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P19024 (KCNA5_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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):
RCK7
RK4
Voltage-gated potassium channel subunit Kv1.5
Gene names
Name:Kcna5
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length602 AA.
Sequence statusComplete.
Protein existenceEvidence 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. This channel displays rapid activation and slow inactivation. Ref.5

Subunit structure

Heterotetramer of potassium channel proteins By similarity. Interacts with DLG1, which enhances channel currents. Forms a ternary complex with DLG1 and CAV3. Interacts with UBE2I By similarity. Ref.4 Ref.5

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed equally in atrium, ventricle, aorta and skeletal muscle. Weaker expression in brain. Ref.2

Induction

Expression regulated by cAMP in a tissue-specific manner. In primary cardiac cells, levels increase by 6-fold, and in GH3 cells, levels decrease 5-6-fold.

Domain

The N-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.

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. Kv1.5/KCNA5 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentMembrane
   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 mutant phenotype PubMed 15151918. Source: RGD

negative regulation of potassium ion transport

Inferred from electronic annotation. Source: Ensembl

positive regulation of G1/S transition of mitotic cell cycle

Inferred from direct assay PubMed 18230363. Source: RGD

positive regulation of myoblast proliferation

Inferred from direct assay PubMed 18230363. Source: RGD

potassium ion export

Inferred from electronic annotation. Source: Ensembl

potassium ion homeostasis

Inferred from mutant phenotype PubMed 12127166. Source: RGD

potassium ion transport

Inferred from mutant phenotype PubMed 12127166. Source: RGD

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

protein oligomerization

Inferred from mutant phenotype PubMed 12127166. Source: RGD

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 mutant phenotype PubMed 18230363. Source: RGD

regulation of vasoconstriction

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from expression pattern PubMed 15151918. Source: RGD

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 16185660. Source: RGD

Z disc

Inferred from direct assay PubMed 17054951. Source: RGD

endoplasmic reticulum

Inferred from direct assay PubMed 16185660. Source: RGD

intercalated disc

Inferred from direct assay PubMed 20357183. Source: RGD

intracellular canaliculus

Inferred from direct assay PubMed 17496801. Source: RGD

membrane raft

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from direct assay PubMed 17496801. Source: RGD

plasma membrane

Inferred from direct assay PubMed 17496801. Source: RGD

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 mutant phenotype PubMed 12127166PubMed 15930148. Source: RGD

potassium channel inhibitor activity

Inferred from electronic annotation. Source: Ensembl

receptor binding

Inferred from physical interaction PubMed 16527989. Source: RGD

voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 602602Potassium voltage-gated channel subfamily A member 5
PRO_0000053989

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
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

Experimental info

Mutagenesis600 – 6023TDL → AAA: Loss of interaction with DLG1. Ref.4
Sequence conflict5531C → S no nucleotide entry Ref.2

Sequences

Sequence LengthMass (Da)Tools
P19024 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 6A784535FF226ED7

FASTA60266,553
        10         20         30         40         50         60 
MEISLVPLEN GSAMTLRGGG EAGASCVQTP RGECGCPPTS GLNNQSKETL LRGRTTLEDA 

        70         80         90        100        110        120 
NQGGRPLPPM AQELPQPRRL SAEDEEGEGD PGLGTVEEDQ APQDAGSLHH QRVLINISGL 

       130        140        150        160        170        180 
RFETQLGTLA QFPNTLLGDP AKRLHYFDPL 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 QPPAPAPGIN GSVSGALSSG 

       310        320        330        340        350        360 
PTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDVVAIFPYF 

       370        380        390        400        410        420 
ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM 

       430        440        450        460        470        480 
RELGLLIFFL FIGVILFSSA VYFAEADNHG SHFSSIPDAF WWAVVTMTTV GYGDMRPITV 

       490        500        510        520        530        540 
GGKIVGSLCA IAGVLTIALP VPVIVSNFNY FYHRETDHEE QAALKEEQGN QRRESGLDTG 

       550        560        570        580        590        600 
GQRKVSCSKA SFCKTGGSLE SSDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET 


DL 

« Hide

References

[1]"Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain."
Swanson R., Marshall J., Smith J., Williams J., Boyle M.B., Folander K., Luneau C.J., Antanavage J., Oliva C., Buhrow S.A., Bennett C., Stein R.B., Kaczmarek L.M.
Neuron 4:929-939(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[2]"Cloning and tissue-specific expression of five voltage-gated potassium channel cDNAs expressed in rat heart."
Roberds S.L., Tamkun M.M.
Proc. Natl. Acad. Sci. U.S.A. 88:1798-1802(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Heart.
[3]"The transcription of a mammalian voltage-gated potassium channel is regulated by cAMP in a cell-specific manner."
Mori Y., Matsubara H., Folco E., Siegel A., Koren G.
J. Biol. Chem. 268:26482-26493(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
[4]"SAP97 interacts with Kv1.5 in heterologous expression systems."
Murata M., Buckett P.D., Zhou J., Brunner M., Folco E., Koren G.
Am. J. Physiol. 281:H2575-H2584(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1, MUTAGENESIS OF 600-THR--LEU-602.
[5]"Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5."
Folco E.J., Liu G.-X., Koren G.
Am. J. Physiol. 287:H681-H690(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1 AND CAV3, FUNCTION IN CELL EXCITATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27158 Genomic DNA. Translation: AAA41498.1.
L23434 Genomic DNA. Translation: AAA42337.1.
PIRJH0166.
RefSeqNP_037104.1. NM_012972.1.
UniGeneRn.162789.

3D structure databases

ProteinModelPortalP19024.
SMRP19024. Positions 111-516.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247503. 4 interactions.
IntActP19024. 2 interactions.
MINTMINT-3973915.
STRING10116.ENSRNOP00000026691.

Proteomic databases

PaxDbP19024.
PRIDEP19024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000026691; ENSRNOP00000026691; ENSRNOG00000019719.
GeneID25470.
KEGGrno:25470.
UCSCRGD:2953. rat.

Organism-specific databases

CTD3741.
RGD2953. Kcna5.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000115291.
HOGENOMHOG000231015.
HOVERGENHBG052230.
InParanoidP19024.
KOK04878.
OMAGGELQCP.
OrthoDBEOG7M0NRD.
PhylomeDBP19024.
TreeFamTF313103.

Gene expression databases

GenevestigatorP19024.

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

NextBio606769.
PROP19024.

Entry information

Entry nameKCNA5_RAT
AccessionPrimary (citable) accession number: P19024
Secondary accession number(s): Q6LEB7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 127 of the entry and version 1 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