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Database: UniProt
Entry: Q5BLW6_BOVIN
LinkDB: Q5BLW6_BOVIN
Original site: Q5BLW6_BOVIN 
ID   Q5BLW6_BOVIN            Unreviewed;       491 AA.
AC   Q5BLW6;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   25-OCT-2017, entry version 96.
DE   SubName: Full=Potassium voltage-gated channel delayed rectifier subfamily S member 3 {ECO:0000313|EMBL:AAX33295.1};
DE   SubName: Full=Potassium voltage-gated channel modifier subfamily S member 3 {ECO:0000313|Ensembl:ENSBTAP00000025570};
GN   Name=KCNS3 {ECO:0000313|EMBL:AAX33295.1,
GN   ECO:0000313|Ensembl:ENSBTAP00000025570};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAX33295.1};
RN   [1] {ECO:0000313|EMBL:AAX33295.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lens epithelium {ECO:0000313|EMBL:AAX33295.1};
RX   PubMed=10484328;
RA   Shepard A.R., Rae J.L.;
RT   "Electrically silent potassium channel subunits from human lens
RT   epithelium.";
RL   Am. J. Physiol. 277:C412-C424(1999).
RN   [2] {ECO:0000313|EMBL:AAX33295.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lens epithelium {ECO:0000313|EMBL:AAX33295.1};
RA   Rae J.L.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSBTAP00000025570, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000025570,
RC   ECO:0000313|Proteomes:UP000009136};
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C.,
RA   Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S.,
RA   Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
RN   [4] {ECO:0000313|Ensembl:ENSBTAP00000025570}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000025570};
RG   Ensembl;
RL   Submitted (MAR-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the potassium channel family.
CC       {ECO:0000256|SAAS:SAAS00692852}.
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DR   EMBL; DAAA02031803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY940664; AAX33295.1; -; mRNA.
DR   RefSeq; NP_001013624.1; NM_001013606.1.
DR   RefSeq; XP_005213093.1; XM_005213036.3.
DR   RefSeq; XP_005213094.1; XM_005213037.3.
DR   RefSeq; XP_010808544.1; XM_010810242.2.
DR   RefSeq; XP_010808545.1; XM_010810243.2.
DR   RefSeq; XP_015329027.1; XM_015473541.1.
DR   UniGene; Bt.33145; -.
DR   STRING; 9913.ENSBTAP00000025570; -.
DR   Ensembl; ENSBTAT00000025570; ENSBTAP00000025570; ENSBTAG00000019212.
DR   GeneID; 541460; -.
DR   KEGG; bta:541460; -.
DR   CTD; 3790; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   GeneTree; ENSGT00760000118981; -.
DR   HOGENOM; HOG000231016; -.
DR   HOVERGEN; HBG052230; -.
DR   KO; K04933; -.
DR   OMA; WDQKSND; -.
DR   OrthoDB; EOG091G0FP3; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-BTA-1296072; Voltage gated Potassium channels.
DR   Reactome; R-BTA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000019212; -.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated 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   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
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   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000009136};
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:UP000009136};
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    324    343       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    355    373       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    385    406       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       15    124       BTB. {ECO:0000259|SMART:SM00225}.
SQ   SEQUENCE   491 AA;  56148 MW;  69FB4CE2A5DBBD54 CRC64;
     MVFGEFFHRP GPDEELVNLN VGGFKQTVDQ STLLRFPHTR LGKLLSCHSE EAILELCDDY
     SVADKEYYFD RNPSLFRYVL NFYYTGKLHV MEELCVFSFC QEIEYWGINE LFLDSCCSNR
     YQERKEENHE KDWDQKSNDV STDSSFEESS LFEKELEKFD KLRFGQLRKK IWIRMENPAY
     CLSAKLIAIS SLSVVLASIV AMCIHSMSEF QNEDGEVDDP VLEGVEIACI AWFTGELVIR
     LVTAPCQKKF WKNPLNIIDF VSIVPFYATL AVDTKEEESE DIENMGKVVQ ILRLMRIFRI
     LKLARHSVGL RSLGATLRHS YHEVGLLLLF LSVGISIFSV LIYSVEKDDH TSSLTSIPVC
     WWWATISMTT VGYGDTHPVT LVGKLIASTC IICGILVVAL PITIIFNKFS KYYQKQKDID
     VDQCSEDPPE KCQELPYFNI RDIYAQRMHA FITSLSSVGI MVSDPDSTDA SSIEDNEDVY
     NTASLENCPP M
//
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