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Protein

Potassium voltage-gated channel subfamily D member 1

Gene

Kcnd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi104 – 1041ZincBy similarity
Metal bindingi131 – 1311ZincBy similarity
Metal bindingi132 – 1321ZincBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Metal-binding, Potassium, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.
R-MMU-5576894. Phase 1 - inactivation of fast Na+ channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily D member 1
Alternative name(s):
Voltage-gated potassium channel subunit Kv4.1
Short name:
mShal
Gene namesi
Name:Kcnd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:96671. Kcnd1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 184184CytoplasmicSequence analysisAdd
BLAST
Transmembranei185 – 20521Helical; Name=Segment S1Sequence analysisAdd
BLAST
Transmembranei227 – 24721Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini248 – 26114CytoplasmicSequence analysisAdd
BLAST
Transmembranei262 – 28221Helical; Name=Segment S3Sequence analysisAdd
BLAST
Transmembranei292 – 31221Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini313 – 32513CytoplasmicSequence analysisAdd
BLAST
Transmembranei326 – 34621Helical; Name=Segment S5Sequence analysisAdd
BLAST
Intramembranei365 – 38521Pore-forming; Name=Segment H5Sequence analysisAdd
BLAST
Transmembranei387 – 40721Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini408 – 651244CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Membrane

Pathology & Biotechi

Chemistry

GuidetoPHARMACOLOGYi552.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 651651Potassium voltage-gated channel subfamily D member 1PRO_0000054062Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence analysis
Modified residuei458 – 4581PhosphoserineCombined sources
Modified residuei555 – 5551PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ03719.
PaxDbiQ03719.
PRIDEiQ03719.

PTM databases

iPTMnetiQ03719.
PhosphoSiteiQ03719.

Expressioni

Gene expression databases

BgeeiQ03719.
ExpressionAtlasiQ03719. baseline and differential.
GenevisibleiQ03719. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi200889. 1 interaction.
IntActiQ03719. 1 interaction.
MINTiMINT-103872.
STRINGi10090.ENSMUSP00000009875.

Structurei

3D structure databases

ProteinModelPortaliQ03719.
SMRiQ03719. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2019Interaction with KCNIP2By similarityAdd
BLAST
Regioni474 – 48916Mediates dendritic targetingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi372 – 3776Selectivity filterBy similarity

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4390. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231013.
HOVERGENiHBG106687.
InParanoidiQ03719.
KOiK04891.
OMAiPREQPCG.
OrthoDBiEOG7SR4MG.
PhylomeDBiQ03719.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
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_N.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF11879. DUF3399. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11601. Shal-type. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01516. KV41CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequencei

Sequence statusi: Complete.

Q03719-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAGVATWLP FARAAAVGWL PLAQQPLPPA PEVKASRGDE VLVVNVSGRR
60 70 80 90 100
FETWKNTLDR YPDTLLGSSE KEFFYDAESG EYFFDRDPDM FRHVLNFYRT
110 120 130 140 150
GRLHCPRQEC IQAFDEELAF YGLVPELVGD CCLEEYRDRK KENAERLAED
160 170 180 190 200
EEAEQAGEGP ALPAGSSLRQ RLWRAFENPH TSTAALVFYY VTGFFIAVSV
210 220 230 240 250
IANVVETIPC RGTPRWPSKE QSCGDRFPTA FFCMDTACVL IFTGEYLLRL
260 270 280 290 300
FAAPSRCRFL RSVMSLIDVV AILPYYIGLF VPKNDDVSGA FVTLRVFRVF
310 320 330 340 350
RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG
360 370 380 390 400
TSKTNFTSIP AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI
410 420 430 440 450
ALPVPVIVSN FSRIYHQNQR ADKRRAQQKV RLARIRLAKS GTTNAFLQYK
460 470 480 490 500
QNGGLEDSGS GDGQMLCVRS RSAFEQQHHH LLHCLEKTTC HEFTDELTFS
510 520 530 540 550
EALGAVSLGG RTSRSTSVSS QPMGPGSLFS SCCSRRVNRR AIRLANSTAS
560 570 580 590 600
VSRGSMQELD TLAGLRRSPA PQTRSSLNAK PHDSLDLNCD SRDFVAAIIS
610 620 630 640 650
IPTPPANTPD ESQPSSPSGG GGSGGTPNTT LRNSSLGTPC LLPETVKISS

L
Length:651
Mass (Da):71,698
Last modified:November 1, 1996 - v1
Checksum:i801DECC3C56C721F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64226 mRNA. Translation: AAA39745.1.
AK033805 mRNA. Translation: BAC28480.1.
CCDSiCCDS29974.1.
PIRiA39372.
RefSeqiNP_032449.1. NM_008423.2.
UniGeneiMm.335968.

Genome annotation databases

EnsembliENSMUST00000009875; ENSMUSP00000009875; ENSMUSG00000009731.
GeneIDi16506.
KEGGimmu:16506.
UCSCiuc009sms.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64226 mRNA. Translation: AAA39745.1.
AK033805 mRNA. Translation: BAC28480.1.
CCDSiCCDS29974.1.
PIRiA39372.
RefSeqiNP_032449.1. NM_008423.2.
UniGeneiMm.335968.

3D structure databases

ProteinModelPortaliQ03719.
SMRiQ03719. Positions 3-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200889. 1 interaction.
IntActiQ03719. 1 interaction.
MINTiMINT-103872.
STRINGi10090.ENSMUSP00000009875.

Chemistry

GuidetoPHARMACOLOGYi552.

PTM databases

iPTMnetiQ03719.
PhosphoSiteiQ03719.

Proteomic databases

MaxQBiQ03719.
PaxDbiQ03719.
PRIDEiQ03719.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009875; ENSMUSP00000009875; ENSMUSG00000009731.
GeneIDi16506.
KEGGimmu:16506.
UCSCiuc009sms.1. mouse.

Organism-specific databases

CTDi3750.
MGIiMGI:96671. Kcnd1.

Phylogenomic databases

eggNOGiKOG4390. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231013.
HOVERGENiHBG106687.
InParanoidiQ03719.
KOiK04891.
OMAiPREQPCG.
OrthoDBiEOG7SR4MG.
PhylomeDBiQ03719.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.
R-MMU-5576894. Phase 1 - inactivation of fast Na+ channels.

Miscellaneous databases

PROiQ03719.
SOURCEiSearch...

Gene expression databases

BgeeiQ03719.
ExpressionAtlasiQ03719. baseline and differential.
GenevisibleiQ03719. MM.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
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_N.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF02214. BTB_2. 1 hit.
PF11879. DUF3399. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11601. Shal-type. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01516. KV41CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKCND1_MOUSE
AccessioniPrimary (citable) accession number: Q03719
Secondary accession number(s): Q8CC68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.