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Database: UniProt
Entry: W5N4S1_LEPOC
LinkDB: W5N4S1_LEPOC
Original site: W5N4S1_LEPOC 
ID   W5N4S1_LEPOC            Unreviewed;       849 AA.
AC   W5N4S1;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 26.
DE   SubName: Full=Potassium voltage-gated channel subfamily Q member 3 {ECO:0000313|Ensembl:ENSLOCP00000015630};
GN   Name=KCNQ3 {ECO:0000313|Ensembl:ENSLOCP00000015630};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000015630, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Ensembl:ENSLOCP00000015630, ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000015630}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2014) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the potassium channel family.
CC       {ECO:0000256|SAAS:SAAS00692852}.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data. {ECO:0000313|Ensembl:ENSLOCP00000015630}.
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DR   EMBL; AHAT01002476; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01002477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015210100.1; XM_015354614.1.
DR   Ensembl; ENSLOCT00000015659; ENSLOCP00000015630; ENSLOCG00000012702.
DR   GeneID; 102684269; -.
DR   CTD; 3786; -.
DR   GeneTree; ENSGT00550000074513; -.
DR   OMA; RNEPYVA; -.
DR   OrthoDB; EOG091G02ZT; -.
DR   Proteomes; UP000018468; Unassembled WGS sequence.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR020969; Ankyrin-G_BS.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR003948; K_chnl_volt-dep_KCNQ3.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   PANTHER; PTHR11537:SF5; PTHR11537:SF5; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 1.
DR   Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01462; KCNQ3CHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000018468};
KW   Ion channel {ECO:0000256|SAAS:SAAS00417203};
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:UP000018468};
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}.
FT   TRANSMEM    100    120       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    132    154       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    175    192       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    238    259       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    312    338       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      102    334       Ion_trans. {ECO:0000259|Pfam:PF00520}.
FT   DOMAIN      429    631       KCNQ_channel. {ECO:0000259|Pfam:PF03520}.
SQ   SEQUENCE   849 AA;  95429 MW;  1F112598013A1D42 CRC64;
     MGIKSRNVGN ASVEQRDKKA GLPGDLDQGT LGLGAGADKD GALLLVGPSR DDFKRGSQGI
     GLLAKTPLGY TRPVKRNNIR YRRTQNLIYD ALERPRGWAL LYHAFVFLIV LGCLILAILT
     TFKEHEKVSA HWLVILETFT IFIFGAEFAL RIWAAGCCCR YKGWRGRLKF ARKPLCILDI
     FVLIASVPVV AVRNQGNVLA TSLRSLRFLQ ILRMLRMDRR GGTWKLLGSA IYAHSKELIT
     AWYIGFLSLI LASFLVYLVE KDDITVEVTD GPTTQPPSQD FDTYADALWW GLITLTTIGY
     GDKTPKTWAG RLLAGTFALI GVSFFALPAG ILGSGLALKV QEQHRQKHFE KRRHPAAGLI
     QSAWRYYATN PVRSDLIATW RFYESIISLP CFRKDQMEGV ASSQKLSLLE RVRQSNPRAS
     AIKGKLFMPM STDTIEESPS KEPKPGGFSN RERFRTAFRM KAYAFRQSSE DAAALPDPAC
     EDRGFPSDLI LEEMIPTLKT VIRAVRILKF LLNKKRFKET LRPYDVKDVI EQYSAGHLDM
     LSRIKYLQTR IDMILAPGPP STPKHKKAQK GPFSYPSQQS PRHDPYIAKA SGPEAEDQSM
     MGRFVKVEKQ VEHMEKKLDF LVDMHIQRMD HMQVDPVTNE VAVDSCIPQS HTAEKEDSRY
     TEIRRVFFNY AETCPHMSFQ IPVSKVMPYG FFQKEPSDTG FPADRPGCIM LPPSTVPSYM
     ERPSVLPIST LMDTRRDSDG EFQSPFMDYL SPRQGRTVVR DTDTPLSLLS VNHEELERSP
     SGFSISQDRD DLTFGPCGGG SSWMKEKRYL AEGETDTDTD PFTPSGPLPL SSTGEGFPDS
     VWTTPSNPN
//
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