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Q61762 (KCNA5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandPotassium
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMGlycoprotein
Isopeptide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmembrane hyperpolarization

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

negative regulation of potassium ion transport

Inferred from direct assay Ref.1. Source: MGI

positive regulation of G1/S transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of myoblast proliferation

Inferred from electronic annotation. Source: Ensembl

potassium ion export

Inferred from electronic annotation. Source: Ensembl

potassium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Inferred from direct assay Ref.1. Source: MGI

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

regulation of atrial cardiac muscle cell membrane repolarization

Inferred from electronic annotation. Source: Ensembl

regulation of heart rate by cardiac conduction

Inferred from electronic annotation. Source: Ensembl

regulation of membrane potential

Inferred from genetic interaction PubMed 15277200. Source: MGI

regulation of vasoconstriction

Inferred from mutant phenotype PubMed 11481235. Source: MGI

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred by curator Ref.1. Source: MGI

intercalated disc

Inferred from direct assay PubMed 18603586. Source: MGI

intracellular canaliculus

Inferred from electronic annotation. Source: Ensembl

membrane

Inferred from direct assay PubMed 18603586. Source: MGI

membrane raft

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay PubMed 15277200. Source: MGI

voltage-gated potassium channel complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondelayed rectifier potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

outward rectifier potassium channel activity

Inferred from electronic annotation. Source: Ensembl

potassium channel inhibitor activity

Inferred from direct assay Ref.1. Source: MGI

protein binding

Inferred from physical interaction PubMed 15277200PubMed 18603586. Source: MGI

voltage-gated potassium channel 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: Ensembl

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602Potassium voltage-gated channel subfamily A member 5
PRO_0000053986

Regions

Transmembrane242 – 26019Helical; Name=Segment S1; Potential
Transmembrane316 – 33621Helical; Name=Segment S2; Potential
Transmembrane347 – 36822Helical; Name=Segment S3; Potential
Transmembrane387 – 40822Helical; Voltage-sensor; Name=Segment S4; Potential
Transmembrane423 – 44422Helical; Name=Segment S5; Potential
Transmembrane484 – 50522Helical; Name=Segment S6; Potential
Motif469 – 4746Selectivity filter By similarity
Motif600 – 6023PDZ-binding
Compositional bias373 – 3764Poly-Gly

Amino acid modifications

Modified residue811Phosphoserine; by CK2 and PKA Potential
Modified residue5351Phosphoserine; by PKA Potential
Modified residue5461Phosphoserine; by PKA Potential
Modified residue5691Phosphoserine; by PKA Potential
Lipidation3371S-palmitoyl cysteine Potential
Glycosylation101N-linked (GlcNAc...) Potential
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation1811N-linked (GlcNAc...) Potential
Glycosylation2901N-linked (GlcNAc...) Potential
Cross-link212Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link525Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 200200Missing in isoform 2.
VSP_000961
Alternative sequence515 – 60288Missing in isoform 3.
VSP_000962

Experimental info

Sequence conflict81M → T in AAA39365. Ref.1
Sequence conflict231G → V in AAA39365. Ref.1
Sequence conflict611G → A in AAA39365. Ref.1
Sequence conflict1271G → D in AAA39365. Ref.1
Sequence conflict1301A → V in AAA39365. Ref.1
Sequence conflict1351T → N in AAA39365. Ref.1
Sequence conflict2491L → S in AAA39365. Ref.1
Sequence conflict268 – 2692DE → VD in AAA39365. Ref.1
Sequence conflict2741R → L in AAA39365. Ref.1
Sequence conflict289 – 2913ANG → TNA in AAA39365. Ref.1
Sequence conflict3011P → T in AAA39365. Ref.1
Sequence conflict452 – 4532HF → QL in AAA39365. Ref.1
Sequence conflict5531C → H in AAA39365. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 02926E85DC022DDA

FASTA60266,580
        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 

« Hide

Isoform 2 (5') [UniParc].

Checksum: 6BB846FB2409473D
Show »

FASTA40244,539
Isoform 3 (3') [UniParc].

Checksum: 9A047A2DE9D6DC7B
Show »

FASTA51456,871

References

« Hide '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. expand/collapse author list , 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.
CCDSCCDS20554.1. [Q61762-1]
PIRA49507.
RefSeqNP_666095.1. NM_145983.2. [Q61762-1]
UniGeneMm.222831.

3D structure databases

ProteinModelPortalQ61762.
SMRQ61762. Positions 111-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000055673.

PTM databases

PhosphoSiteQ61762.

Proteomic databases

PaxDbQ61762.
PRIDEQ61762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000060972; ENSMUSP00000055673; ENSMUSG00000045534. [Q61762-1]
GeneID16493.
KEGGmmu:16493.
UCSCuc009dva.2. mouse. [Q61762-1]

Organism-specific databases

CTD3741.
MGIMGI:96662. Kcna5.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000115291.
HOGENOMHOG000231015.
HOVERGENHBG052230.
InParanoidQ9Z1R6.
KOK04878.
OMAGGELQCP.
OrthoDBEOG7M0NRD.
TreeFamTF313103.

Gene expression databases

BgeeQ61762.
GenevestigatorQ61762.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. 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.
IPR004052. K_chnl_volt-dep_Kv1.5.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PTHR11537:SF25. PTHR11537:SF25. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01512. KV15CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

NextBio289799.
PROQ61762.
SOURCESearch...

Entry information

Entry nameKCNA5_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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