Q9NSA2 (KCND1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Potassium voltage-gated channel subfamily D member 1

Alternative name(s):
Voltage-gated potassium channel subunit Kv4.1

Gene names

Name:

KCND1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	647 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 KCND2 and/or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4 By similarity. Interacts with DPP10 Probable. Ref.7
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Widely expressed. Highly expressed in brain, in particular in cerebellum and thalamus; detected at lower levels in the other parts of the brain. Ref.1
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. Kv4.1/KCND1 sub-subfamily. [View classification]

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Metal-binding Potassium Zinc
Molecular function	Ionic channel Potassium channel Voltage-gated channel
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	synaptic transmission Traceable author statement. Source: Reactome
Cellular component	voltage-gated potassium channel complex Inferred from electronic annotation. Source: InterPro
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated potassium channel activity Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 647	647	Potassium voltage-gated channel subfamily D member 1		PRO_0000054061
Regions
	Topological domain	1 – 184	184	Cytoplasmic Potential
	Transmembrane	185 – 205	21	Helical; Name=Segment S1; Potential
	Transmembrane	227 – 247	21	Helical; Name=Segment S2; Potential
	Topological domain	248 – 261	14	Cytoplasmic Potential
	Transmembrane	262 – 282	21	Helical; Name=Segment S3; Potential
	Transmembrane	292 – 312	21	Helical; Voltage-sensor; Name=Segment S4; Potential
	Topological domain	313 – 325	13	Cytoplasmic Potential
	Transmembrane	326 – 346	21	Helical; Name=Segment S5; Potential
	Intramembrane	365 – 385	21	Pore-forming; Name=Segment H5; Potential
	Transmembrane	387 – 407	21	Helical; Name=Segment S6; Potential
	Topological domain	408 – 647	240	Cytoplasmic Potential
	Region	2 – 20	19	Interaction with KCNIP2 By similarity
	Motif	372 – 377	6	Selectivity filter By similarity
Sites
	Metal binding	104	1	Zinc By similarity
	Metal binding	131	1	Zinc By similarity
	Metal binding	132	1	Zinc By similarity
Amino acid modifications
	Glycosylation	352	1	N-linked (GlcNAc...) Potential
	Glycosylation	355	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	358	1	S → N in BAA96454. Ref.2
	Sequence conflict	406	1	V → I in BAA96454. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NSA2 [UniParc]. Last modified November 7, 2003. Version 2. Checksum: 8672C299CDB7C5AA	FASTA	647	71,330
	10 20 30 40 50 60 MAAGLATWLP FARAAAVGWL PLAQQPLPPA PGVKASRGDE VLVVNVSGRR FETWKNTLDR 70 80 90 100 110 120 YPDTLLGSSE KEFFYDADSG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF 130 140 150 160 170 180 YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGDGP ALPAGSSLRQ RLWRAFENPH 190 200 210 220 230 240 TSTAALVFYY VTGFFIAVSV IANVVETIPC RGSARRSSRE QPCGERFPQA FFCMDTACVL 250 260 270 280 290 300 IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLL VPKNDDVSGA FVTLRVFRVF 310 320 330 340 350 360 RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TNKTNFTSIP 370 380 390 400 410 420 AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR 430 440 450 460 470 480 ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGGLEDSGS GEEQALCVRN RSAFEQQHHH 490 500 510 520 530 540 LLHCLEKTTC HEFTDELTFS EALGAVSPGG RTSRSTSVSS QPVGPGSLLS SCCPRRAKRR 550 560 570 580 590 600 AIRLANSTAS VSRGSMQELD MLAGLRRSHA PQSRSSLNAK PHDSLDLNCD SRDFVAAIIS 610 620 630 640 IPTPPANTPD ESQPSSPGGG GRAGSTLRNS SLGTPCLFPE TVKISSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 10729221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY. Tissue: Embryonic kidney.
[2]	"Homo sapiens mRNA for shal-type potassium channel KCND1 (Kv4.1)." Makita N., Shirai N., Sawa H., Sasaki K., Nagashima K., Yoshida M.C., Kitabatake A. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	"Transcription map in Xp11.23." Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A. Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cerebellum.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[7]	"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: 15454437] [Abstract] Cited for: INTERACTION WITH DPP10.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF166003 mRNA. Translation: AAF65516.1. AF166006, AF166004, AF166005 Genomic DNA. Translation: AAF65617.1. AB021865 mRNA. Translation: BAA96454.1. AJ005898 mRNA. Translation: CAA06755.1. AK315092 mRNA. Translation: BAG37557.1. CH471224 Genomic DNA. Translation: EAW50721.1. BC045659 mRNA. Translation: AAH45659.1.
IPI	IPI00007507.
RefSeq	NP_004970.3. NM_004979.4.
UniGene	Hs.55276.
3D structure databases
ProteinModelPortal	Q9NSA2.
SMR	Q9NSA2. Positions 6-418.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9NSA2.
PTM databases
PhosphoSite	Q9NSA2.
Polymorphism databases
DMDM	38258256.
Proteomic databases
PRIDE	Q9NSA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000218176; ENSP00000218176; ENSG00000102057.
GeneID	3750.
KEGG	hsa:3750.
NMPDR	fig|9606.3.peg.32758.
UCSC	uc004dlx.1. human.
Organism-specific databases
CTD	3750.
GeneCards	GC0XM048818.
H-InvDB	HIX0203285.
HGNC	HGNC:6237. KCND1.
HPA	HPA001066.
MIM	300281. gene.
neXtProt	NX_Q9NSA2.
PharmGKB	PA30029.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12214.
GeneTree	ENSGT00580000081431.
HOGENOM	HBG315067.
HOVERGEN	HBG106687.
InParanoid	Q9NSA2.
OMA	PCGDRFP.
OrthoDB	EOG473PQX.
PhylomeDB	Q9NSA2.
Enzyme and pathway databases
Reactome	REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	Q9NSA2.
Bgee	Q9NSA2.
CleanEx	HS_KCND1.
Genevestigator	Q9NSA2.
GermOnline	ENSG00000102057. Homo sapiens.
Family and domain databases
InterPro	IPR000210. BTB/POZ-like. IPR011333. BTB/POZ_fold. IPR005821. Ion_trans. IPR003091. K_chnl. IPR003968. K_chnl_volt-dep_Kv. IPR003975. K_chnl_volt-dep_Kv4. IPR004054. K_chnl_volt-dep_Kv4.1. IPR024587. K_chnl_volt-dep_Kv4_C. IPR003131. K_chnl_volt-dep_Kv_tetra. IPR021645. Shal-type. [Graphical view]
Gene3D	G3DSA:3.30.710.10. BTB/POZ_fold. 1 hit.
KO	K04891.
PANTHER	PTHR11537:SF15. KV41channel. 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. PR01516. KV41CHANNEL. PR01491. KVCHANNEL. PR01497. SHALCHANNEL.
SMART	SM00225. BTB. 1 hit. [Graphical view]
SUPFAM	SSF54695. BTB/POZ_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	14683.
SOURCE	Search...

Entry information

Entry name

KCND1_HUMAN

Accession

Primary (citable) accession number: Q9NSA2
Secondary accession number(s): B2RCG0, O75671

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	November 7, 2003
Last modified:	January 25, 2012
This is version 96 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.