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Protein

Potassium voltage-gated channel subfamily A member 6

Gene

Kcna6

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, KNCA5, KCNA6, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:1993474, PubMed:15618540). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation (Probable). Homotetrameric channels display rapid activation and slow inactivation (PubMed:1993474).Curated2 Publications

GO - Molecular functioni

  • delayed rectifier potassium channel activity Source: UniProtKB

GO - Biological processi

  • potassium ion transmembrane transport Source: UniProtKB
  • 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 6
Alternative name(s):
RCK2
Voltage-gated potassium channel subunit Kv1.6
Voltage-gated potassium channel subunit Kv2
Gene namesi
Name:Kcna6
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi62083. Kcna6.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei172 – 193Helical; Name=Segment S1By similarityAdd BLAST22
Transmembranei264 – 285Helical; Name=Segment S2By similarityAdd BLAST22
Transmembranei297 – 317Helical; Name=Segment S3By similarityAdd BLAST21
Transmembranei339 – 359Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST21
Transmembranei375 – 396Helical; Name=Segment S5By similarityAdd BLAST22
Intramembranei411 – 422Helical; Name=Pore helixBy similarityAdd BLAST12
Intramembranei423 – 430By similarity8
Transmembranei438 – 466Helical; Name=Segment S6By similarityAdd BLAST29

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry databases

GuidetoPHARMACOLOGYi543.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539921 – 530Potassium voltage-gated channel subfamily A member 6Add BLAST530

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3PhosphoserineBy similarity1
Modified residuei222Phosphoserine; by CK2Sequence analysis1
Lipidationi286S-palmitoyl cysteineSequence analysis1
Modified residuei512Phosphoserine; by PKACurated1
Modified residuei528Phosphothreonine; by PKASequence analysis1

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP17659.
PRIDEiP17659.

PTM databases

iPTMnetiP17659.
PhosphoSitePlusiP17659.

Interactioni

Subunit structurei

Homotetramer and heterotetramer of potassium channel proteins (Probable). Interacts with KCNAB1 and KCNAB2 (PubMed:9334400).Curated1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067348.

Structurei

3D structure databases

ProteinModelPortaliP17659.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni361 – 374S4-S5 linkerBy similarityAdd BLAST14

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi423 – 428Selectivity filterBy similarity6
Motifi527 – 529PDZ-bindingSequence analysis3

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.
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.
InParanoidiP17659.
PhylomeDBiP17659.

Family and domain databases

Gene3Di1.20.120.350. 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.
IPR004053. K_chnl_volt-dep_Kv1.6.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 3 hits.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01513. KV16CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

P17659-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSEKSLTLA APGEVRGPEG EQQDAGEFQE AEGGGGCCSS ERLVINISGL
60 70 80 90 100
RYETQLRTLS LFPDTLLGDP GRRVRFFDPL RNEYFFDRNR PSFDAILYYY
110 120 130 140 150
QSGGRLRRPV NVPLDIFMEE IRFYQLGDEA LAAFREDEGC LPEGGEDEKP
160 170 180 190 200
LPSQPFQRQV WLLFEYPESS GPARGIAIVS VLVILISIVI FCLETLPQFR
210 220 230 240 250
ADGRGGSNEG SGTRMSPASR GSHEEEDEDE DSYAFPGSIP SGGLGTGGTS
260 270 280 290 300
SFSTLGGSFF TDPFFLVETL CIVWFTFELL VRFSACPSKA AFFRNIMNII
310 320 330 340 350
DLVAIFPYFI TLGTELVQRH EQQPVSGGSG QNRQQAMSLA ILRVIRLVRV
360 370 380 390 400
FRIFKLSRHS KGLQILGKTL QASMRELGLL IFFLFIGVIL FSSAVYFAEA
410 420 430 440 450
DDVDSLFPSI PDAFWWAVVT MTTVGYGDMY PMTVGGKIVG SLCAIAGVLT
460 470 480 490 500
IALPVPVIVS NFNYFYHRET EQEEQGQYTH VTCGQPTPDL KATDNGLGKP
510 520 530
DFAEASRERR SSYLPTPHRA YAEKRMLTEV
Length:530
Mass (Da):58,884
Last modified:August 1, 1990 - v1
Checksum:i30A9774B66CF1DA5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti241S → L no nucleotide entry (PubMed:1993474).Curated1
Sequence conflicti333R → G in AAA41499 (PubMed:2361015).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17621 mRNA. Translation: CAA35622.1.
M27159 Genomic DNA. Translation: AAA41499.1. Sequence problems.
PIRiJH0167.
UniGeneiRn.60676.

Genome annotation databases

UCSCiRGD:62083. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17621 mRNA. Translation: CAA35622.1.
M27159 Genomic DNA. Translation: AAA41499.1. Sequence problems.
PIRiJH0167.
UniGeneiRn.60676.

3D structure databases

ProteinModelPortaliP17659.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067348.

Chemistry databases

GuidetoPHARMACOLOGYi543.

PTM databases

iPTMnetiP17659.
PhosphoSitePlusiP17659.

Proteomic databases

PaxDbiP17659.
PRIDEiP17659.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:62083. rat.

Organism-specific databases

RGDi62083. Kcna6.

Phylogenomic databases

eggNOGiKOG1545. Eukaryota.
COG1226. LUCA.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP17659.
PhylomeDBiP17659.

Miscellaneous databases

PROiP17659.

Family and domain databases

Gene3Di1.20.120.350. 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.
IPR004053. K_chnl_volt-dep_Kv1.6.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 3 hits.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01513. KV16CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKCNA6_RAT
AccessioniPrimary (citable) accession number: P17659
Secondary accession number(s): P19025
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 2, 2016
This is version 129 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

Complete proteome, Reference proteome

Documents

  1. 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.