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Protein

Potassium voltage-gated channel subfamily S member 1

Gene

Kcns1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiREACT_352543. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily S member 1
Alternative name(s):
Delayed-rectifier K(+) channel alpha subunit 1
Voltage-gated potassium channel subunit Kv9.1
Gene namesi
Name:Kcns1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621524. Kcns1.

Subcellular locationi

  • Cell membrane By similarity; Multi-pass membrane protein By similarity

  • Note: May not reach the plasma membrane but remain in an intracellular compartment in the absence of KCNB1 or KCNB2.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 186186CytoplasmicBy similarityAdd
BLAST
Transmembranei187 – 20822Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini209 – 23931ExtracellularBy similarityAdd
BLAST
Transmembranei240 – 26223Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini263 – 27311CytoplasmicBy similarityAdd
BLAST
Transmembranei274 – 29118Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini292 – 30918ExtracellularBy similarityAdd
BLAST
Transmembranei310 – 33021Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini331 – 34515CytoplasmicBy similarityAdd
BLAST
Transmembranei346 – 36722Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini368 – 37912ExtracellularBy similarityAdd
BLAST
Intramembranei380 – 39112Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei392 – 3998By similarity
Topological domaini400 – 4067ExtracellularBy similarity
Transmembranei407 – 43529Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini436 – 49762CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 497497Potassium voltage-gated channel subfamily S member 1PRO_0000054083Add
BLAST

Proteomic databases

PRIDEiO88758.

PTM databases

PhosphoSiteiO88758.

Expressioni

Tissue specificityi

Highly expressed in brain, but not in the other tissues tested (PubMed:9704029).1 Publication

Gene expression databases

GenevisibleiO88758. RN.

Interactioni

Subunit structurei

Heteromultimer with KCNB1 and KCNB2. Does not form homomultimers.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018364.

Structurei

3D structure databases

ProteinModelPortaliO88758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi392 – 3976Selectivity filterBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi219 – 22810Poly-Ala

Domaini

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

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231016.
HOVERGENiHBG052230.
InParanoidiO88758.
KOiK04931.
OMAiWLTLENP.
OrthoDBiEOG7CRTPP.
PhylomeDBiO88758.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. 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.
IPR003971. K_chnl_volt-dep_Kv9.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01494. KV9CHANNEL.
PR01491. KVCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

O88758-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSEFPGPGS RVPWRPRDEA LRVNVGGVRR LLSARALARF PGTRLGRLQA
60 70 80 90 100
AVSEEQARRL CDDYDAAARE FYFDRHPGFF LGLLHFYRTG HLHVLDELCV
110 120 130 140 150
FAFGQEADYW GLGENALATC CRARYLERRV TRPRAWDEDS DAPSSVDPCP
160 170 180 190 200
DEISDVQREL ARYGAARCGR LRRRLWLTME NPGYSLPSKL FSCVSIGVVL
210 220 230 240 250
ASIAAMCIHS LPEYQAREAA AAVAAVAAGR SAEDVRDDPV LRRLEYFCIA
260 270 280 290 300
WFSFEVSSRL LLAPSTRNFF CHPLNLIDIV SVLPFYLTLL AGAALGDRRG
310 320 330 340 350
ASGEELGDLG KVVQVFRLMR IFRVLKLARH STGLRSLGAT LKHSYREVGI
360 370 380 390 400
LLLYLAVGVS VFSGVAYTAE EKNVGFDTIP ACWWWGTVSM TTVGYGDVVP
410 420 430 440 450
ETVAGKLAAS GCILGGILVV ALPITIIFNK FSHFYRRQKA LEAAVRSSGQ
460 470 480 490
REFEDLLSSV DGVSDVSLET SRETSQEGRS TDLETQAPSE PAKSHSY
Length:497
Mass (Da):54,915
Last modified:November 1, 1998 - v1
Checksum:i268AE4D56051F7A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17606 mRNA. Translation: CAA76804.1.
PIRiJE0275.
RefSeqiNP_446406.1. NM_053954.1.
XP_006235571.1. XM_006235509.2.
UniGeneiRn.30012.

Genome annotation databases

EnsembliENSRNOT00000018364; ENSRNOP00000018364; ENSRNOG00000013681.
GeneIDi117023.
KEGGirno:117023.
UCSCiRGD:621524. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17606 mRNA. Translation: CAA76804.1.
PIRiJE0275.
RefSeqiNP_446406.1. NM_053954.1.
XP_006235571.1. XM_006235509.2.
UniGeneiRn.30012.

3D structure databases

ProteinModelPortaliO88758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000018364.

PTM databases

PhosphoSiteiO88758.

Proteomic databases

PRIDEiO88758.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018364; ENSRNOP00000018364; ENSRNOG00000013681.
GeneIDi117023.
KEGGirno:117023.
UCSCiRGD:621524. rat.

Organism-specific databases

CTDi3787.
RGDi621524. Kcns1.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231016.
HOVERGENiHBG052230.
InParanoidiO88758.
KOiK04931.
OMAiWLTLENP.
OrthoDBiEOG7CRTPP.
PhylomeDBiO88758.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_352543. Voltage gated Potassium channels.

Miscellaneous databases

NextBioi619783.
PROiO88758.

Gene expression databases

GenevisibleiO88758. RN.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. 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.
IPR003971. K_chnl_volt-dep_Kv9.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01494. KV9CHANNEL.
PR01491. KVCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cloning and tissue distribution of two new potassium channel alpha-subunits from rat brain."
    Stocker M., Kerschensteiner D.
    Biochem. Biophys. Res. Commun. 248:927-934(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.

Entry informationi

Entry nameiKCNS1_RAT
AccessioniPrimary (citable) accession number: O88758
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: November 1, 1998
Last modified: July 22, 2015
This is version 110 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

External Data

Dasty 3

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 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.