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Q63881 (KCND2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 128. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily D member 2
Alternative name(s):
RK5
Shal1
Voltage-gated potassium channel subunit Kv4.2
Gene names
Name:Kcnd2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length630 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

Subunit structure

Homotetramer or heterotetramer with KCND1 and/or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3and KCND2. The KCND2-KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits. Interacts with FLNA and FLNC By similarity. Interacts with DPP6, DPP10, DLG4, NCS1/FREQ and DLG1. Ref.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell projectiondendrite. Note: Interaction with DPP6, DLG4 or NCS1/FREQ may increase cell surface expression. Localized preferentially to the dendrites of pyramidal cells. Ref.8

Tissue specificity

Highly expressed in heart and throughout the brain, with similar levels in cortex and hypothalamus, and much higher levels in hippocampus, dentate gyrus and the habenular nucleus of the thalamus. Detected at similar levels in heart atrium and ventricle. Detected in aorta, cardiac and smooth muscle. Ref.1 Ref.2

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

Phosphorylated on serine and threonine residues By similarity. Ref.7

Sequence similarities

Belongs to the potassium channel family. D (Shal) (TC 1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily. [View classification]

Sequence caution

The sequence AAA40929.1 differs from that shown. Reason: Frameshift at position 477.

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentCell membrane
Cell projection
Membrane
   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_processaction potential

Inferred from mutant phenotype PubMed 16141270. Source: RGD

potassium ion transport

Traceable author statement PubMed 10330244. Source: RGD

protein heterooligomerization

Inferred from direct assay PubMed 16123112. Source: RGD

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentdendrite

Inferred from direct assay Ref.10PubMed 15736227. Source: RGD

dendritic spine

Inferred from direct assay PubMed 16141270. Source: RGD

integral component of plasma membrane

Inferred from direct assay PubMed 10330244. Source: RGD

neuron projection

Inferred from direct assay PubMed 17635915. Source: RGD

neuronal cell body

Inferred from direct assay PubMed 15736227PubMed 20849929. Source: RGD

perinuclear endoplasmic reticulum

Inferred from direct assay PubMed 12967630. Source: RGD

plasma membrane

Inferred from direct assay PubMed 12967630PubMed 15736227. Source: RGD

postsynaptic density

Inferred from direct assay PubMed 17635915. Source: RGD

potassium channel complex

Inferred from direct assay Ref.15. Source: RGD

voltage-gated potassium channel complex

Inferred from direct assay Ref.10PubMed 16123112. Source: RGD

   Molecular_functionA-type (transient outward) potassium channel activity

Inferred from mutant phenotype PubMed 16123112. 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 10325948PubMed 12403671. Source: RGD

protein binding

Inferred from physical interaction PubMed 11805342Ref.9Ref.15Ref.10PubMed 16123112PubMed 18565539PubMed 20849929PubMed 21147063. Source: RGD

protein heterodimerization activity

Inferred from direct assay Ref.15. Source: RGD

voltage-gated potassium channel activity

Inferred from direct assay PubMed 10325948PubMed 12967630Ref.15. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 630630Potassium voltage-gated channel subfamily D member 2
PRO_0000054067

Regions

Topological domain1 – 183183Cytoplasmic Potential
Transmembrane184 – 20421Helical; Name=Segment S1; Potential
Transmembrane225 – 24521Helical; Name=Segment S2; Potential
Topological domain246 – 25914Cytoplasmic Potential
Transmembrane260 – 28021Helical; Name=Segment S3; Potential
Transmembrane290 – 31021Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain311 – 32313Cytoplasmic Potential
Transmembrane324 – 34421Helical; Name=Segment S5; Potential
Intramembrane363 – 38321Pore-forming; Name=Segment H5; Potential
Transmembrane385 – 40521Helical; Name=Segment S6; Potential
Topological domain406 – 630225Cytoplasmic Potential
Region2 – 2019Interaction with KCNIP2 By similarity
Region7 – 115Interaction with KCNIP1
Region71 – 9020Interaction with KCNIP1
Region474 – 48916Mediates dendritic targeting
Motif370 – 3756Selectivity filter By similarity

Sites

Metal binding1051Zinc By similarity
Metal binding1321Zinc By similarity
Metal binding1331Zinc By similarity

Amino acid modifications

Modified residue381Phosphothreonine By similarity
Modified residue5521Phosphoserine Ref.7
Modified residue6021Phosphothreonine By similarity
Modified residue6071Phosphothreonine By similarity
Modified residue6161Phosphoserine By similarity

Experimental info

Mutagenesis7 – 115Missing: Greatly reduces interaction with KCNIP1. Ref.11 Ref.15
Mutagenesis81W → A: Abolishes interaction with KCNP1; when associated with A-11. Ref.15
Mutagenesis111F → A: Abolishes interaction with KCNP1; when associated with A-8. Ref.15
Mutagenesis661L → R: Abolishes expression. Ref.14
Mutagenesis711E → K: Abolishes interaction with KCNIP1. Ref.11
Mutagenesis731D → M: Abolishes interaction with KCNIP1. Ref.11
Mutagenesis741F → R: Abolishes interaction with KCNIP1. Ref.11
Mutagenesis791E → L or R: Abolishes interaction with KCNIP1. Ref.11
Mutagenesis931R → A: Greatly reduces expression and changes multimerization. Ref.14
Mutagenesis481 – 4822Missing: Loss of dendritic targeted expression. Ref.8
Mutagenesis627 – 6304Missing: Abolishes interaction with DLG4. Ref.6

Secondary structure

........................ 630
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q63881 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: FDE57E8A5113BABF

FASTA63070,549
        10         20         30         40         50         60 
MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE 

        70         80         90        100        110        120 
RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR TGKLHYPRHE CISAYDEELA 

       130        140        150        160        170        180 
FFGLIPEIIG DCCYEEYKDR RRENAERLQD DADTDNTGES ALPTMTARQR VWRAFENPHT 

       190        200        210        220        230        240 
STMALVFYYV TGFFIAVSVI ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF 

       250        260        270        280        290        300 
TVEYLLRLAA APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI 

       310        320        330        340        350        360 
FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS ASKFTSIPAA 

       370        380        390        400        410        420 
FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD 

       430        440        450        460        470        480 
KRRAQKKARL ARIRAAKSGS ANAYMQSKRN GLLSNQLQSS EDEPAFVSKS GSSFETQHHH 

       490        500        510        520        530        540 
LLHCLEKTTN HEFVDEQVFE ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKSFRI 

       550        560        570        580        590        600 
PNANVSGSHR GSVQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI 

       610        620        630 
PTPPVTTPEG DDRPESPEYS GGNIVRVSAL 

« Hide

References

[1]"Characterization of a mammalian cDNA for an inactivating voltage-sensitive K+ channel."
Baldwin T.J., Tsaur M.-L., Lopez G.A., Jan Y.N., Jan L.Y.
Neuron 7:471-483(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Hippocampus.
[2]"Cloning and tissue-specific expression of five voltage-gated potassium channel cDNAs expressed in rat heart."
Roberds S.L., Tamkun M.M.
Proc. Natl. Acad. Sci. U.S.A. 88:1798-1802(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Heart.
[3]"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.
[4]"A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents."
Nakamura T.Y., Pountney D.J., Ozaita A., Nandi S., Ueda S., Rudy B., Coetzee W.A.
Proc. Natl. Acad. Sci. U.S.A. 98:12808-12813(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP1 AND NCS1.
[5]"Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4."
Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T.
J. Biol. Chem. 277:14965-14975(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP4.
[6]"Cell surface targeting and clustering interactions between heterologously expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2."
Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C.
J. Biol. Chem. 277:20423-20430(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 627-VAL--LEU-630, INTERACTION WITH DLG4.
[7]"A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels."
Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A., Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.
J. Biol. Chem. 278:36445-36454(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-552.
[8]"An evolutionarily conserved dileucine motif in Shal K+ channels mediates dendritic targeting."
Rivera J.F., Ahmad S., Quick M.W., Liman E.R., Arnold D.B.
Nat. Neurosci. 6:243-250(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DENDRITIC TARGETING REGION, MUTAGENESIS OF 481-LEU--LEU-482.
[9]"The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical component of neuronal A-type K+ channels."
Nadal M.S., Ozaita A., Amarillo Y., Vega-Saenz de Miera E., Ma Y., Mo W., Goldberg E.M., Misumi Y., Ikehara Y., Neubert T.A., Rudy B.
Neuron 37:449-461(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPP6.
[10]"KChIPs and Kv4 alpha subunits as integral components of A-type potassium channels in mammalian brain."
Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M., Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F., Trimmer J.S.
J. Neurosci. 24:7903-7915(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP1 AND KCNIP3.
[11]"Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1."
Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W., Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L., Taylor M., Stahl M., Malakian K., Somers W., Mosyak L. expand/collapse author list , Bowlby M.R., Chanda P., Rhodes K.J.
Neuron 41:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP1, MUTAGENESIS OF 7-ALA--PHE-11; GLU-71; ASP-73; PHE-74 AND GLU-79.
[12]"DPP10 modulates Kv4-mediated A-type potassium channels."
Zagha E., Ozaita A., Chang S.Y., Nadal M.S., Lin U., Saganich M.J., McCormack T., Akinsanya K.O., Qi S.Y., Rudy B.
J. Biol. Chem. 280:18853-18861(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DPP6 AND DPP10.
[13]"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.
[14]"Determining the basis of channel-tetramerization specificity by X-ray crystallography and a sequence-comparison algorithm: family values (FamVal)."
Nanao M.H., Zhou W., Pfaffinger P.J., Choe S.
Proc. Natl. Acad. Sci. U.S.A. 100:8670-8675(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 42-146, MUTAGENESIS OF LEU-66 AND ARG-93.
[15]"Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels."
Zhou W., Qian Y., Kunjilwar K., Pfaffinger P.J., Choe S.
Neuron 41:573-586(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-30, INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3, MUTAGENESIS OF TRP-8 AND PHE-11.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S64320 mRNA. Translation: AAB19939.1.
M59980 mRNA. Translation: AAA40929.1. Frameshift.
PIRI57681.
JU0271.
RefSeqNP_113918.2. NM_031730.2.
UniGeneRn.87841.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NN7X-ray2.10A42-146[»]
1S6CX-ray2.00B1-30[»]
ProteinModelPortalQ63881.
SMRQ63881. Positions 3-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249292. 2 interactions.
IntActQ63881. 3 interactions.
MINTMINT-104113.
STRING10116.ENSRNOP00000039227.

Chemistry

ChEMBLCHEMBL1075227.
GuidetoPHARMACOLOGY553.

PTM databases

PhosphoSiteQ63881.

Proteomic databases

PaxDbQ63881.
PRIDEQ63881.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID65180.
KEGGrno:65180.
UCSCRGD:68393. rat.

Organism-specific databases

CTD3751.
RGD68393. Kcnd2.

Phylogenomic databases

eggNOGCOG1226.
HOGENOMHOG000231013.
HOVERGENHBG106687.
InParanoidQ63881.
KOK04892.
PhylomeDBQ63881.

Gene expression databases

GenevestigatorQ63881.

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.
IPR004055. K_chnl_volt-dep_Kv4.2.
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.
PR01517. KV42CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ63881.
NextBio614080.
PROQ63881.

Entry information

Entry nameKCND2_RAT
AccessionPrimary (citable) accession number: Q63881
Secondary accession number(s): Q00090, Q99249
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 1, 1996
Last modified: June 11, 2014
This is version 128 of the entry and version 1 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