Potassium voltage-gated channel subfamily A member 3

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P15384 (KCNA3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:

Kcna3

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Evidence 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]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Potassium
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein homooligomerization Inferred from electronic annotation. Source: InterPro
Cellular_component	membrane raft Inferred from direct assay PubMed 18218624. Source: BHF-UCL plasma membrane Inferred from direct assay PubMed 18218624. Source: BHF-UCL voltage-gated potassium channel complex Inferred from electronic annotation. Source: InterPro
Molecular_function	delayed rectifier potassium channel activity Inferred from mutant phenotype PubMed 14602579. Source: RGD outward rectifier potassium channel activity Inferred from mutant phenotype PubMed 14602579. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DLG4	P78352	2	EBI-631478,EBI-80389	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 525

525

Potassium voltage-gated channel subfamily A member 3

PRO_0000053979

Regions

Topological domain

1 – 184

184

Cytoplasmic Potential

Transmembrane

185 – 203

Helical; Name=Segment S1; Potential

Topological domain

204 – 244

Extracellular Potential

Transmembrane

245 – 266

Helical; Name=Segment S2; Potential

Topological domain

267 – 277

Cytoplasmic Potential

Transmembrane

278 – 298

Helical; Name=Segment S3; Potential

Topological domain

299 – 312

Extracellular Potential

Transmembrane

313 – 331

Helical; Voltage-sensor; Name=Segment S4; Potential

Topological domain

332 – 347

Cytoplasmic Potential

Transmembrane

348 – 367

Helical; Name=Segment S5; Potential

Topological domain

368 – 408

Extracellular Potential

Transmembrane

409 – 431

Helical; Name=Segment S6; Potential

Topological domain

432 – 525

Cytoplasmic Potential

Motif

394 – 399

Selectivity filter By similarity

Motif

523 – 525

PDZ-binding

Sites

Site

228

Not glycosylated

Amino acid modifications

Modified residue

470

Phosphoserine; by PKA Potential

Lipidation

267

S-palmitoyl cysteine Potential

Glycosylation

229

N-linked (GlcNAc...) Ref.5

Experimental info

Sequence conflict

106

F → L in CAA34132. Ref.1

Sequence conflict

181

G → R in AAA42035. Ref.3

Sequence conflict

430

V → L in AAA42035. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P15384 [UniParc].

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

FASTA

525

58,425

        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.
IPI	IPI00208359.
PIR	A43531.
RefSeq	NP_062143.3. NM_019270.3.
UniGene	Rn.44292.
3D structure databases
ProteinModelPortal	P15384.
SMR	P15384. Positions 54-441.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15384. 1 interaction.
STRING	10116.ENSRNOP00000024372.
Proteomic databases
PaxDb	P15384.
PRIDE	P15384.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000024372; ENSRNOP00000024372; ENSRNOG00000018116.
GeneID	29731.
KEGG	rno:29731.
UCSC	RGD:2951. rat.
Organism-specific databases
CTD	3738.
RGD	2951. Kcna3.
Phylogenomic databases
eggNOG	COG1226.
GeneTree	ENSGT00560000076957.
HOGENOM	HOG000231015.
HOVERGEN	HBG052230.
InParanoid	P15384.
KO	K04876.
OMA	CDRYEPL.
OrthoDB	EOG4QC155.
Gene expression databases
ArrayExpress	P15384.
Genevestigator	P15384.
GermOnline	ENSRNOG00000018116. Rattus norvegicus.
Family and domain databases
Gene3D	1.20.120.350. 1 hit. 3.30.710.10. 1 hit.
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR005821. Ion_trans_dom. IPR027359. K_channel_four-helix_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. [Graphical view]
PANTHER	PTHR11537. PTHR11537. 1 hit.
Pfam	PF00520. Ion_trans. 1 hit. PF02214. K_tetra. 1 hit. [Graphical view]
PRINTS	PR00169. KCHANNEL. PR01510. KV13CHANNEL. PR01491. KVCHANNEL. PR01496. SHAKERCHANEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
ChEMBL	CHEMBL4248.
NextBio	610214.

Entry information

Entry name

KCNA3_RAT

Accession

Primary (citable) accession number: P15384

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 29, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents