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Database: UniProt
Entry: E1AZA5_DANRE
LinkDB: E1AZA5_DANRE
Original site: E1AZA5_DANRE 
ID   E1AZA5_DANRE            Unreviewed;       659 AA.
AC   E1AZA5;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   22-NOV-2017, entry version 67.
DE   SubName: Full=Potassium voltage-gated channel, Shaw-related subfamily, member 3a {ECO:0000313|Ensembl:ENSDARP00000124090};
DE   SubName: Full=Voltage-gated potassium channel Kv3.3a variant 2 {ECO:0000313|EMBL:ADM18971.1};
GN   Name=kcnc3a {ECO:0000313|EMBL:ADM18971.1,
GN   ECO:0000313|Ensembl:ENSDARP00000124090,
GN   ECO:0000313|ZFIN:ZDB-GENE-100901-1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:ADM18971.1};
RN   [1] {ECO:0000313|EMBL:ADM18971.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=AB {ECO:0000313|EMBL:ADM18971.1};
RX   PubMed=20712895; DOI=10.1186/1471-2202-11-99;
RA   Mock A.F., Richardson J.L., Hsieh J.Y., Rinetti G., Papazian D.M.;
RT   "Functional effects of spinocerebellar ataxia type 13 mutations are
RT   conserved in zebrafish Kv3.3 channels.";
RL   BMC Neurosci. 11:99-99(2010).
RN   [2] {ECO:0000313|Ensembl:ENSDARP00000124090}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000124090};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000124090, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000124090,
RC   ECO:0000313|Proteomes:UP000000437};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J.,
RA   Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P.,
RA   Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G.,
RA   Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D.,
RA   Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K.,
RA   Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C.,
RA   Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J.,
RA   Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S.,
RA   Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A.,
RA   Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D.,
RA   Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z.,
RA   Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J.,
RA   Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C.,
RA   Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C.,
RA   Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human genome.";
RL   Nature 496:498-503(2013).
RN   [4] {ECO:0000313|Ensembl:ENSDARP00000138260}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000138260};
RG   Ensembl;
RL   Submitted (NOV-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the potassium channel family.
CC       {ECO:0000256|SAAS:SAAS00692852}.
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DR   EMBL; BX324157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX511080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; HQ118213; ADM18971.1; -; mRNA.
DR   RefSeq; NP_001182169.1; NM_001195240.1.
DR   RefSeq; XP_005164092.1; XM_005164035.3.
DR   UniGene; Dr.34696; -.
DR   Ensembl; ENSDART00000148861; ENSDARP00000124090; ENSDARG00000055855.
DR   Ensembl; ENSDART00000163158; ENSDARP00000138260; ENSDARG00000055855.
DR   GeneID; 559096; -.
DR   CTD; 559096; -.
DR   ZFIN; ZDB-GENE-100901-1; kcnc3a.
DR   eggNOG; KOG3713; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   GeneTree; ENSGT00760000118846; -.
DR   Reactome; R-DRE-1296072; Voltage gated Potassium channels.
DR   Proteomes; UP000000437; Chromosome 3.
DR   Bgee; ENSDARG00000055855; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:ZFIN.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR   GO; GO:0048666; P:neuron development; IMP:ZFIN.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR021105; K_chnl_volt-dep_Kv3_ID.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF11404; Potassium_chann; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000437};
KW   Ion channel {ECO:0000256|SAAS:SAAS00417203,
KW   ECO:0000313|EMBL:ADM18971.1};
KW   Ion transport {ECO:0000256|SAAS:SAAS00417186};
KW   Membrane {ECO:0000256|SAAS:SAAS00788393, ECO:0000256|SAM:Phobius};
KW   Potassium {ECO:0000256|SAAS:SAAS00417282};
KW   Potassium channel {ECO:0000256|SAAS:SAAS00417246};
KW   Potassium transport {ECO:0000256|SAAS:SAAS00417240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00793138,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00789957,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|SAAS:SAAS00417268};
KW   Voltage-gated channel {ECO:0000256|SAAS:SAAS00091688}.
FT   TRANSMEM    206    225       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    363    384       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    405    422       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    434    463       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       36    140       BTB. {ECO:0000259|SMART:SM00225}.
SQ   SEQUENCE   659 AA;  73212 MW;  39877E1DEAF81470 CRC64;
     MLSSVCVSSF KGRKGGNKSS NKACYSADMT CPSDSEKIVI NCGGIRHETY RSTLKTLPGT
     RLSWLTEPDA FSNFDYDPKS DEFFFDRHPN TFAFILNYYR TGKLHCPSDV CGPLFEEELA
     FWGIDETDVE ACCWMNYRQH RDAEEALDSF ETPEPDPPED DPALTGGADG DLKRLCLQED
     GRNPSRWSTW QPWVWALFED PYSSKYARYV AFGSLLFILI SISTFCLETH EAFNTIYNKT
     ENVTVGNVTR EEVVFEVVTD NWLTYVEGVC VVWFTIEVFT RVIFCPDKAE FFKSSLNIID
     FVAILPFYLE MALSGLSSKA AKDVLGFLRV VRFVRILRIF KLTRHFVGLR VLGHTLRAST
     NEFLLLIIFL ALGVLIFATM IYYAERIGAD PDDPTASAHT AFKNIPIGFW WAVVTMTTLG
     YGDMYPETWS GMLVGALCAL AGVLTIAMPV PVIVNNFGMY YSLAMAKQKL PKKKNKHIPR
     APQPGSPNYC KPDALAMATA SPHRIMGNVL GSMVVSGSMA GDCPLAQEEI IEINRADSKQ
     NGDAANAALA NEDCPTIDQV LGPDDRSPAT GGLGTGTGRE RYPHDRACFL LSTGEFRTTD
     SNVRKAAGYE KSRSLNNISG MTGAPLRLTP ITPINNPPYE PYESPGPLRR CRSPIPSIL
//
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