.
Genevestigator	Q61423.
GermOnline	ENSMUSG00000042604. Mus musculus.
Family and domain databases
Gene3D	1.20.5.600. 1 hit. 3.30.710.10. 1 hit.
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. 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. [Graphical view]
PANTHER	PTHR11537. PTHR11537. 1 hit.
Pfam	PF00520. Ion_trans. 1 hit. PF07941. K_channel_TID. 1 hit. PF02214. K_tetra. 1 hit. [Graphical view]
PRINTS	PR00169. KCHANNEL. PR01511. KV14CHANNEL. PR01491. KVCHANNEL. PR01496. SHAKERCHANEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL4474.
NextBio	289795.
SOURCE	Search...

Entry information

Entry name

KCNA4_MOUSE

Accession

Primary (citable) accession number: Q61423
Secondary accession number(s): Q8CBF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program