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Protein

Potassium voltage-gated channel subfamily S member 3

Gene

Kcns3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1. Heterotetrameric channel activity formed with KCNB1 show increased current amplitude with the threshold for action potential activation shifted towards more negative values in hypoxic-treated pulmonary artery smooth muscle cells.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_287159. Voltage gated Potassium channels.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily S member 3
Alternative name(s):
Voltage-gated potassium channel subunit Kv9.3
Gene namesi
Name:Kcns3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:1098804. Kcns3.

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.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 182182CytoplasmicBy similarityAdd
BLAST
Transmembranei183 – 20422Helical; Name=Segment S1By similarityAdd
BLAST
Topological domaini205 – 22016ExtracellularBy similarityAdd
BLAST
Transmembranei221 – 24323Helical; Name=Segment S2By similarityAdd
BLAST
Topological domaini244 – 25411CytoplasmicBy similarityAdd
BLAST
Transmembranei255 – 27521Helical; Name=Segment S3By similarityAdd
BLAST
Topological domaini276 – 28510ExtracellularBy similarity
Transmembranei286 – 30621Helical; Voltage-sensor; Name=Segment S4By similarityAdd
BLAST
Topological domaini307 – 32115CytoplasmicBy similarityAdd
BLAST
Transmembranei322 – 34322Helical; Name=Segment S5By similarityAdd
BLAST
Topological domaini344 – 35714ExtracellularBy similarityAdd
BLAST
Intramembranei358 – 36912Helical; Name=Pore helixBy similarityAdd
BLAST
Intramembranei370 – 3778By similarity
Topological domaini378 – 3847ExtracellularBy similarity
Transmembranei385 – 41329Helical; Name=Segment S6By similarityAdd
BLAST
Topological domaini414 – 49178CytoplasmicBy 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 – 491491Potassium voltage-gated channel subfamily S member 3PRO_0000320143Add
BLAST

Proteomic databases

PRIDEiQ8BQZ8.

Expressioni

Gene expression databases

BgeeiQ8BQZ8.
ExpressionAtlasiQ8BQZ8. baseline and differential.
GenevisibleiQ8BQZ8. MM.

Interactioni

Subunit structurei

Heterotetramer with KCNB1. Does not form homomultimers.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060706.

Structurei

3D structure databases

ProteinModelPortaliQ8BQZ8.
SMRiQ8BQZ8. Positions 14-416.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi370 – 3756Selectivity 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.
InParanoidiQ8BQZ8.
KOiK04933.
OMAiVCWWWAT.
OrthoDBiEOG7CRTPP.
PhylomeDBiQ8BQZ8.
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.

Q8BQZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFGEFFHRP GQDEELVNLN VGGFKQSVDQ STLLRFPHTR LGKLLTCHSE
60 70 80 90 100
EAILELCDDY SVADKEYYFD RNPFLFRYVL NFYYTGKLHV MEELCVFSFC
110 120 130 140 150
QEIEYWGINE LFIDSCCSSR YQERKEESHD KDWDQKSNDV STDSSFEESS
160 170 180 190 200
LFEKELEKFD ELRFGQLRKK IWIRMENPAY CLSAKLIAIS SLSVVLASIV
210 220 230 240 250
AMCVHSMSEF QNEDGEVDDP VLEGVEIACI AWFTGELAIR LVAAPSQKKF
260 270 280 290 300
WKNPLNIIDF VSIIPFYATL AVDTKEEESE DIENMGKVVQ ILRLMRIFRI
310 320 330 340 350
LKLARHSVGL RSLGATLRHS YHEVGLLLLF LSVGISIFSV LIYSVEKDEH
360 370 380 390 400
KSSLTSIPIC WWWATISMTT VGYGDTHPVT LAGKIIASTC IICGILVVAL
410 420 430 440 450
PITIIFNKFS KYYQKQKDME VDQCSEDPPE KCHELPYFNI RDVYAQQVHA
460 470 480 490
FITSLSSIGI VVSDPDSTDA SSVEDNEDAY NTASLENCTG K
Length:491
Mass (Da):55,993
Last modified:March 1, 2003 - v1
Checksum:iB36B818126D439C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046054 mRNA. Translation: BAC32583.1.
AK162957 mRNA. Translation: BAE37134.1.
BC132164 mRNA. Translation: AAI32165.1.
BC132464 mRNA. Translation: AAI32465.1.
CCDSiCCDS25813.1.
RefSeqiNP_001162036.1. NM_001168564.1.
NP_775593.1. NM_173417.3.
XP_006515143.1. XM_006515080.2.
XP_011242164.1. XM_011243862.1.
XP_011242165.1. XM_011243863.1.
XP_011242166.1. XM_011243864.1.
XP_011242167.1. XM_011243865.1.
XP_011242168.1. XM_011243866.1.
UniGeneiMm.113278.

Genome annotation databases

EnsembliENSMUST00000055673; ENSMUSP00000060706; ENSMUSG00000043673.
ENSMUST00000164495; ENSMUSP00000129412; ENSMUSG00000043673.
GeneIDi238076.
KEGGimmu:238076.
UCSCiuc007nas.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046054 mRNA. Translation: BAC32583.1.
AK162957 mRNA. Translation: BAE37134.1.
BC132164 mRNA. Translation: AAI32165.1.
BC132464 mRNA. Translation: AAI32465.1.
CCDSiCCDS25813.1.
RefSeqiNP_001162036.1. NM_001168564.1.
NP_775593.1. NM_173417.3.
XP_006515143.1. XM_006515080.2.
XP_011242164.1. XM_011243862.1.
XP_011242165.1. XM_011243863.1.
XP_011242166.1. XM_011243864.1.
XP_011242167.1. XM_011243865.1.
XP_011242168.1. XM_011243866.1.
UniGeneiMm.113278.

3D structure databases

ProteinModelPortaliQ8BQZ8.
SMRiQ8BQZ8. Positions 14-416.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000060706.

Proteomic databases

PRIDEiQ8BQZ8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000055673; ENSMUSP00000060706; ENSMUSG00000043673.
ENSMUST00000164495; ENSMUSP00000129412; ENSMUSG00000043673.
GeneIDi238076.
KEGGimmu:238076.
UCSCiuc007nas.1. mouse.

Organism-specific databases

CTDi3790.
MGIiMGI:1098804. Kcns3.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231016.
HOVERGENiHBG052230.
InParanoidiQ8BQZ8.
KOiK04933.
OMAiVCWWWAT.
OrthoDBiEOG7CRTPP.
PhylomeDBiQ8BQZ8.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_287159. Voltage gated Potassium channels.
REACT_297430. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.

Miscellaneous databases

NextBioi383663.
PROiQ8BQZ8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BQZ8.
ExpressionAtlasiQ8BQZ8. baseline and differential.
GenevisibleiQ8BQZ8. 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

  1. "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: Corpora quadrigemina and Spinal cord.
  2. "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].
    Tissue: Brain.

Entry informationi

Entry nameiKCNS3_MOUSE
AccessioniPrimary (citable) accession number: Q8BQZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: July 22, 2015
This is version 107 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.