Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P15384 (KCNA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Kcna3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length525 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.5.

Domain

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.

Post-translational modification

N-glycosylation promotes the cell surface expression.

Sequence similarities

Belongs to the potassium channel family. A (Shaker) (TC 1.A.1.2) subfamily. Kv1.3/KCNA3 sub-subfamily. [View classification]

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DLG4P783522EBI-631478,EBI-80389From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 525525Potassium voltage-gated channel subfamily A member 3
PRO_0000053979

Regions

Topological domain1 – 184184Cytoplasmic Potential
Transmembrane185 – 20319Helical; Name=Segment S1; Potential
Topological domain204 – 24441Extracellular Potential
Transmembrane245 – 26622Helical; Name=Segment S2; Potential
Topological domain267 – 27711Cytoplasmic Potential
Transmembrane278 – 29821Helical; Name=Segment S3; Potential
Topological domain299 – 31214Extracellular Potential
Transmembrane313 – 33119Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain332 – 34716Cytoplasmic Potential
Transmembrane348 – 36720Helical; Name=Segment S5; Potential
Topological domain368 – 40841Extracellular Potential
Transmembrane409 – 43123Helical; Name=Segment S6; Potential
Topological domain432 – 52594Cytoplasmic Potential
Motif394 – 3996Selectivity filter By similarity
Motif523 – 5253PDZ-binding

Sites

Site2281Not glycosylated

Amino acid modifications

Modified residue4701Phosphoserine; by PKA Potential
Lipidation2671S-palmitoyl cysteine Potential
Glycosylation2291N-linked (GlcNAc...) Ref.5

Experimental info

Sequence conflict1061F → L in CAA34132. Ref.1
Sequence conflict1811G → R in AAA42035. Ref.3
Sequence conflict4301V → L in AAA42035. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P15384 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 6DA8869D5471C401

FASTA52558,425
        10         20         30         40         50         60 
MTVVPGDHLL EPEAAGGGGG DPPQGGCVSG GGCDRYEPLP PALPAAGEQD CCGERVVINI 

        70         80         90        100        110        120 
SGLRFETQLK TLCQFPETLL GDPKRRMRYF DPLRNEYFFD RNRPSFDAIL YYYQSGGRIR 

       130        140        150        160        170        180 
RPVNVPIDIF SEEIRFYQLG EEAMEKFRED EGFLREEERP LPRRDFQRQV WLLFEYPESS 

       190        200        210        220        230        240 
GPARGIAIVS VLVILISIVI FCLETLPEFR DEKDYPASPS QDVFEAANNS TSGASSGASS 

       250        260        270        280        290        300 
FSDPFFVVET LCIIWFSFEL LVRFFACPSK ATFSRNIMNL IDIVAIIPYF ITLGTELAER 

       310        320        330        340        350        360 
QGNGQQAMSL AILRVIRLVR VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI 

       370        380        390        400        410        420 
LFSSAVYFAE ADDPSSGFNS IPDAFWWAVV TMTTVGYGDM HPVTIGGKIV GSLCAIAGVL 

       430        440        450        460        470        480 
TIALPVPVIV SNFNYFYHRE TEGEEQAQYM HVGSCQHLSS SAEELRKARS NSTLSKSEYM 

       490        500        510        520 
VIEEGGMNHS AFPQTPFKTG NSTATCTTNN NPNSCVNIKK IFTDV 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16001 mRNA. Translation: CAA34132.1.
M30312 Genomic DNA. Translation: AAA42035.1.
M31744 Genomic DNA. Translation: AAA41500.1.
PIRA43531.
RefSeqNP_062143.3. NM_019270.3.
UniGeneRn.44292.

3D structure databases

ProteinModelPortalP15384.
SMRP15384. Positions 54-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP15384. 1 interaction.
STRING10116.ENSRNOP00000024372.

Chemistry

ChEMBLCHEMBL4248.
GuidetoPHARMACOLOGY540.

Proteomic databases

PaxDbP15384.
PRIDEP15384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000024372; ENSRNOP00000024372; ENSRNOG00000018116.
GeneID29731.
KEGGrno:29731.
UCSCRGD:2951. rat.

Organism-specific databases

CTD3738.
RGD2951. Kcna3.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000115256.
HOGENOMHOG000231015.
HOVERGENHBG052230.
InParanoidP15384.
KOK04876.
OMAKRRMRYF.
OrthoDBEOG7M0NRD.
PhylomeDBP15384.
TreeFamTF313103.

Gene expression databases

GenevestigatorP15384.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. 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]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01510. KV13CHANNEL.
PR01491. KVCHANNEL.
PR01496. SHAKERCHANEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

NextBio610214.
PROP15384.

Entry information

Entry nameKCNA3_RAT
AccessionPrimary (citable) accession number: P15384
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families