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Protein

Potassium voltage-gated channel subfamily S member 3

Gene

KCNS3

Organism
Oryctolagus cuniculus (Rabbit)
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

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily S member 3
Alternative name(s):
Delayed-rectifier K(+) channel alpha subunit 3
Voltage-gated potassium channel subunit Kv9.3
Gene namesi
Name:KCNS3
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 2

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_0000054088Add
BLAST

Interactioni

Subunit structurei

Heterotetramer with KCNB1. Does not form homomultimers.By similarity

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000006367.

Structurei

3D structure databases

ProteinModelPortaliQ9TT17.
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

eggNOGiKOG3713. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231016.
HOVERGENiHBG052230.
InParanoidiQ9TT17.
KOiK04933.
OMAiMENPASC.
OrthoDBiEOG091G0FP3.
TreeFamiTF313103.

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.
IPR003971. K_chnl_volt-dep_Kv9.
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.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01494. KV9CHANNEL.
PR01491. KVCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9TT17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFGEFFHRP GPDEELVNLN VGGFKQSVDQ STLLRFPHTR LGKLLTCHSE
60 70 80 90 100
EAILELCDDY SVADKEYYFD RNPSLFRYVL NFYYTGKLHV MEELCVFSFC
110 120 130 140 150
QEIEYWGINE LFIDSCCSNR YQERKEENHE KDWDQKSNDV STDTSFEESS
160 170 180 190 200
VFEKELEKFD QLRFGQLRKK IWIRMENPAY CLSAKLIAIS SLSVVLASIV
210 220 230 240 250
AMCVHSMSEF QNEDGEVDDP VLEGVEIACI AWFTGELAVR LVAAPCQKKF
260 270 280 290 300
WKNPLNIIDF VSIIPFYATL AVDTKEEESE DIENMGKVVQ ILRLMRIFRI
310 320 330 340 350
LKLARHSVGL RSLGATLRHS YHEVGLLLLF LSVGISIFSV LIYSVEKDDH
360 370 380 390 400
TSSLTSIPIC WWWATISMTT VGYGDTHPVT LAGKLIASTC IICGILVVAL
410 420 430 440 450
PITIIFNKFS KYYQKQKDID VDQCSEDPPE KCPELPYFNI RDLYAQRVHA
460 470 480 490
FITSLSSVGI VVSDPDSTDA SSIEDNEDVY NTASLENCTA K
Length:491
Mass (Da):55,942
Last modified:May 1, 2000 - v1
Checksum:i2EE396E0889D6F77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF209723 mRNA. Translation: AAF22833.1.
RefSeqiNP_001076121.1. NM_001082652.1.
UniGeneiOcu.2409.

Genome annotation databases

EnsembliENSOCUT00000007364; ENSOCUP00000006367; ENSOCUG00000007365.
GeneIDi100009354.
KEGGiocu:100009354.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF209723 mRNA. Translation: AAF22833.1.
RefSeqiNP_001076121.1. NM_001082652.1.
UniGeneiOcu.2409.

3D structure databases

ProteinModelPortaliQ9TT17.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9986.ENSOCUP00000006367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000007364; ENSOCUP00000006367; ENSOCUG00000007365.
GeneIDi100009354.
KEGGiocu:100009354.

Organism-specific databases

CTDi3790.

Phylogenomic databases

eggNOGiKOG3713. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118981.
HOGENOMiHOG000231016.
HOVERGENiHBG052230.
InParanoidiQ9TT17.
KOiK04933.
OMAiMENPASC.
OrthoDBiEOG091G0FP3.
TreeFamiTF313103.

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.
IPR003971. K_chnl_volt-dep_Kv9.
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.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01494. KV9CHANNEL.
PR01491. KVCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiKCNS3_RABIT
AccessioniPrimary (citable) accession number: Q9TT17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2002
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 90 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.