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Protein

Potassium voltage-gated channel subfamily A member 4

Gene

Kcna4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 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. 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 (PubMed:2348860, PubMed:8495559, PubMed:10896669). 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:2384173). Likewise, a heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid inactivation (PubMed:2348860).4 Publications

GO - Molecular functioni

  • ion channel activity Source: RGD
  • potassium channel activity Source: RGD
  • potassium ion binding Source: InterPro
  • voltage-gated potassium channel activity Source: UniProtKB

GO - Biological processi

  • potassium ion transmembrane transport Source: UniProtKB
  • potassium ion transport Source: RGD
  • 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

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 4
Alternative name(s):
RCK41 Publication
RHK1
RK3
Voltage-gated potassium channel subunit Kv1.4
Gene namesi
Name:Kcna4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2952. Kcna4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 306306CytoplasmicBy similarityAdd
BLAST
Transmembranei307 – 32822Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini329 – 37244ExtracellularBy similarityAdd
BLAST
Transmembranei373 – 39422Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini395 – 40511CytoplasmicBy similarityAdd
BLAST
Transmembranei406 – 42621Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini427 – 44115ExtracellularBy similarityAdd
BLAST
Transmembranei442 – 46221Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini463 – 47715CytoplasmicBy similarityAdd
BLAST
Transmembranei478 – 49922Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini500 – 51314ExtracellularBy similarityAdd
BLAST
Intramembranei514 – 52512Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei526 – 5338By similarity
Topological domaini534 – 5407ExtracellularBy similarity
Transmembranei541 – 56929Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini570 – 65586CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • axon Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5583.
GuidetoPHARMACOLOGYi541.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Potassium voltage-gated channel subfamily A member 4PRO_0000053984Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei123 – 1231PhosphoserineCombined sources
Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence analysis
Modified residuei601 – 6011Phosphoserine; by PKASequence analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP15385.
PRIDEiP15385.

PTM databases

iPTMnetiP15385.
PhosphoSiteiP15385.

Expressioni

Tissue specificityi

Detected in brain (at protein level) (PubMed:8361540, PubMed:9334400). Heart and brain.3 Publications

Interactioni

Subunit structurei

Homotetramer and heterotetramer of potassium channel proteins (PubMed:10896669). Interacts with KCNAB1 and KCNAB2 (PubMed:9334400). Binds PDZ domains of DLG1, DLG2 and DLG4. Interacts with SIGMAR1 (PubMed:11988171). Part of a complex containing KCNA1, KCNAB1 and LGI1 (PubMed:16504945). Detected in a complex with KCNA1 (PubMed:2348860, PubMed:10896669). Interacts with KCNA2 (PubMed:8361540, PubMed:10896669, PubMed:12632190). Interacts (via cytoplasmic N-terminal domain) with KCNRG (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DLG4P783529EBI-631417,EBI-80389From a different organism.

Protein-protein interaction databases

BioGridi247502. 2 interactions.
IntActiP15385. 5 interactions.
MINTiMINT-222765.
STRINGi10116.ENSRNOP00000006524.

Structurei

Secondary structure

1
655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 133Combined sources
Helixi21 – 244Combined sources
Helixi25 – 306Combined sources
Helixi31 – 333Combined sources
Helixi43 – 464Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KN7NMR-A1-75[»]
1ZTONMR-A1-36[»]
ProteinModelPortaliP15385.
SMRiP15385. Positions 1-75, 178-573.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15385.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni464 – 47714S4-S5 linkerBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi526 – 5316Selectivity filterBy similarity
Motifi653 – 6553PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi38 – 5013Poly-AlaAdd
BLAST
Compositional biasi62 – 654Poly-His
Compositional biasi92 – 954Poly-Lys
Compositional biasi124 – 13815Poly-GluAdd
BLAST
Compositional biasi163 – 1675Poly-Gly
Compositional biasi435 – 4384Poly-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.Curated
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

eggNOGiKOG1545. Eukaryota.
COG1226. LUCA.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP15385.
KOiK04877.
PhylomeDBiP15385.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
1.20.5.600. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
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.
IPR011333. SKP1/BTB/POZ.
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.

P15385-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA
60 70 80 90 100
VEGTGGSGGG PHHHHQTRGA YSSHDPQGSR GSREEEATRT EKKKKLHHRQ
110 120 130 140 150
SSFPHCSDLM PSGSEEKILR ELSEEEEDEE EEEEEEEEGR FYYSEEDHGD
160 170 180 190 200
GCSYTDLLPQ DDGGGGGYSS VRYSDCCERV VINVSGLRFE TQMKTLAQFP
210 220 230 240 250
ETLLGDPEKR TQYFDPLRNE YFFDRNRPSF DAILYYYQSG GRLKRPVNVP
260 270 280 290 300
FDIFTEEVKF YQLGEEALLK FREDEGFVRE EEDRALPENE FKKQIWLLFE
310 320 330 340 350
YPESSSPARG IAIVSVLVIL ISIVIFCLET LPEFRDDRDL IMALSAGGHS
360 370 380 390 400
RLLNDTSAPH LENSGHTIFN DPFFIVETVC IVWFSFEFVV RCFACPSQAL
410 420 430 440 450
FFKNIMNIID IVSILPYFIT LGTDLAQQQG GGNGQQQQAM SFAILRIIRL
460 470 480 490 500
VRVFRIFKLS RHSKGLQILG HTLRASMREL GLLIFFLFIG VILFSSAVYF
510 520 530 540 550
AEADEPTTHF QSIPDAFWWA VVTMTTVGYG DMKPITVGGK IVGSLCAIAG
560 570 580 590 600
VLTIALPVPV IVSNFNYFYH RETENEEQTQ LTQNAVSCPY LPSNLLKKFR
610 620 630 640 650
SSTSSSLGDK SEYLEMEEGV KESLCGKEEK CQGKGDDSET DKNNCSNAKA

VETDV
Length:655
Mass (Da):73,390
Last modified:April 1, 1990 - v1
Checksum:i40AEF2F901A05F43
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti42 – 421A → L in AAA41469 (PubMed:2384173).Curated
Sequence conflicti84 – 885EEEAT → RRRRQ in AAA41469 (PubMed:2384173).Curated
Sequence conflicti95 – 951Missing in AAA41469 (PubMed:2384173).Curated
Sequence conflicti310 – 3101G → A in AAA41469 (PubMed:2384173).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16002 mRNA. Translation: CAA34133.1.
M32867 mRNA. Translation: AAA41469.1.
PIRiS11049.
RefSeqiNP_037103.1. NM_012971.2.
UniGeneiRn.9884.

Genome annotation databases

GeneIDi25469.
KEGGirno:25469.
UCSCiRGD:2952. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16002 mRNA. Translation: CAA34133.1.
M32867 mRNA. Translation: AAA41469.1.
PIRiS11049.
RefSeqiNP_037103.1. NM_012971.2.
UniGeneiRn.9884.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KN7NMR-A1-75[»]
1ZTONMR-A1-36[»]
ProteinModelPortaliP15385.
SMRiP15385. Positions 1-75, 178-573.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247502. 2 interactions.
IntActiP15385. 5 interactions.
MINTiMINT-222765.
STRINGi10116.ENSRNOP00000006524.

Chemistry

ChEMBLiCHEMBL5583.
GuidetoPHARMACOLOGYi541.

PTM databases

iPTMnetiP15385.
PhosphoSiteiP15385.

Proteomic databases

PaxDbiP15385.
PRIDEiP15385.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25469.
KEGGirno:25469.
UCSCiRGD:2952. rat.

Organism-specific databases

CTDi3739.
RGDi2952. Kcna4.

Phylogenomic databases

eggNOGiKOG1545. Eukaryota.
COG1226. LUCA.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP15385.
KOiK04877.
PhylomeDBiP15385.

Miscellaneous databases

EvolutionaryTraceiP15385.
PROiP15385.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
1.20.5.600. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
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.
IPR011333. SKP1/BTB/POZ.
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...

Entry informationi

Entry nameiKCNA4_RAT
AccessioniPrimary (citable) accession number: P15385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 8, 2016
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.