KCND3_MOUSE
ID KCND3_MOUSE Reviewed; 655 AA.
AC Q9Z0V1; Q8CC44; Q9Z0V0;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.3;
GN Name=Kcnd3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Swiss Webster; TISSUE=Heart ventricle;
RA Tanaka H., Janzen K., Winkfein R.J., Fiset C., Clark R.B., Giles W.R.;
RT "Cloning and functional characterization of mouse heart K+ channel alpha
RT subunits, Kv1.5, Kv4.2 and Kv4.3.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP INTERACTION WITH KCNIP3.
RX PubMed=11598014; DOI=10.1093/emboj/20.20.5715;
RA Liss B., Franz O., Sewing S., Bruns R., Neuhoff H., Roeper J.;
RT "Tuning pacemaker frequency of individual dopaminergic neurons by Kv4.3L
RT and KChip3.1 transcription.";
RL EMBO J. 20:5715-5724(2001).
RN [4]
RP INTERACTION WITH KCND2 AND KCNIP2.
RX PubMed=11909823; DOI=10.1161/01.res.0000012664.05949.e0;
RA Guo W., Li H., Aimond F., Johns D.C., Rhodes K.J., Trimmer J.S.,
RA Nerbonne J.M.;
RT "Role of heteromultimers in the generation of myocardial transient outward
RT K+ currents.";
RL Circ. Res. 90:586-593(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; THR-459; SER-569 AND
RP SER-585, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC inactivating A-type potassium channels. May contribute to I(To) current
CC in heart and I(Sa) current in neurons. Channel properties are modulated
CC by interactions with other alpha subunits and with regulatory subunits.
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCND1 and/or KCND2.
CC Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC KCNIP4. Interacts with DLG1, KCNE1, KCNE2, SCN1B and KCNAB1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q62897};
CC Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q62897}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q62897}. Note=Interaction with palmitoylated
CC KCNIP2 and KCNIP3 enhances cell surface expression.
CC {ECO:0000250|UniProtKB:Q62897}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Kv4.3L;
CC IsoId=Q9Z0V1-1; Sequence=Displayed;
CC Name=2; Synonyms=Kv4.3M;
CC IsoId=Q9Z0V1-2; Sequence=VSP_008827;
CC Name=3;
CC IsoId=Q9Z0V1-3; Sequence=VSP_008828, VSP_008829;
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- PTM: Regulated through phosphorylation at Ser-569 by CaMK2D.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Kv4.3/KCND3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF107781; AAD16973.1; -; mRNA.
DR EMBL; AF107782; AAD16974.1; -; mRNA.
DR EMBL; AK033962; BAC28529.1; -; mRNA.
DR CCDS; CCDS17708.1; -. [Q9Z0V1-2]
DR CCDS; CCDS17709.1; -. [Q9Z0V1-1]
DR RefSeq; NP_001034436.1; NM_001039347.1. [Q9Z0V1-2]
DR RefSeq; NP_064315.1; NM_019931.1. [Q9Z0V1-1]
DR RefSeq; XP_006501818.1; XM_006501755.3.
DR RefSeq; XP_006501819.1; XM_006501756.3.
DR AlphaFoldDB; Q9Z0V1; -.
DR SMR; Q9Z0V1; -.
DR BioGRID; 208049; 3.
DR ComplexPortal; CPX-3262; Kv4.3-KChIP1 channel complex.
DR STRING; 10090.ENSMUSP00000096357; -.
DR DrugCentral; Q9Z0V1; -.
DR GuidetoPHARMACOLOGY; 554; -.
DR iPTMnet; Q9Z0V1; -.
DR PhosphoSitePlus; Q9Z0V1; -.
DR MaxQB; Q9Z0V1; -.
DR PaxDb; Q9Z0V1; -.
DR PeptideAtlas; Q9Z0V1; -.
DR PRIDE; Q9Z0V1; -.
DR ProteomicsDB; 263492; -. [Q9Z0V1-1]
DR ProteomicsDB; 263493; -. [Q9Z0V1-2]
DR ProteomicsDB; 263494; -. [Q9Z0V1-3]
DR ABCD; Q9Z0V1; 2 sequenced antibodies.
DR Antibodypedia; 20128; 217 antibodies from 30 providers.
DR DNASU; 56543; -.
DR Ensembl; ENSMUST00000079169; ENSMUSP00000078169; ENSMUSG00000040896. [Q9Z0V1-1]
DR Ensembl; ENSMUST00000098761; ENSMUSP00000096357; ENSMUSG00000040896. [Q9Z0V1-2]
DR Ensembl; ENSMUST00000118360; ENSMUSP00000113436; ENSMUSG00000040896. [Q9Z0V1-1]
DR GeneID; 56543; -.
DR KEGG; mmu:56543; -.
DR UCSC; uc008qux.1; mouse. [Q9Z0V1-3]
DR UCSC; uc008quz.1; mouse. [Q9Z0V1-1]
DR CTD; 3752; -.
DR MGI; MGI:1928743; Kcnd3.
DR VEuPathDB; HostDB:ENSMUSG00000040896; -.
DR eggNOG; KOG4390; Eukaryota.
DR GeneTree; ENSGT00940000155343; -.
DR HOGENOM; CLU_011722_9_1_1; -.
DR InParanoid; Q9Z0V1; -.
DR OMA; XKARLAR; -.
DR PhylomeDB; Q9Z0V1; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR Reactome; R-MMU-5576894; Phase 1 - inactivation of fast Na+ channels.
DR BioGRID-ORCS; 56543; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Kcnd3; mouse.
DR PRO; PR:Q9Z0V1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9Z0V1; protein.
DR Bgee; ENSMUSG00000040896; Expressed in substantia nigra and 157 other tissues.
DR ExpressionAtlas; Q9Z0V1; baseline and differential.
DR Genevisible; Q9Z0V1; MM.
DR GO; GO:0005901; C:caveola; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0034705; C:potassium channel complex; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; ISO:MGI.
DR GO; GO:0005216; F:ion channel activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0099625; P:ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR InterPro; IPR004056; K_chnl_volt-dep_Kv4.3.
DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR InterPro; IPR021645; Shal-type_N.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF11879; DUF3399; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11601; Shal-type; 1.
DR PRINTS; PR01518; KV43CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT CHAIN 1..655
FT /note="Potassium voltage-gated channel subfamily D member
FT 3"
FT /id="PRO_0000054069"
FT TOPO_DOM 1..181
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 243..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 287..307
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 360..380
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..20
FT /note="Interaction with KCNIP2"
FT /evidence="ECO:0000250"
FT REGION 472..487
FT /note="Mediates dendritic targeting"
FT /evidence="ECO:0000250"
FT REGION 523..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 367..372
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 624..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 459
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 488..531
FT /note="GLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNYPST -> VSSS
FT LLPPPASSLTSQGCTHVIIPRRESSSVPFQSKTIVSLPLG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008828"
FT VAR_SEQ 488..506
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_008827"
FT VAR_SEQ 532..655
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_008829"
SQ SEQUENCE 655 AA; 73462 MW; 17FCE5AEC2868B33 CRC64;
MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKNKRQDE LIVLNVSGRR FQTWRTTLER
YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT GKLHYPRYEC ISAYDDELAF
YGILPEIIGD CCYEEYKDRK RENAERLMDD NDSENNQESM PSLSFRQTMW RAFENPHTST
LALVFYYVTG FFIAVSVITN VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE
YLLRLFAAPS RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF
SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK FTSIPASFWY
TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP VIVSNFSRIY HQNQRADKRR
AQKKARLARI RVAKTGSSNA YLHSKRNGLL NEALELTGTP EEEQMGKTTS LIESQHHHLL
HCLEKTTGLS YLVDDPLLSV RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHS
GLTTTCCSRR SKKTTHLPNS NLPATRLRSM QELSTLHIQG SEQPSLTTSR SSLNLKADDG
LRPNCKTSQI TTAIISIPTP PALTPEGESR PPPASPGPNT NIPSITSNVV KVSAL
