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Q03719 (KCND1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily D member 1
Alternative name(s):
Voltage-gated potassium channel subunit Kv4.1
Short name=mShal
Gene names
Name:Kcnd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length651 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 the heart and I(Sa) current in neurons. Channel properties are modulated by subunit assembly. Ref.1

Subunit structure

Homotetramer or heterotetramer with KCND2 and/or KCND3. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Interacts with DPP10 By similarity. Ref.3

Subcellular location

Membrane; Multi-pass membrane protein. Cell projectiondendrite By similarity.

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]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 651651Potassium voltage-gated channel subfamily D member 1
PRO_0000054062

Regions

Topological domain1 – 184184Cytoplasmic Potential
Transmembrane185 – 20521Helical; Name=Segment S1; Potential
Transmembrane227 – 24721Helical; Name=Segment S2; Potential
Topological domain248 – 26114Cytoplasmic Potential
Transmembrane262 – 28221Helical; Name=Segment S3; Potential
Transmembrane292 – 31221Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain313 – 32513Cytoplasmic Potential
Transmembrane326 – 34621Helical; Name=Segment S5; Potential
Intramembrane365 – 38521Pore-forming; Name=Segment H5; Potential
Transmembrane387 – 40721Helical; Name=Segment S6; Potential
Topological domain408 – 651244Cytoplasmic Potential
Region2 – 2019Interaction with KCNIP2 By similarity
Region474 – 48916Mediates dendritic targeting By similarity
Motif372 – 3776Selectivity filter By similarity

Sites

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

Amino acid modifications

Glycosylation3551N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q03719 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 801DECC3C56C721F

FASTA65171,698
        10         20         30         40         50         60 
MAAGVATWLP FARAAAVGWL PLAQQPLPPA PEVKASRGDE VLVVNVSGRR FETWKNTLDR 

        70         80         90        100        110        120 
YPDTLLGSSE KEFFYDAESG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF 

       130        140        150        160        170        180 
YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGEGP ALPAGSSLRQ RLWRAFENPH 

       190        200        210        220        230        240 
TSTAALVFYY VTGFFIAVSV IANVVETIPC RGTPRWPSKE QSCGDRFPTA FFCMDTACVL 

       250        260        270        280        290        300 
IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLF VPKNDDVSGA FVTLRVFRVF 

       310        320        330        340        350        360 
RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TSKTNFTSIP 

       370        380        390        400        410        420 
AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR 

       430        440        450        460        470        480 
ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGGLEDSGS GDGQMLCVRS RSAFEQQHHH 

       490        500        510        520        530        540 
LLHCLEKTTC HEFTDELTFS EALGAVSLGG RTSRSTSVSS QPMGPGSLFS SCCSRRVNRR 

       550        560        570        580        590        600 
AIRLANSTAS VSRGSMQELD TLAGLRRSPA PQTRSSLNAK PHDSLDLNCD SRDFVAAIIS 

       610        620        630        640        650 
IPTPPANTPD ESQPSSPSGG GGSGGTPNTT LRNSSLGTPC LLPETVKISS L 

« Hide

References

« Hide 'large scale' references
[1]"mShal, a subfamily of A-type K+ channel cloned from mammalian brain."
Pak M.D., Baker K., Covarrubias M., Butler A., Ratcliffe A., Salkoff L.
Proc. Natl. Acad. Sci. U.S.A. 88:4386-4390(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Tissue: Brain.
[2]"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. expand/collapse author list , 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] OF 145-647.
Strain: C57BL/6J.
Tissue: Epididymis.
[3]"Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4 subfamily members, Kv4.1 and Kv4.2."
Nakamura T.Y., Nandi S., Pountney D.J., Artman M., Rudy B., Coetzee W.A.
FEBS Lett. 499:205-209(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64226 mRNA. Translation: AAA39745.1.
AK033805 mRNA. Translation: BAC28480.1.
IPIIPI00135598.
PIRA39372.
RefSeqNP_032449.1. NM_008423.1.
UniGeneMm.335968.

3D structure databases

ProteinModelPortalQ03719.
SMRQ03719. Positions 3-417.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-103872.

PTM databases

PhosphoSiteQ03719.

Proteomic databases

PRIDEQ03719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000009875; ENSMUSP00000009875; ENSMUSG00000009731.
GeneID16506.
KEGGmmu:16506.

Organism-specific databases

CTD3750.
MGIMGI:96671. Kcnd1.

Phylogenomic databases

eggNOGCOG1226.
GeneTreeENSGT00630000089518.
HOGENOMHOG000231013.
HOVERGENHBG106687.
InParanoidQ03719.
KOK04891.
OrthoDBEOG473PQX.

Gene expression databases

ArrayExpressQ03719.
BgeeQ03719.
GenevestigatorQ03719.
GermOnlineENSMUSG00000009731. Mus musculus.

Family and domain databases

Gene3D3.30.710.10. 1 hit.
InterProIPR000210. 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.
IPR004054. K_chnl_volt-dep_Kv4.1.
IPR024587. K_chnl_volt-dep_Kv4_C.
IPR021645. Shal-type.
IPR003131. T1-type_BTB.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PTHR11537:SF15. PTHR11537:SF15. 1 hit.
PfamPF11879. DUF3399. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02214. K_tetra. 1 hit.
PF11601. Shal-type. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01516. KV41CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. BTB/POZ_fold. 1 hit.
ProtoNetSearch...

Other

NextBio289835.
SOURCESearch...

Entry information

Entry nameKCND1_MOUSE
AccessionPrimary (citable) accession number: Q03719
Secondary accession number(s): Q8CC68
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 1, 1996
Last modified: May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families