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Q62897 (KCND3_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily D member 3
Alternative name(s):
Voltage-gated potassium channel subunit Kv4.3
Gene names
Name:Kcnd3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. Ref.1 Ref.2 Ref.3 Ref.4

Subunit structure

Homotetramer or heterotetramer with KCND1 and/or KCND2. Interacts with DLG1. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Interacts with KCNE1, KCNE2, SCN1B and KCNAB1 By similarity. Ref.7 Ref.9 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell membranesarcolemma. Cell projectiondendrite By similarity. Note: Interaction with palmitoylated KCNIP2 and KCNIP3 enhances cell surface expression. Ref.8 Ref.11

Tissue specificity

Highly expressed in brain, in particular in the retrosplenial cortex, medial habenula, anterior thalamus, hippocampus, cerebellum and lateral geniculate and superior colliculus. Highly expressed in heart atrium (at protein level) and throughout the ventricle wall, in lung and vas deferens. Ref.1 Ref.2 Ref.3 Ref.4 Ref.11

Domain

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

Regulated through phosphorylation at Ser-569 by CaMK2D.

Sequence similarities

Belongs to the potassium channel family. D (Shal) (TC 1.A.1.2) subfamily. Kv4.3/KCND3 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandMetal-binding
Potassium
Zinc
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmembrane repolarization

Inferred from electronic annotation. Source: Ensembl

potassium ion export

Inferred from electronic annotation. Source: Ensembl

potassium ion transport

Traceable author statement PubMed 10325948. Source: RGD

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentdendrite

Inferred from direct assay PubMed 20849929. Source: RGD

integral component of plasma membrane

Inferred from direct assay PubMed 10325948. Source: RGD

neuron projection

Inferred from direct assay PubMed 15738276. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 15738276PubMed 20849929. Source: RGD

perinuclear endoplasmic reticulum

Inferred from direct assay PubMed 12967630. Source: RGD

plasma membrane

Inferred from direct assay PubMed 12967630. Source: RGD

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

voltage-gated potassium channel complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionA-type (transient outward) potassium channel activity

Inferred from mutant phenotype PubMed 12150935. Source: RGD

ion channel activity

Inferred from direct assay PubMed 10325948. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

potassium channel activity

Inferred from direct assay PubMed 10325948. Source: RGD

protein binding

Inferred from physical interaction PubMed 10794667PubMed 18565539PubMed 20849929PubMed 21147063. Source: RGD

voltage-gated potassium channel activity

Inferred from direct assay PubMed 10325948PubMed 12967630. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q62897-1)

Also known as: Kv4.3 long form;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q62897-2)

The sequence of this isoform differs from the canonical sequence as follows:
     488-506: Missing.
Isoform 3 (identifier: Q62897-3)

The sequence of this isoform differs from the canonical sequence as follows:
     488-506: Missing.
     608-655: SQITTAIISIPTPPALTPEGESRPPPASPGPNTNIPSITSNVVKVSVL → QDQEQPRGRVVTCKQEEIITLCI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655Potassium voltage-gated channel subfamily D member 3
PRO_0000054071

Regions

Topological domain1 – 181181Cytoplasmic Potential
Transmembrane182 – 20221Helical; Name=Segment S1; Potential
Transmembrane222 – 24221Helical; Name=Segment S2; Potential
Topological domain243 – 25614Cytoplasmic Potential
Transmembrane257 – 27721Helical; Name=Segment S3; Potential
Transmembrane287 – 30721Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain308 – 32013Cytoplasmic Potential
Transmembrane321 – 34121Helical; Name=Segment S5; Potential
Intramembrane360 – 38021Pore-forming; Name=Segment H5; Potential
Transmembrane382 – 40221Helical; Name=Segment S6; Potential
Topological domain403 – 655253Cytoplasmic Potential
Region2 – 2019Interaction with KCNIP2 By similarity
Region474 – 48916Mediates dendritic targeting By similarity
Motif367 – 3726Selectivity filter By similarity

Sites

Metal binding1041Zinc By similarity
Metal binding1311Zinc By similarity
Metal binding1321Zinc By similarity

Amino acid modifications

Modified residue5691Phosphoserine; by CaMK2D Ref.10

Natural variations

Alternative sequence488 – 50619Missing in isoform 2 and isoform 3.
VSP_008831
Alternative sequence608 – 65548SQITT…KVSVL → QDQEQPRGRVVTCKQEEIIT LCI in isoform 3.
VSP_008832

Experimental info

Sequence conflict1241L → H in AAA80459. Ref.3
Sequence conflict4041S → T in AAC52695. Ref.2
Sequence conflict4041S → T in AAK07651. Ref.5
Sequence conflict5691S → T in AAA80459. Ref.3
Sequence conflict6311P → A in AAC52695. Ref.2
Sequence conflict6541V → A in AAB18337. Ref.1
Sequence conflict6541V → A in BAA24525. Ref.4

Secondary structure

....................... 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Kv4.3 long form) [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: 26BC512BDE069C09

FASTA65573,513
        10         20         30         40         50         60 
MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKNKRQDE LIVLNVSGRR FQTWRTTLER 

        70         80         90        100        110        120 
YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT GKLHYPRYEC ISAYDDELAF 

       130        140        150        160        170        180 
YGILPEIIGD CCYEEYKDRK RENAERLMDD NESENNQESM PSLSFRQTMW RAFENPHTST 

       190        200        210        220        230        240 
LALVFYYVTG FFIAVSVITN VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE 

       250        260        270        280        290        300 
YLLRLFAAPS RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF 

       310        320        330        340        350        360 
SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK FTSIPASFWY 

       370        380        390        400        410        420 
TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP VIVSNFSRIY HQNQRADKRR 

       430        440        450        460        470        480 
AQKKARLARI RVAKTGSSNA YLHSKRNGLL NEALELTGTP EEEHMGKTTS LIESQHHHLL 

       490        500        510        520        530        540 
HCLEKTTGLS YLVDDPLLSV RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHS 

       550        560        570        580        590        600 
GLTTTCCSRR SKKTTHLPNS NLPATRLRSM QELSTIHIQG SEQPSLTTSR SSLNLKADDG 

       610        620        630        640        650 
LRPNCKTSQI TTAIISIPTP PALTPEGESR PPPASPGPNT NIPSITSNVV KVSVL 

« Hide

Isoform 2 [UniParc].

Checksum: A2D65B7C3FA5A58A
Show »

FASTA63671,454
Isoform 3 [UniParc].

Checksum: 0D6042030E46F4C1
Show »

FASTA61169,294

References

[1]"Role of the Kv4.3 K+ channel in ventricular muscle. A molecular correlate for the transient outward current."
Dixon J.E., Shi W., Wang H.-S., McDonald C., Yu H., Wymore R.S., Cohen I.S., McKinnon D.
Circ. Res. 79:659-668(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
[2]"Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain."
Serodio P., Vega-Saenz de Miera E., Rudy B.
J. Neurophysiol. 75:2174-2179(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain.
[3]"Cloning, expression and CNS distribution of Kv4.3, an A-type K+ channel alpha subunit."
Tsaur M.-L., Chou C.-C., Shih Y.-H., Wang H.-L.
FEBS Lett. 400:215-220(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
Tissue: Hippocampus.
[4]"Molecular cloning and tissue distribution of an alternatively spliced variant of an A-type K+ channel alpha-subunit, Kv4.3 in the rat."
Ohya S., Tanaka M., Oku T., Asai Y., Watanabe M., Giles W.R., Imaizumi Y.
FEBS Lett. 420:47-53(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Smooth muscle and Vas deferens.
[5]"Remodeling of Kv4.3 potassium channel gene expression under the control of sex hormones."
Song M., Helguera G., Eghbali M., Zhu N., Zarei M.M., Olcese R., Toro L., Stefani E.
J. Biol. Chem. 276:31883-31890(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Strain: Sprague-Dawley.
Tissue: Uterus.
[6]"Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit mRNAs in ventricles of renovascular hypertensive rats."
Takimoto K., Li D., Hershman K.M., Li P., Jackson E.K., Levitan E.S.
Circ. Res. 81:533-539(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 455-606 (ISOFORM 1).
Strain: Sprague-Dawley.
[7]"Modulation of A-type potassium channels by a family of calcium sensors."
An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G., Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.
Nature 403:553-556(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3.
[8]"Palmitoylation of KChIP splicing variants is required for efficient cell surface expression of Kv4.3 channels."
Takimoto K., Yang E.-K., Conforti L.
J. Biol. Chem. 277:26904-26911(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"Elimination of fast inactivation in Kv4 A-type potassium channels by an auxiliary subunit domain."
Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., Carroll K.I., Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., Jurman M.E., Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., Rhodes K.J., Distefano P.S., An W.F.
Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP4.
[10]"Regulation of Kv4.3 currents by Ca2+/calmodulin-dependent protein kinase II."
Sergeant G.P., Ohya S., Reihill J.A., Perrino B.A., Amberg G.C., Imaizumi Y., Horowitz B., Sanders K.M., Koh S.D.
Am. J. Physiol. 288:C304-C313(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-569 BY CAMK2D.
[11]"Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes."
El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N.
Circ. Res. 104:758-769(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[12]"Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer."
Pioletti M., Findeisen F., Hura G.L., Minor D.L. Jr.
Nat. Struct. Mol. Biol. 13:987-995(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 2-143 IN COMPLEX WITH KCNIP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U75448 mRNA. Translation: AAB18337.1.
U42975 mRNA. Translation: AAC52695.1.
L48619 mRNA. Translation: AAA80459.1.
AB003587 mRNA. Translation: BAA24525.1.
AF334791 mRNA. Translation: AAK07651.1.
U92897 mRNA. Translation: AAB53321.1.
RefSeqNP_001257891.1. NM_001270962.1.
NP_001257892.1. NM_001270963.1.
NP_113927.2. NM_031739.3. [Q62897-3]
UniGeneRn.10540.
Rn.214215.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I2RX-ray3.35A/B/C/D/I/J/K/L2-143[»]
ProteinModelPortalQ62897.
SMRQ62897. Positions 3-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29245N.
IntActQ62897. 1 interaction.
MINTMINT-103596.

Chemistry

GuidetoPHARMACOLOGY554.

PTM databases

PhosphoSiteQ62897.

Proteomic databases

PaxDbQ62897.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000019997; ENSRNOP00000019997; ENSRNOG00000014686.
ENSRNOT00000051835; ENSRNOP00000049111; ENSRNOG00000014686.
GeneID65195.
KEGGrno:65195.
UCSCRGD:68394. rat. [Q62897-1]

Organism-specific databases

CTD3752.
RGD68394. Kcnd3.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00740000115211.
HOGENOMHOG000231013.
HOVERGENHBG106687.
InParanoidQ62897.
KOK04893.
PhylomeDBQ62897.
TreeFamTF313103.

Gene expression databases

GenevestigatorQ62897.

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.
IPR003975. K_chnl_volt-dep_Kv4.
IPR004056. K_chnl_volt-dep_Kv4.3.
IPR024587. K_chnl_volt-dep_Kv4_C.
IPR021645. Shal-type.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF11879. DUF3399. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11601. Shal-type. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01518. KV43CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ62897.
NextBio614128.
PROQ62897.

Entry information

Entry nameKCND3_RAT
AccessionPrimary (citable) accession number: Q62897
Secondary accession number(s): O08723 expand/collapse secondary AC list , P70622, Q63286, Q99P42
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 7, 2003
Last modified: July 9, 2014
This is version 123 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references