Q9Z0V2 (KCND2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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
ORF Names:	MNCb-7013

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.
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 3 and KCND2. The KCND2-KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits. Interacts with DPP6, DPP10, DLG4, NCS1/FREQ, FLNA, FLNC and DLG1 By similarity. Ref.7 Ref.8 Ref.9
Subcellular location	Membrane; Multi-pass membrane protein. Cell projection › dendrite By similarity.
Tissue specificity	Detected in brain, especially in hippocampus, medial habenular nucleus, striatum, amygdala, cortex and cerebellum. Ref.6
Domain	The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
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 BAA97986.1 differs from that shown. Reason: Frameshift at position 520. The sequence BAC41464.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	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	protein homooligomerization Inferred from electronic annotation. Source: InterPro regulation of action potential Inferred from mutant phenotype PubMed 20573902. Source: MGI
Cellular_component	cell surface Inferred from electronic annotation. Source: Compara dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay PubMed 18603586. Source: MGI 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kif17	Q99PW8	3	EBI-959779,EBI-959754

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_0000054065
Regions
	Topological domain	1 – 183	183	Cytoplasmic Potential
	Transmembrane	184 – 204	21	Helical; Name=Segment S1; Potential
	Transmembrane	225 – 245	21	Helical; Name=Segment S2; Potential
	Topological domain	246 – 259	14	Cytoplasmic Potential
	Transmembrane	260 – 280	21	Helical; Name=Segment S3; Potential
	Transmembrane	290 – 310	21	Helical; Voltage-sensor; Name=Segment S4; Potential
	Topological domain	311 – 323	13	Cytoplasmic Potential
	Transmembrane	324 – 344	21	Helical; Name=Segment S5; Potential
	Intramembrane	363 – 383	21	Pore-forming; Name=Segment H5; Potential
	Transmembrane	385 – 405	21	Helical; Name=Segment S6; Potential
	Topological domain	406 – 630	225	Cytoplasmic Potential
	Region	2 – 20	19	Interaction with KCNIP2 By similarity
	Region	7 – 11	5	Interaction with KCNIP1 By similarity
	Region	71 – 90	20	Interaction with KCNIP1 By similarity
	Region	474 – 489	16	Mediates dendritic targeting By similarity
	Motif	370 – 375	6	Selectivity filter By similarity
Sites
	Metal binding	105	1	Zinc By similarity
	Metal binding	132	1	Zinc By similarity
	Metal binding	133	1	Zinc By similarity
Amino acid modifications
	Modified residue	38	1	Phosphothreonine
	Modified residue	548	1	Phosphoserine Ref.10
	Modified residue	552	1	Phosphoserine
	Modified residue	602	1	Phosphothreonine
	Modified residue	607	1	Phosphothreonine
	Modified residue	616	1	Phosphoserine
Experimental info
	Mutagenesis	552	1	S → A: Abolishes PKA-mediated modulation of channel activity. Ref.7
	Sequence conflict	22	1	V → A in BAA97986. Ref.2
	Sequence conflict	516	1	S → R in BAC41464. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Z0V2 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 7FB94277429E7683	FASTA	630	70,577
	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 EDEPAFISKS GSSFETQHHH 490 500 510 520 530 540 LLHCLEKTTN HEFVDEQVFE ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKTFRI 550 560 570 580 590 600 PNANVSGSHR GSVQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI 610 620 630 PTPPVTTPEG DDRPESPEYS GGNIVRVSAL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional characterization of mouse heart K+ channel alpha subunits, Kv1.5, Kv4.2 and Kv4.3." Tanaka H., Janzen K., Winkfein R.J., Fiset C., Clark R.B., Giles W.R. Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Swiss Webster. Tissue: Heart ventricle.
[2]	"Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method." Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K. Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[3]	"Prediction of the coding sequences of mouse homologues of KIAA gene: I. The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O., Koga H. DNA Res. 9:179-188(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mesonephros and Olfactory bulb.
[5]	"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]. Strain: C57BL/6. Tissue: Brain.
[6]	"Input-specific immunolocalization of differentially phosphorylated Kv4.2 in the mouse brain." Varga A.W., Anderson A.E., Adams J.P., Vogel H., Sweatt J.D. Learn. Memory 7:321-332(2000) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, TISSUE SPECIFICITY.
[7]	"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, MUTAGENESIS OF SER-552, PHOSPHORYLATION.
[8]	"Role of heteromultimers in the generation of myocardial transient outward K+ currents." Guo W., Li H., Aimond F., Johns D.C., Rhodes K.J., Trimmer J.S., Nerbonne J.M. Circ. Res. 90:586-593(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KCND3 AND KCNIP2.
[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]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF107780 mRNA. Translation: AAD16972.1. AB045326 mRNA. Translation: BAA97986.1. Frameshift. AB093280 mRNA. Translation: BAC41464.1. Different initiation. AK032268 mRNA. Translation: BAC27787.1. AK032772 mRNA. Translation: BAC28015.1. BC079667 mRNA. Translation: AAH79667.1.
IPI	IPI00129491.
RefSeq	NP_062671.1. NM_019697.3.
UniGene	Mm.425316.
3D structure databases
ProteinModelPortal	Q9Z0V2.
SMR	Q9Z0V2. Positions 6-415.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z0V2. 3 interactions.
PTM databases
PhosphoSite	Q9Z0V2.
Proteomic databases
PaxDb	Q9Z0V2.
PRIDE	Q9Z0V2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000081542; ENSMUSP00000080257; ENSMUSG00000060882.
GeneID	16508.
KEGG	mmu:16508.
UCSC	uc009baq.1. mouse.
Organism-specific databases
CTD	3751.
MGI	MGI:102663. Kcnd2.
Rouge	Search...
Phylogenomic databases
eggNOG	COG1226.
GeneTree	ENSGT00630000089518.
HOGENOM	HOG000231013.
HOVERGEN	HBG106687.
InParanoid	Q9Z0V2.
KO	K04892.
OMA	SCCGRCC.
OrthoDB	EOG4HMJ8X.
Gene expression databases
Bgee	Q9Z0V2.
Genevestigator	Q9Z0V2.
GermOnline	ENSMUSG00000060882. Mus musculus.
Family and domain databases
Gene3D	3.30.710.10. 1 hit.
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. 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. [Graphical view]
PANTHER	PTHR11537. PTHR11537. 1 hit.
Pfam	PF11879. DUF3399. 1 hit. PF00520. Ion_trans. 1 hit. PF02214. K_tetra. 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. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	289839.
SOURCE	Search...

Entry information

Entry name

KCND2_MOUSE

Accession

Primary (citable) accession number: Q9Z0V2
Secondary accession number(s): Q8BSK3, Q8CHB7, Q9JJ60

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program