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Protein

Potassium voltage-gated channel subfamily A member 3

Gene

Kcna3

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

Functioni

Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei228 – 2281Not glycosylated

GO - Molecular functioni

  • delayed rectifier potassium channel activity Source: RGD
  • outward rectifier potassium channel activity Source: RGD
  • voltage-gated potassium channel activity Source: UniProtKB

GO - Biological processi

  • potassium ion transmembrane transport Source: UniProtKB
  • potassium ion transport Source: RGD
  • 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

Enzyme and pathway databases

ReactomeiREACT_352543. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 3
Alternative name(s):
RCK3
RGK5
Voltage-gated potassium channel subunit Kv1.3
Voltage-gated potassium channel subunit Kv3
Gene namesi
Name:Kcna3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unassembled WGS sequence

Organism-specific databases

RGDi2951. Kcna3.

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 184184CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei185 – 20319Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Topological domaini204 – 24441ExtracellularSequence AnalysisAdd
BLAST
Transmembranei245 – 26622Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Topological domaini267 – 27711CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei278 – 29821Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Topological domaini299 – 31214ExtracellularSequence AnalysisAdd
BLAST
Transmembranei313 – 33119Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Topological domaini332 – 34716CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei348 – 36720Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Topological domaini368 – 40841ExtracellularSequence AnalysisAdd
BLAST
Transmembranei409 – 43123Helical; Name=Segment S6Sequence AnalysisAdd
BLAST
Topological domaini432 – 52594CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • membrane raft Source: BHF-UCL
  • plasma membrane Source: BHF-UCL
  • 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 – 525525Potassium voltage-gated channel subfamily A member 3PRO_0000053979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi229 – 2291N-linked (GlcNAc...)1 Publication
Lipidationi267 – 2671S-palmitoyl cysteineSequence Analysis
Modified residuei470 – 4701Phosphoserine; by PKASequence Analysis

Post-translational modificationi

N-glycosylation promotes the cell surface expression.1 Publication

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP15384.
PRIDEiP15384.

Expressioni

Gene expression databases

ExpressionAtlasiP15384. baseline and differential.
GenevisibleiP15384. RN.

Interactioni

Subunit structurei

Heterotetramer of potassium channel proteins (By similarity). Binds PDZ domains of DLG1, DLG2 and DLG4.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DLG4P783522EBI-631478,EBI-80389From a different organism.

Protein-protein interaction databases

BioGridi248344. 1 interaction.
IntActiP15384. 1 interaction.
STRINGi10116.ENSRNOP00000024372.

Structurei

3D structure databases

ProteinModelPortaliP15384.
SMRiP15384. Positions 54-441.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi394 – 3996Selectivity filterBy similarity
Motifi523 – 5253PDZ-binding

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 segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP15384.
KOiK04876.
OMAiKRRMRYF.
OrthoDBiEOG7M0NRD.
PhylomeDBiP15384.
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.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004050. K_chnl_volt-dep_Kv1.3.
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.
PR01510. KV13CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

P15384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVVPGDHLL EPEAAGGGGG DPPQGGCVSG GGCDRYEPLP PALPAAGEQD
60 70 80 90 100
CCGERVVINI SGLRFETQLK TLCQFPETLL GDPKRRMRYF DPLRNEYFFD
110 120 130 140 150
RNRPSFDAIL YYYQSGGRIR RPVNVPIDIF SEEIRFYQLG EEAMEKFRED
160 170 180 190 200
EGFLREEERP LPRRDFQRQV WLLFEYPESS GPARGIAIVS VLVILISIVI
210 220 230 240 250
FCLETLPEFR DEKDYPASPS QDVFEAANNS TSGASSGASS FSDPFFVVET
260 270 280 290 300
LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER
310 320 330 340 350
QGNGQQAMSL AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL
360 370 380 390 400
LIFFLFIGVI LFSSAVYFAE ADDPSSGFNS IPDAFWWAVV TMTTVGYGDM
410 420 430 440 450
HPVTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE TEGEEQAQYM
460 470 480 490 500
HVGSCQHLSS SAEELRKARS NSTLSKSEYM VIEEGGMNHS AFPQTPFKTG
510 520
NSTATCTTNN NPNSCVNIKK IFTDV
Length:525
Mass (Da):58,425
Last modified:November 1, 1990 - v2
Checksum:i6DA8869D5471C401
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1061F → L in CAA34132 (PubMed:2555158).Curated
Sequence conflicti181 – 1811G → R in AAA42035 (PubMed:2351830).Curated
Sequence conflicti430 – 4301V → L in AAA42035 (PubMed:2351830).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16001 mRNA. Translation: CAA34132.1.
M30312 Genomic DNA. Translation: AAA42035.1.
M31744 Genomic DNA. Translation: AAA41500.1.
PIRiA43531.
RefSeqiNP_062143.3. NM_019270.3.
UniGeneiRn.44292.

Genome annotation databases

GeneIDi29731.
KEGGirno:29731.
UCSCiRGD:2951. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16001 mRNA. Translation: CAA34132.1.
M30312 Genomic DNA. Translation: AAA42035.1.
M31744 Genomic DNA. Translation: AAA41500.1.
PIRiA43531.
RefSeqiNP_062143.3. NM_019270.3.
UniGeneiRn.44292.

3D structure databases

ProteinModelPortaliP15384.
SMRiP15384. Positions 54-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248344. 1 interaction.
IntActiP15384. 1 interaction.
STRINGi10116.ENSRNOP00000024372.

Chemistry

ChEMBLiCHEMBL4248.
GuidetoPHARMACOLOGYi540.

Proteomic databases

PaxDbiP15384.
PRIDEiP15384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29731.
KEGGirno:29731.
UCSCiRGD:2951. rat.

Organism-specific databases

CTDi3738.
RGDi2951. Kcna3.

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP15384.
KOiK04876.
OMAiKRRMRYF.
OrthoDBiEOG7M0NRD.
PhylomeDBiP15384.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_352543. Voltage gated Potassium channels.

Miscellaneous databases

NextBioi610214.
PROiP15384.

Gene expression databases

ExpressionAtlasiP15384. baseline and differential.
GenevisibleiP15384. 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.
IPR003972. K_chnl_volt-dep_Kv1.
IPR004050. K_chnl_volt-dep_Kv1.3.
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.
PR01510. KV13CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain."
    Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B., Stocker M., Giese K.P., Perschke A., Baumann A., Pongs O.
    EMBO J. 8:3235-3244(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Cloning and expression of cDNA and genomic clones encoding three delayed rectifier potassium channels in rat brain."
    Swanson R., Marshall J., Smith J., Williams J., Boyle M.B., Folander K., Luneau C.J., Antanavage J., Oliva C., Buhrow S.A., Bennett C., Stein R.B., Kaczmarek L.M.
    Neuron 4:929-939(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Brain.
  3. "Characterization and functional expression of a rat genomic DNA clone encoding a lymphocyte potassium channel."
    Douglass J., Osborne P.B., Cai Y.C., Wilkinson M., Christie M.J., Adelman J.P.
    J. Immunol. 144:4841-4850(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lymphocyte.
  4. "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases."
    Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.
    Nature 378:85-88(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG1; DLG2 AND DLG4.
  5. "N-glycosylation promotes the cell surface expression of Kv1.3 potassium channels."
    Zhu J., Yan J., Thornhill W.B.
    FEBS J. 279:2632-2644(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-229, ABSENCE OF GLYCOSYLATION AT ASN-228, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiKCNA3_RAT
AccessioniPrimary (citable) accession number: P15384
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1990
Last modified: July 22, 2015
This is version 134 of the entry and version 2 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.