ID Q5VSI1_DANRE Unreviewed; 630 AA.
AC Q5VSI1; A0A8M1NDB1;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 149.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 2 {ECO:0000256|ARBA:ARBA00017096};
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.2 {ECO:0000256|ARBA:ARBA00030657};
GN Name=kcnd2 {ECO:0000313|Ensembl:ENSDARP00000114104,
GN ECO:0000313|RefSeq:NP_001076336.1, ECO:0000313|RefSeq:XP_005164719.1,
GN ECO:0000313|ZFIN:ZDB-GENE-041210-70};
GN Synonyms=si:dkey-24j9.3 {ECO:0000313|RefSeq:NP_001076336.1,
GN ECO:0000313|RefSeq:XP_005164719.1}, si:dkeyp-97c5.3
GN {ECO:0000313|RefSeq:NP_001076336.1,
GN ECO:0000313|RefSeq:XP_005164719.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000114104};
RN [1] {ECO:0000313|RefSeq:NP_001076336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001076336.1};
RX PubMed=18261223;
RA Nakamura T.Y., Coetzee W.A.;
RT "Functional and pharmacological characterization of a Shal-related K+
RT channel subunit in Zebrafish.";
RL BMC Physiol. 8:2-2(2008).
RN [2] {ECO:0000313|Ensembl:ENSDARP00000114104}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000114104};
RG Ensembl;
RL Submitted (FEB-2012) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSDARP00000114104, ECO:0000313|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000114104};
RX PubMed=23594743; DOI=10.1038/nature12111;
RG Genome Reference Consortium Zebrafish;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [4] {ECO:0000313|RefSeq:NP_001076336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001076336.1};
RX PubMed=26469318;
RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M.,
RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D.,
RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E.,
RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M.,
RA Reith W., Hertzano R.;
RT "RFX transcription factors are essential for hearing in mice.";
RL Nat. Commun. 6:8549-8549(2015).
RN [5] {ECO:0000313|RefSeq:NP_001076336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001076336.1};
RX PubMed=26476318;
RA Wu M., Wu D., Wang C., Guo Z., Li B., Zuo Z.;
RT "Hexabromocyclododecane exposure induces cardiac hypertrophy and arrhythmia
RT by inhibiting miR-1 expression via up-regulation of the homeobox gene
RT Nkx2.5.";
RL J. Hazard. Mater. 302:304-313(2016).
RN [6] {ECO:0000313|RefSeq:NP_001076336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001076336.1};
RX PubMed=28252024;
RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A.,
RA Choudhary J.S., Emes R.D., Grant S.G.;
RT "Evolution of complexity in the zebrafish synapse proteome.";
RL Nat. Commun. 8:14613-14613(2017).
RN [7] {ECO:0000313|Ensembl:ENSDARP00000154866}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000154866};
RG Ensembl;
RL Submitted (APR-2018) to UniProtKB.
RN [8] {ECO:0000313|RefSeq:NP_001076336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001076336.1};
RX PubMed=31031593;
RA Tsata V., Kroehne V., Reinhardt S., El-Armouche A., Brand M., Wagner M.,
RA Reimer M.M.;
RT "Electrophysiological Properties of Adult Zebrafish Oligodendrocyte
RT Progenitor Cells.";
RL Front. Cell. Neurosci. 13:102-102(2019).
RN [9] {ECO:0000313|RefSeq:NP_001076336.1, ECO:0000313|RefSeq:XP_005164719.1}
RP IDENTIFICATION.
RC STRAIN=Tuebingen {ECO:0000313|RefSeq:NP_001076336.1,
RC ECO:0000313|RefSeq:XP_005164719.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, dendrite
CC {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic spine
CC {ECO:0000256|ARBA:ARBA00004552}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. Postsynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034100}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily.
CC {ECO:0000256|ARBA:ARBA00009309}.
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DR EMBL; AL929016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001076336.1; NM_001082867.2.
DR RefSeq; XP_005164719.1; XM_005164662.4.
DR STRING; 7955.ENSDARP00000154866; -.
DR PaxDb; 7955-ENSDARP00000114104; -.
DR Ensembl; ENSDART00000138890.4; ENSDARP00000114104.2; ENSDARG00000032799.7.
DR Ensembl; ENSDART00000189901.1; ENSDARP00000154866.1; ENSDARG00000032799.7.
DR GeneID; 570188; -.
DR KEGG; dre:570188; -.
DR AGR; ZFIN:ZDB-GENE-041210-70; -.
DR CTD; 3751; -.
DR ZFIN; ZDB-GENE-041210-70; kcnd2.
DR eggNOG; KOG4390; Eukaryota.
DR HOGENOM; CLU_011722_9_1_1; -.
DR OMA; VETIPCW; -.
DR OrthoDB; 1478695at2759; -.
DR TreeFam; TF313103; -.
DR Reactome; R-DRE-1296072; Voltage gated Potassium channels.
DR Reactome; R-DRE-5576894; Phase 1 - inactivation of fast Na+ channels.
DR PRO; PR:Q5VSI1; -.
DR Proteomes; UP000000437; Chromosome 4.
DR Bgee; ENSDARG00000032799; Expressed in brain and 5 other cell types or tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR004055; K_chnl_volt-dep_Kv4.2.
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; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF265; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 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; PR00169; KCHANNEL.
DR PRINTS; PR01517; KV42CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium channel {ECO:0000256|ARBA:ARBA00022826};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001076336.1};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..630
FT /note="Potassium voltage-gated channel subfamily D member
FT 2"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001076336.1"
FT /id="PRO_5035034702"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 323..344
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 384..405
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 40..139
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
SQ SEQUENCE 630 AA; 70904 MW; CCA0DEEF8E18CD1A CRC64;
MAAGVAAWLP FARAAAIGWM PVASAPMPPP PRDKKRGQDG LIILNVSGTR FQTWRNTLER
YPDTLLGSTE RDFFFHEETN EYFFDRDPDI FRHILNFYRT GKLHYPRHEC ISAYDEELAF
FGIIPEIIGD CCYEEYKDRR RENAERIQDD EENDNNNDLV MPDLSFRESM WRAFENPHTS
TMALVFYYVT GFFIAVSVMA NVVETVPCGI SLNRAKELSC GERYALAFFC LDTACVMIFT
VEYLLRLIAA PSRYKFVKSV MSIIDVVAIM PYYIGLVMTD NEDVSGAFVT LRVFRVFRIF
KFSRHSAGLR ILGYTLKSCA SELGFLLFSL TMAIIIFATV MFYAEKGSSA SKFTSIPAAF
WYTIVTMTTL GYGDMVPKTI MGKIFGSICS LSGVLVIALP VPVIVSNFSR IYHQSQRAEK
RRAQKKTRLA RIRAAKSGGA NAYLQYKRNG MLVDMEEEAS KEAGQALVCK ANPTFETQHH
HLLHCLEKTT NHEFVDEQTY ETSCMEVSLA KPSMSRSSSM SSSPHGLSSC CTRRNKRKSF
NVPNSNMAGG RRGSIQELST IQIRERPLSN SRSSLNAKFE ETVPLNSEEP SYITAAVISM
PTPPVTTPEG VDLASSHDFL QSNIVRVSAL
//
