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Protein

Potassium voltage-gated channel subfamily S member 2

Gene

Kcns2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 (PubMed:9305895).1 Publication

GO - Molecular functioni

GO - Biological processi

  • potassium ion transmembrane transport Source: GO_Central
  • potassium ion transport Source: UniProtKB
  • protein homooligomerization Source: InterPro
  • regulation of delayed rectifier potassium channel activity Source: UniProtKB
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_287159. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily S member 2
Alternative name(s):
Delayed-rectifier K(+) channel alpha subunit 2
Voltage-gated potassium channel subunit Kv9.2
Gene namesi
Name:Kcns2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1197011. Kcns2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 184184CytoplasmicBy similarityAdd
BLAST
Transmembranei185 – 20622Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini207 – 22519ExtracellularBy similarityAdd
BLAST
Transmembranei226 – 24823Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini249 – 25911CytoplasmicBy similarityAdd
BLAST
Transmembranei260 – 28021Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini281 – 29010ExtracellularBy similarity
Transmembranei291 – 31121Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini312 – 32615CytoplasmicBy similarityAdd
BLAST
Transmembranei327 – 34822Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini349 – 36113ExtracellularBy similarityAdd
BLAST
Intramembranei362 – 37312Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei374 – 3818By similarity
Topological domaini382 – 3887ExtracellularBy similarity
Transmembranei389 – 41729Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini418 – 47760CytoplasmicBy similarityAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: GO_Central
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • voltage-gated potassium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Potassium voltage-gated channel subfamily S member 2PRO_0000054085Add
BLAST

Proteomic databases

PRIDEiO35174.

PTM databases

PhosphoSiteiO35174.

Expressioni

Tissue specificityi

Detected in brain, but not in the other tissues tested. Expression was highest in the olfactory bulb, cerebral cortex, hippocampus, habenula, basolateral amygdaloid nuclei and cerebellum (PubMed:9305895).1 Publication

Gene expression databases

BgeeiO35174.
CleanExiMM_KCNS2.
ExpressionAtlasiO35174. baseline.
GenevisibleiO35174. MM.

Interactioni

Subunit structurei

Heterotetramer with KCNB1 and KCNB2 (PubMed:9305895). Does not form homomultimers (PubMed:9305895).1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000072645.

Structurei

3D structure databases

ProteinModelPortaliO35174.
SMRiO35174. Positions 15-420.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi374 – 3796Selectivity filterBy similarity

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.
InParanoidiO35174.
KOiK04932.
OMAiQSLWDMS.
OrthoDBiEOG7CRTPP.
PhylomeDBiO35174.
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.

O35174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRQSLWDVS DTDVEDGEIR INVGGFKRRL RSHTLLRFPE TRLGRLLLCH
60 70 80 90 100
SREAILELCD DYDDVQREFY FDRNPELFPY VLHFYHTGKL HVMAELCVFS
110 120 130 140 150
FSQEIEYWGI NEFFIDSCCS YSYHGRKVEP EQEKWDEQSD QESTTSSFDE
160 170 180 190 200
ILAFYNDASK FDGQPLGNFR RQLWLALDNP GYSVLSRVFS VLSILVVLGS
210 220 230 240 250
IITMCLNSLP DFQIPDSQGN PGEDPRFEIV EHFGIAWFTF ELVARFAVAP
260 270 280 290 300
DFLKFFKNAL NLIDLMSIVP FYITLVVNLV VESSPTLANL GRVAQVLRLM
310 320 330 340 350
RIFRILKLAR HSTGLRSLGA TLKYSYKEVG LLLLYLSVGI SIFSVVAYTI
360 370 380 390 400
EKEENEGLAT IPACWWWATV SMTTVGYGDV VPGTTAGKLT ASACILAGIL
410 420 430 440 450
VVVLPITLIF NKFSHFYRRQ KQLESAMRSC DFGDGMKEVP SVNLRDYYAH
460 470
KVKSLMASLT NMSRSSPSEL SLDDSLH
Length:477
Mass (Da):54,289
Last modified:January 1, 1998 - v1
Checksum:iC7AD7AA3AE312B2C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008574 mRNA. Translation: AAB72051.1.
AK048819 mRNA. Translation: BAC33468.1.
AK087481 mRNA. Translation: BAC39892.1.
BC059833 mRNA. Translation: AAH59833.1.
CCDSiCCDS27421.1.
RefSeqiNP_001258633.1. NM_001271704.1.
NP_851834.1. NM_181317.4.
UniGeneiMm.487585.
Mm.71045.

Genome annotation databases

EnsembliENSMUST00000072868; ENSMUSP00000072645; ENSMUSG00000050963.
GeneIDi16539.
KEGGimmu:16539.
UCSCiuc007vly.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF008574 mRNA. Translation: AAB72051.1.
AK048819 mRNA. Translation: BAC33468.1.
AK087481 mRNA. Translation: BAC39892.1.
BC059833 mRNA. Translation: AAH59833.1.
CCDSiCCDS27421.1.
RefSeqiNP_001258633.1. NM_001271704.1.
NP_851834.1. NM_181317.4.
UniGeneiMm.487585.
Mm.71045.

3D structure databases

ProteinModelPortaliO35174.
SMRiO35174. Positions 15-420.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000072645.

PTM databases

PhosphoSiteiO35174.

Proteomic databases

PRIDEiO35174.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000072868; ENSMUSP00000072645; ENSMUSG00000050963.
GeneIDi16539.
KEGGimmu:16539.
UCSCiuc007vly.2. mouse.

Organism-specific databases

CTDi3788.
MGIiMGI:1197011. Kcns2.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231016.
HOVERGENiHBG052230.
InParanoidiO35174.
KOiK04932.
OMAiQSLWDMS.
OrthoDBiEOG7CRTPP.
PhylomeDBiO35174.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_287159. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiKcns2. mouse.
NextBioi289995.
PROiO35174.
SOURCEiSearch...

Gene expression databases

BgeeiO35174.
CleanExiMM_KCNS2.
ExpressionAtlasiO35174. baseline.
GenevisibleiO35174. MM.

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

« Hide 'large scale' publications
  1. "New modulatory alpha subunits for mammalian Shab K+ channels."
    Salinas M., Duprat F., Heurteaux C., Hugnot J.-P., Lazdunski M.
    J. Biol. Chem. 272:24371-24379(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "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.
    , 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: Cerebellum and Eye.
  3. "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].
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiKCNS2_MOUSE
AccessioniPrimary (citable) accession number: O35174
Secondary accession number(s): Q543P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 123 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.