Q61762 (KCNA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Potassium voltage-gated channel subfamily A member 5

Alternative name(s):
Voltage-gated potassium channel subunit Kv1.5
Short name=KV1-5

Gene names

Name:

Kcna5

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	602 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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. This channel displays rapid activation and slow inactivation. Ref.2
Subunit structure	Heterotetramer of potassium channel proteins. Interacts with DLG1, which enhances channel currents. Forms a ternary complex with DLG1 and CAV3 By similarity. Interacts with UBE2I By similarity.
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Highly expressed in heart and moderately in brain. Low levels in thymus, skeletal muscle and spleen. Not expressed in liver, lung or kidney.
Domain	The amino terminus may be important in determining the rate of inactivation of the channel while the C-terminal PDZ-binding motif may play a role in modulation of channel activity and/or targeting of the channel to specific subcellular compartments By similarity. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
Post-translational modification	Sumoylated on Lys-212, and Lys-525, preferentially with SUMO3. Sumoylation regulates the voltage sensitivity of the channel By similarity.
Disruption phenotype	No visible phenotype. The action potential in myocytes is not prolonged by low concentrations of 4-aminopyridine, contrary to the situation in wild-type. Ref.2
Sequence similarities	Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Glycoprotein Isopeptide bond Lipoprotein Palmitate Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	membrane hyperpolarization Inferred from electronic annotation. Source: Compara negative regulation of potassium ion transport Inferred from direct assay Ref.1. Source: MGI potassium ion export Inferred from electronic annotation. Source: Compara potassium ion homeostasis Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: InterPro reduction of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara regulation of atrial cardiac muscle cell membrane repolarization Inferred from electronic annotation. Source: Compara regulation of heart rate by cardiac conduction Inferred from electronic annotation. Source: Compara regulation of membrane potential Inferred from genetic interaction PubMed 15277200. Source: MGI regulation of potassium ion transport Inferred from electronic annotation. Source: Compara regulation of vasoconstriction Inferred from mutant phenotype PubMed 11481235. Source: MGI response to hypoxia Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred from direct assay Ref.1. Source: MGI intercalated disc Inferred from direct assay PubMed 18603586. Source: MGI membrane raft Inferred from electronic annotation. Source: Compara voltage-gated potassium channel complex Inferred from electronic annotation. Source: Compara
Molecular_function	delayed rectifier potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome outward rectifier potassium channel activity Inferred from electronic annotation. Source: Compara potassium channel inhibitor activity Inferred from direct assay Ref.1. Source: MGI voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q61762-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q61762-2)

Also known as: 5';

The sequence of this isoform differs from the canonical sequence as follows:
     1-200: Missing.

Isoform 3 (identifier: Q61762-3)

Also known as: 3';

The sequence of this isoform differs from the canonical sequence as follows:
     515-602: Missing.

Note: Inactive. Inhibits expression of isoform 1 and isoform 2.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 602	602	Potassium voltage-gated channel subfamily A member 5		PRO_0000053986
Regions
	Transmembrane	242 – 260	19	Helical; Name=Segment S1; Potential
	Transmembrane	316 – 336	21	Helical; Name=Segment S2; Potential
	Transmembrane	347 – 368	22	Helical; Name=Segment S3; Potential
	Transmembrane	387 – 408	22	Helical; Voltage-sensor; Name=Segment S4; Potential
	Transmembrane	423 – 444	22	Helical; Name=Segment S5; Potential
	Transmembrane	484 – 505	22	Helical; Name=Segment S6; Potential
	Motif	469 – 474	6	Selectivity filter By similarity
	Motif	600 – 602	3	PDZ-binding
	Compositional bias	373 – 376	4	Poly-Gly
Amino acid modifications
	Modified residue	81	1	Phosphoserine; by CK2 and PKA Potential
	Modified residue	535	1	Phosphoserine; by PKA Potential
	Modified residue	546	1	Phosphoserine; by PKA Potential
	Modified residue	569	1	Phosphoserine; by PKA Potential
	Lipidation	337	1	S-palmitoyl cysteine Potential
	Glycosylation	10	1	N-linked (GlcNAc...) Potential
	Glycosylation	44	1	N-linked (GlcNAc...) Potential
	Glycosylation	116	1	N-linked (GlcNAc...) Potential
	Glycosylation	181	1	N-linked (GlcNAc...) Potential
	Glycosylation	290	1	N-linked (GlcNAc...) Potential
	Cross-link	212		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	525		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 200	200	Missing in isoform 2.		VSP_000961
	Alternative sequence	515 – 602	88	Missing in isoform 3.		VSP_000962
Experimental info
	Sequence conflict	8	1	M → T in AAA39365. Ref.1
	Sequence conflict	23	1	G → V in AAA39365. Ref.1
	Sequence conflict	61	1	G → A in AAA39365. Ref.1
	Sequence conflict	127	1	G → D in AAA39365. Ref.1
	Sequence conflict	130	1	A → V in AAA39365. Ref.1
	Sequence conflict	135	1	T → N in AAA39365. Ref.1
	Sequence conflict	249	1	L → S in AAA39365. Ref.1
	Sequence conflict	268 – 269	2	DE → VD in AAA39365. Ref.1
	Sequence conflict	274	1	R → L in AAA39365. Ref.1
	Sequence conflict	289 – 291	3	ANG → TNA in AAA39365. Ref.1
	Sequence conflict	301	1	P → T in AAA39365. Ref.1
	Sequence conflict	452 – 453	2	HF → QL in AAA39365. Ref.1
	Sequence conflict	553	1	C → H in AAA39365. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 02926E85DC022DDA	FASTA	602	66,580
	10 20 30 40 50 60 MEISLVPMEN GSAMTLRGGG EAGASCVQSP RGECGCPPTA GLNNQSKETS PRRRATHEDA 70 80 90 100 110 120 GQGGRPLPPM PQELPQPRRP SAEDEEGEGD PGLGTVEEDQ APQDSGSLHH QRVLINISGL 130 140 150 160 170 180 RFETQLGTLA QFPNTLLGDP VKRLRYFDPL RNEYFFDRNR PSFDGILYYY QSGGRLRRPV 190 200 210 220 230 240 NVSLDVFADE IRFYQLGDEA MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA 250 260 270 280 290 300 RAIAIVSVLV ILISIITFCL ETLPEFRDER ELLRHPPVPP QPPAPAPGAN GSGSGVLSSG 310 320 330 340 350 360 PTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDIVAIFPYF 370 380 390 400 410 420 ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM 430 440 450 460 470 480 RELGLLIFFL FIGVILFSSA VYFAEADNQG SHFSSIPDAF WWAVVTMTTV GYGDMRPITV 490 500 510 520 530 540 GGKIVGSLCA IAGVLTIALP VPVIVSNFNY FYHRETDHEE QAALKEEQGI QRRESGLDTG 550 560 570 580 590 600 GQRKVSCSKA SFCKTGGPLE STDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET DL
	Isoform 2 (5') [UniParc]. Checksum: 6BB846FB2409473D	FASTA	402	44,539
	10 20 30 40 50 60 MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA RAIAIVSVLV ILISIITFCL 70 80 90 100 110 120 ETLPEFRDER ELLRHPPVPP QPPAPAPGAN GSGSGVLSSG PTVAPLLPRT LADPFFIVET 130 140 150 160 170 180 TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDIVAIFPYF ITLGTELAEQ QPGGGGQNGQ 190 200 210 220 230 240 QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM RELGLLIFFL FIGVILFSSA 250 260 270 280 290 300 VYFAEADNQG SHFSSIPDAF WWAVVTMTTV GYGDMRPITV GGKIVGSLCA IAGVLTIALP 310 320 330 340 350 360 VPVIVSNFNY FYHRETDHEE QAALKEEQGI QRRESGLDTG GQRKVSCSKA SFCKTGGPLE 370 380 390 400 STDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET DL
	Isoform 3 (3') [UniParc]. Checksum: 9A047A2DE9D6DC7B	FASTA	514	56,871
	10 20 30 40 50 60 MEISLVPMEN GSAMTLRGGG EAGASCVQSP RGECGCPPTA GLNNQSKETS PRRRATHEDA 70 80 90 100 110 120 GQGGRPLPPM PQELPQPRRP SAEDEEGEGD PGLGTVEEDQ APQDSGSLHH QRVLINISGL 130 140 150 160 170 180 RFETQLGTLA QFPNTLLGDP VKRLRYFDPL RNEYFFDRNR PSFDGILYYY QSGGRLRRPV 190 200 210 220 230 240 NVSLDVFADE IRFYQLGDEA MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA 250 260 270 280 290 300 RAIAIVSVLV ILISIITFCL ETLPEFRDER ELLRHPPVPP QPPAPAPGAN GSGSGVLSSG 310 320 330 340 350 360 PTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDIVAIFPYF 370 380 390 400 410 420 ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM 430 440 450 460 470 480 RELGLLIFFL FIGVILFSSA VYFAEADNQG SHFSSIPDAF WWAVVTMTTV GYGDMRPITV 490 500 510 GGKIVGSLCA IAGVLTIALP VPVIVSNFNY FYHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Multiple mRNA isoforms encoding the mouse cardiac Kv1-5 delayed rectifier K+ channel." Attali B., Lesage F., Ziliani P., Guillemare E., Honore E., Waldmann R., Hugnot J.-P., Mattei M.-G., Lazdunski M., Barhanin J. J. Biol. Chem. 268:24283-24289(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3). Strain: Swiss. Tissue: Heart.
[2]	"Targeted replacement of KV1.5 in the mouse leads to loss of the 4-aminopyridine-sensitive component of I(K,slow) and resistance to drug-induced qt prolongation." London B., Guo W., Pan X., Lee J.S., Shusterman V., Rocco C.J., Logothetis D.A., Nerbonne J.M., Hill J.A. Circ. Res. 88:940-946(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION. Strain: 129/Sv.
[3]	"Cloning and functional expression of mouse heart K+ channel alpha-subunits, Kv1.5, Kv4.2, and Kv4.3." Tanaka H., Janzen K., Winkfein R.J., Fiset C., Clark B., Giles W.R. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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: Stomach.
[5]	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].
[6]	"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]. Tissue: Eye.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L22218 mRNA. Translation: AAA39365.1. AF108659 mRNA. Translation: AAD13779.1. AF302768 Genomic DNA. Translation: AAG40241.1. AK146843 mRNA. Translation: BAE27474.1. CH466523 Genomic DNA. Translation: EDK99840.1. BC021787 mRNA. Translation: AAH21787.1.
IPI	IPI00124939. IPI00222003. IPI00222004.
PIR	A49507.
RefSeq	NP_666095.1. NM_145983.2.
UniGene	Mm.222831.
3D structure databases
ProteinModelPortal	Q61762.
SMR	Q61762. Positions 111-516.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000055673.
PTM databases
PhosphoSite	Q61762.
Proteomic databases
PaxDb	Q61762.
PRIDE	Q61762.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000060972; ENSMUSP00000055673; ENSMUSG00000045534.
GeneID	16493.
KEGG	mmu:16493.
Organism-specific databases
CTD	3741.
MGI	MGI:96662. Kcna5.
Phylogenomic databases
eggNOG	COG1226.
GeneTree	ENSGT00560000076957.
HOGENOM	HOG000231015.
HOVERGEN	HBG052230.
InParanoid	Q9Z1R6.
KO	K04878.
OMA	KRLRYFD.
OrthoDB	EOG4R502V.
Gene expression databases
Bgee	Q61762.
Genevestigator	Q61762.
GermOnline	ENSMUSG00000045534. Mus musculus.
Family and domain databases
Gene3D	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. IPR004052. K_chnl_volt-dep_Kv1.5. IPR003131. T1-type_BTB. [Graphical view]
PANTHER	PTHR11537. PTHR11537. 1 hit. PTHR11537:SF25. PTHR11537:SF25. 1 hit.
Pfam	PF00520. Ion_trans. 1 hit. PF02214. K_tetra. 1 hit. [Graphical view]
PRINTS	PR00169. KCHANNEL. PR01512. KV15CHANNEL. PR01491. KVCHANNEL. PR01496. SHAKERCHANEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL4473.
NextBio	289799.
SOURCE	Search...

Entry information

Entry name

KCNA5_MOUSE

Accession

Primary (citable) accession number: Q61762
Secondary accession number(s): Q9Z1R6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program