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Q9Z0V1

- KCND3_MOUSE

UniProt

Q9Z0V1 - KCND3_MOUSE

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Protein
Potassium voltage-gated channel subfamily D member 3
Gene
Kcnd3
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 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 heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits.

Sites

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

GO - Molecular functioni

  1. A-type (transient outward) potassium channel activity Source: RefGenome
  2. metal ion binding Source: UniProtKB-KW
  3. protein binding Source: MGI

GO - Biological processi

  1. membrane repolarization Source: Ensembl
  2. potassium ion export Source: Ensembl
  3. protein homooligomerization Source: InterPro
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

ReactomeiREACT_199077. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily D member 3
Alternative name(s):
Voltage-gated potassium channel subunit Kv4.3
Gene namesi
Name:Kcnd3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1928743. Kcnd3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 181181Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei182 – 20221Helical; Name=Segment S1; Reviewed prediction
Add
BLAST
Transmembranei222 – 24221Helical; Name=Segment S2; Reviewed prediction
Add
BLAST
Topological domaini243 – 25614Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei257 – 27721Helical; Name=Segment S3; Reviewed prediction
Add
BLAST
Transmembranei287 – 30721Helical; Voltage-sensor; Name=Segment S4; Reviewed prediction
Add
BLAST
Topological domaini308 – 32013Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei321 – 34121Helical; Name=Segment S5; Reviewed prediction
Add
BLAST
Intramembranei360 – 38021Pore-forming; Name=Segment H5; Reviewed prediction
Add
BLAST
Transmembranei382 – 40221Helical; Name=Segment S6; Reviewed prediction
Add
BLAST
Topological domaini403 – 655253Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. dendrite Source: UniProtKB-SubCell
  2. membrane Source: MGI
  3. neuronal cell body Source: Ensembl
  4. perinuclear endoplasmic reticulum Source: Ensembl
  5. sarcolemma Source: UniProtKB-SubCell
  6. voltage-gated potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 655655Potassium voltage-gated channel subfamily D member 3
PRO_0000054069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei569 – 5691Phosphoserine; by CaMK2D By similarity

Post-translational modificationi

Regulated through phosphorylation at Ser-569 by CaMK2D.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9Z0V1.
PRIDEiQ9Z0V1.

PTM databases

PhosphoSiteiQ9Z0V1.

Expressioni

Gene expression databases

ArrayExpressiQ9Z0V1.
BgeeiQ9Z0V1.
GenevestigatoriQ9Z0V1.

Interactioni

Subunit structurei

Homotetramer or heterotetramer with KCND1 and/or KCND2. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4. Interacts with DLG1, KCNE1, KCNE2, SCN1B and KCNAB1 By similarity.2 Publications

Protein-protein interaction databases

IntActiQ9Z0V1. 1 interaction.
MINTiMINT-4099679.
STRINGi10090.ENSMUSP00000113436.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0V1.
SMRiQ9Z0V1. Positions 6-412.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 2019Interaction with KCNIP2 By similarity
Add
BLAST
Regioni472 – 48716Mediates dendritic targeting By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi367 – 3726Selectivity filter By 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

eggNOGiCOG1226.
GeneTreeiENSGT00740000115211.
HOGENOMiHOG000231013.
HOVERGENiHBG106687.
InParanoidiQ9Z0V1.
KOiK04893.
OMAiPEVFRCI.
OrthoDBiEOG7SR4MG.
PhylomeDBiQ9Z0V1.
TreeFamiTF313103.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProiIPR000210. 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.
IPR004056. K_chnl_volt-dep_Kv4.3.
IPR024587. K_chnl_volt-dep_Kv4_C.
IPR021645. Shal-type.
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.
PR01518. KV43CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Z0V1-1) [UniParc]FASTAAdd to Basket

Also known as: Kv4.3L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKNKRQDE LIVLNVSGRR    50
FQTWRTTLER YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT 100
GKLHYPRYEC ISAYDDELAF YGILPEIIGD CCYEEYKDRK RENAERLMDD 150
NDSENNQESM PSLSFRQTMW RAFENPHTST LALVFYYVTG FFIAVSVITN 200
VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE YLLRLFAAPS 250
RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF 300
SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK 350
FTSIPASFWY TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP 400
VIVSNFSRIY HQNQRADKRR AQKKARLARI RVAKTGSSNA YLHSKRNGLL 450
NEALELTGTP EEEQMGKTTS LIESQHHHLL HCLEKTTGLS YLVDDPLLSV 500
RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHS GLTTTCCSRR 550
SKKTTHLPNS NLPATRLRSM QELSTLHIQG SEQPSLTTSR SSLNLKADDG 600
LRPNCKTSQI TTAIISIPTP PALTPEGESR PPPASPGPNT NIPSITSNVV 650
KVSAL 655
Length:655
Mass (Da):73,462
Last modified:May 1, 1999 - v1
Checksum:i17FCE5AEC2868B33
GO
Isoform 2 (identifier: Q9Z0V1-2) [UniParc]FASTAAdd to Basket

Also known as: Kv4.3M

The sequence of this isoform differs from the canonical sequence as follows:
     488-506: Missing.

Show »
Length:636
Mass (Da):71,403
Checksum:iABC972B74CA982AA
GO
Isoform 3 (identifier: Q9Z0V1-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     488-531: GLSYLVDDPL...ESSMQNYPST → VSSSLLPPPA...SKTIVSLPLG
     532-655: Missing.

Note: May be due to intron retention. No experimental confirmation available.

Show »
Length:531
Mass (Da):59,862
Checksum:i5580144E7899BE5F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei488 – 53144GLSYL…NYPST → VSSSLLPPPASSLTSQGCTH VIIPRRESSSVPFQSKTIVS LPLG in isoform 3.
VSP_008828Add
BLAST
Alternative sequencei488 – 50619Missing in isoform 2.
VSP_008827Add
BLAST
Alternative sequencei532 – 655124Missing in isoform 3.
VSP_008829Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF107781 mRNA. Translation: AAD16973.1.
AF107782 mRNA. Translation: AAD16974.1.
AK033962 mRNA. Translation: BAC28529.1.
CCDSiCCDS17708.1. [Q9Z0V1-2]
CCDS17709.1. [Q9Z0V1-1]
RefSeqiNP_001034436.1. NM_001039347.1. [Q9Z0V1-2]
NP_064315.1. NM_019931.1. [Q9Z0V1-1]
XP_006501818.1. XM_006501755.1. [Q9Z0V1-1]
XP_006501819.1. XM_006501756.1. [Q9Z0V1-1]
UniGeneiMm.44530.

Genome annotation databases

EnsembliENSMUST00000079169; ENSMUSP00000078169; ENSMUSG00000040896. [Q9Z0V1-1]
ENSMUST00000098761; ENSMUSP00000096357; ENSMUSG00000040896. [Q9Z0V1-2]
ENSMUST00000118360; ENSMUSP00000113436; ENSMUSG00000040896. [Q9Z0V1-1]
GeneIDi56543.
KEGGimmu:56543.
UCSCiuc008qux.1. mouse. [Q9Z0V1-3]
uc008quz.1. mouse. [Q9Z0V1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF107781 mRNA. Translation: AAD16973.1 .
AF107782 mRNA. Translation: AAD16974.1 .
AK033962 mRNA. Translation: BAC28529.1 .
CCDSi CCDS17708.1. [Q9Z0V1-2 ]
CCDS17709.1. [Q9Z0V1-1 ]
RefSeqi NP_001034436.1. NM_001039347.1. [Q9Z0V1-2 ]
NP_064315.1. NM_019931.1. [Q9Z0V1-1 ]
XP_006501818.1. XM_006501755.1. [Q9Z0V1-1 ]
XP_006501819.1. XM_006501756.1. [Q9Z0V1-1 ]
UniGenei Mm.44530.

3D structure databases

ProteinModelPortali Q9Z0V1.
SMRi Q9Z0V1. Positions 6-412.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Z0V1. 1 interaction.
MINTi MINT-4099679.
STRINGi 10090.ENSMUSP00000113436.

Chemistry

GuidetoPHARMACOLOGYi 554.

PTM databases

PhosphoSitei Q9Z0V1.

Proteomic databases

PaxDbi Q9Z0V1.
PRIDEi Q9Z0V1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000079169 ; ENSMUSP00000078169 ; ENSMUSG00000040896 . [Q9Z0V1-1 ]
ENSMUST00000098761 ; ENSMUSP00000096357 ; ENSMUSG00000040896 . [Q9Z0V1-2 ]
ENSMUST00000118360 ; ENSMUSP00000113436 ; ENSMUSG00000040896 . [Q9Z0V1-1 ]
GeneIDi 56543.
KEGGi mmu:56543.
UCSCi uc008qux.1. mouse. [Q9Z0V1-3 ]
uc008quz.1. mouse. [Q9Z0V1-1 ]

Organism-specific databases

CTDi 3752.
MGIi MGI:1928743. Kcnd3.

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00740000115211.
HOGENOMi HOG000231013.
HOVERGENi HBG106687.
InParanoidi Q9Z0V1.
KOi K04893.
OMAi PEVFRCI.
OrthoDBi EOG7SR4MG.
PhylomeDBi Q9Z0V1.
TreeFami TF313103.

Enzyme and pathway databases

Reactomei REACT_199077. Voltage gated Potassium channels.

Miscellaneous databases

NextBioi 312914.
PROi Q9Z0V1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Z0V1.
Bgeei Q9Z0V1.
Genevestigatori Q9Z0V1.

Family and domain databases

Gene3Di 1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProi 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.
IPR004056. K_chnl_volt-dep_Kv4.3.
IPR024587. K_chnl_volt-dep_Kv4_C.
IPR021645. Shal-type.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view ]
PANTHERi PTHR11537. PTHR11537. 1 hit.
Pfami PF02214. BTB_2. 1 hit.
PF11879. DUF3399. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11601. Shal-type. 1 hit.
[Graphical view ]
PRINTSi PR00169. KCHANNEL.
PR01518. KV43CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTi SM00225. BTB. 1 hit.
[Graphical view ]
SUPFAMi SSF54695. SSF54695. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 2).
    Strain: Swiss Webster.
    Tissue: Heart ventricle.
  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] (ISOFORM 3).
    Strain: C57BL/6J.
    Tissue: Diencephalon.
  3. "Tuning pacemaker frequency of individual dopaminergic neurons by Kv4.3L and KChip3.1 transcription."
    Liss B., Franz O., Sewing S., Bruns R., Neuhoff H., Roeper J.
    EMBO J. 20:5715-5724(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNIP3.
  4. "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 KCND2 AND KCNIP2.

Entry informationi

Entry nameiKCND3_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0V1
Secondary accession number(s): Q8CC44, Q9Z0V0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 121 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

External Data

Dasty 3

Similar proteinsi