Potassium voltage-gated channel subfamily D member 2 - KCND2

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Q9NZV8 (KCND2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. History...

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

Documents (3) |

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 D member 2

Alternative name(s):
Voltage-gated potassium channel subunit Kv4.2

Gene names

Name:	KCND2
Synonyms:	KIAA1044

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Protein existence	Evidence 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.3 Ref.4
Subunit structure	Homotetramer or heterotetramer with KCND1 and/or KCND3. Interacts with DPP6, DLG4 and NCS1/FREQ By similarity. Interacts with DLG1. 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, FLNC and DPP10. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16 Ref.17
Subcellular location	Cell membrane; Multi-pass membrane protein. Cell projection › dendrite. Note: Detected in dendrites in cultured hippocampal neurons. Association with KCNIP2 probably enhances cell surface expression. Ref.7
Tissue specificity	Highly expressed throughout the brain. Expression is very low or absent in other tissues. Ref.3 Ref.4
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.
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 BAA82996.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cell membrane Cell projection Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Metal-binding Potassium Zinc
Molecular function	Ion channel Potassium channel Voltage-gated channel
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	action potential Traceable author statement Ref.7. Source: UniProtKB protein homooligomerization Inferred from electronic annotation. Source: InterPro synaptic transmission Traceable author statement Ref.7. Source: UniProtKB
Cellular_component	dendritic spine Non-traceable author statement Ref.7. Source: UniProtKB plasma membrane Traceable author statement. Source: Reactome voltage-gated potassium channel complex Inferred from electronic annotation. Source: InterPro
Molecular_function	A-type (transient outward) potassium channel activity Inferred from Biological aspect of Ancestor. Source: RefGenome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.9. Source: UniProtKB voltage-gated potassium channel activity Non-traceable author statement Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KCNIP1	Q9NZI2	4	EBI-1646745,EBI-2120635
KCNIP2	Q9NS61-3	3	EBI-1646745,EBI-1053010

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 630

630

Potassium voltage-gated channel subfamily D member 2

PRO_0000054064

Regions

Topological domain

1 – 183

183

Cytoplasmic Potential

Transmembrane

184 – 204

Helical; Name=Segment S1; Potential

Transmembrane

225 – 245

Helical; Name=Segment S2; Potential

Topological domain

246 – 259

Cytoplasmic Potential

Transmembrane

260 – 280

Helical; Name=Segment S3; Potential

Transmembrane

290 – 310

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

Topological domain

311 – 323

Cytoplasmic Potential

Transmembrane

324 – 344

Helical; Name=Segment S5; Potential

Intramembrane

363 – 383

Pore-forming; Name=Segment H5; Potential

Transmembrane

385 – 405

Helical; Name=Segment S6; Potential

Topological domain

406 – 630

225

Cytoplasmic Potential

Region

2 – 20

Interaction with KCNIP2

Region

7 – 11

Interaction with KCNIP1 By similarity

Region

71 – 90

Interaction with KCNIP1 By similarity

Region

474 – 489

Mediates dendritic targeting By similarity

Motif

370 – 375

Selectivity filter By similarity

Sites

Metal binding

105

Zinc By similarity

Metal binding

132

Zinc By similarity

Metal binding

133

Zinc By similarity

Amino acid modifications

Modified residue

Phosphothreonine By similarity

Modified residue

552

Phosphoserine By similarity

Modified residue

602

Phosphothreonine By similarity

Modified residue

607

Phosphothreonine By similarity

Modified residue

616

Phosphoserine By similarity

Experimental info

Mutagenesis

601 – 604

PTPP → ATAA: Abolishes interaction with FLNC. Ref.7

Sequence conflict

450

N → S in AAD22053. Ref.1

Sequence conflict

464

Q → P in AAD22053. Ref.1

Sequence conflict

550

Q → R in AAD22053. Ref.1

Sequence conflict

553

I → V in AAD22053. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

Q9NZV8 [UniParc].

Last modified November 7, 2003. Version 2.
Checksum: 0C11E62FFA220421
Show »

FASTA

630

70,537

        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 DADTDTAGES 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 EDEQAFVSKS GSSFETQHHH 

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

       550        560        570        580        590        600 
PNANVSGSHQ GSIQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI 

       610        620        630 
PTPPVTTPEG DDRPESPEYS GGNIVRVSAL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing." Kong W., Po S., Yamagishi T., Ashen M.D., Stetten G., Tomaselli G.F. Am. J. Physiol. 275:H1963-H1970(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current." Zhu X.-R., Wulf A., Schwarz M., Isbrandt D., Pongs O. Recept. Channels 6:387-400(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, FUNCTION.
[4]	"Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA)." Isbrandt D., Leicher T., Waldschuetz R., Zhu X.-R., Luhmann U., Michel U., Sauter K., Pongs O. Genomics 64:144-154(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Brain cortex.
[5]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]	"Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin." Petrecca K., Miller D.M., Shrier A. J. Neurosci. 20:8736-8744(2000) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF 601-PRO--PRO-604, SUBCELLULAR LOCATION, INTERACTION WITH FLNA AND FLNC.
[8]	"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.
[9]	"Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating." Baehring R., Dannenberg J., Peters H.C., Leicher T., Pongs O., Isbrandt D. J. Biol. Chem. 276:23888-23894(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNIP2.
[10]	"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.
[11]	"PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex." Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D. J. Neurosci. 22:10123-10133(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNIP3.
[12]	"Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10)." Jerng H.H., Qian Y., Pfaffinger P.J. Biophys. J. 87:2380-2396(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DPP10.
[13]	"Protein-protein interactions of KChIP proteins and Kv4.2." Lin Y.-L., Chen C.Y., Cheng C.P., Chang L.S. Biochem. Biophys. Res. Commun. 321:606-610(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNIP1 AND KCNIP2.
[14]	"Ito channels are octameric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2." Kim L.A., Furst J., Butler M.H., Xu S., Grigorieff N., Goldstein S.A. J. Biol. Chem. 279:5549-5554(2004) [PubMed] [Europe PMC] [Abstract] Cited for: COMPOSITION OF THE COMPLEX WITH KCNIP2.
[15]	"Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by electron microscopy at 21 Angstrom resolution." Kim L.A., Furst J., Gutierrez D., Butler M.H., Xu S., Goldstein S.A., Grigorieff N. Neuron 41:513-519(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE KCND2-KCNIP2 COMPLEX.
[16]	"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. , Bowlby M.R., Chanda P., Rhodes K.J. Neuron 41:587-598(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCNIP1.
[17]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF121104 mRNA. Translation: AAD22053.1. AB028967 mRNA. Translation: BAA82996.2. Different initiation. AJ010969 mRNA. Translation: CAB56841.1. AF166008, AF166007 Genomic DNA. Translation: AAF65618.1. AC004888 Genomic DNA. Translation: AAC83405.1. AC004946 Genomic DNA. No translation available. AF142568 Genomic DNA. Translation: AAD52159.1. BC110449 mRNA. Translation: AAI10450.1. BC110450 mRNA. Translation: AAI10451.1.
CCDS	CCDS5776.1.
RefSeq	NP_036413.1. NM_012281.2.
UniGene	Hs.654739.
3D structure databases
ProteinModelPortal	Q9NZV8.
SMR	Q9NZV8. Positions 6-415.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	109953. 10 interactions.
IntAct	Q9NZV8. 2 interactions.
STRING	9606.ENSP00000333496.
Chemistry
ChEMBL	CHEMBL2362996.
Protein family/group databases
TCDB	1.A.1.2.5. the voltage-gated ion channel (vic) superfamily.
PTM databases
PhosphoSite	Q9NZV8.
Polymorphism databases
DMDM	38258257.
Proteomic databases
PaxDb	Q9NZV8.
PRIDE	Q9NZV8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331113; ENSP00000333496; ENSG00000184408.
GeneID	3751.
KEGG	hsa:3751.
UCSC	uc003vjj.1. human.
Organism-specific databases
CTD	3751.
GeneCards	GC07P119913.
HGNC	HGNC:6238. KCND2.
HPA	HPA029068.
MIM	605410. gene.
neXtProt	NX_Q9NZV8.
PharmGKB	PA30030.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1226.
HOVERGEN	HBG106687.
InParanoid	Q9NZV8.
KO	K04892.
OMA	SCCGRCC.
OrthoDB	EOG7SR4MG.
PhylomeDB	Q9NZV8.
TreeFam	TF313103.
Enzyme and pathway databases
Reactome	REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	Q9NZV8.
Bgee	Q9NZV8.
CleanEx	HS_KCND2.
Genevestigator	Q9NZV8.
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. 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]
PANTHER	PTHR11537. PTHR11537. 1 hit.
Pfam	PF02214. BTB_2. 1 hit. PF11879. DUF3399. 1 hit. PF00520. Ion_trans. 1 hit. PF11601. Shal-type. 1 hit. [Graphical view]
PRINTS	PR00169. KCHANNEL. PR01517. KV42CHANNEL. PR01491. KVCHANNEL. PR01497. SHALCHANNEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. SSF54695. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	KCND2. human.
GeneWiki	KCND2.
GenomeRNAi	3751.
NextBio	14687.
PRO	Q9NZV8.
SOURCE	Search...

Entry information

Entry name

KCND2_HUMAN

Accession

Primary (citable) accession number: Q9NZV8
Secondary accession number(s): O95012 expand/collapse secondary AC list

Q9UNH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	November 7, 2003
Last modified:	July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

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

Chemistry

Protein family/group databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents