ID F1MFZ3_BOVIN Unreviewed; 661 AA.
AC F1MFZ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 4 {ECO:0000256|ARBA:ARBA00020938};
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.4 {ECO:0000256|ARBA:ARBA00033201};
GN Name=KCNA4 {ECO:0000313|Ensembl:ENSBTAP00000027710.4,
GN ECO:0000313|VGNC:VGNC:30424};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000027710.4, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000027710.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027710.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000027710.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000027710.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC projection, axon {ECO:0000256|ARBA:ARBA00004489}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily.
CC {ECO:0000256|ARBA:ARBA00008202}.
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DR AlphaFoldDB; F1MFZ3; -.
DR SMR; F1MFZ3; -.
DR Ensembl; ENSBTAT00000027710.5; ENSBTAP00000027710.4; ENSBTAG00000020793.5.
DR VEuPathDB; HostDB:ENSBTAG00000020793; -.
DR VGNC; VGNC:30424; KCNA4.
DR GeneTree; ENSGT00940000162248; -.
DR HOGENOM; CLU_011722_4_0_1; -.
DR InParanoid; F1MFZ3; -.
DR OMA; GDECSYT; -.
DR TreeFam; TF313103; -.
DR Reactome; R-BTA-1296072; Voltage gated Potassium channels.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000020793; Expressed in prostate gland and 40 other cell types or tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022839; F:monoatomic ion-gated channel activity; IEA:UniProt.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0099508; F:voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl.
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; 1.20.5.600; Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain; 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; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR020467; K_chnl_volt-dep_Kv1.4.
DR InterPro; IPR012897; K_chnl_volt-dep_Kv1.4_TID.
DR InterPro; IPR037065; K_chnl_volt-dep_Kv1.4_TID_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537:SF284; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY A MEMBER 4; 1.
DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07941; K_channel_TID; 1.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01511; KV14CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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 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:UP000009136};
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 TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..508
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 185..285
FT /note="BTB"
FT /evidence="ECO:0000259|SMART:SM00225"
FT REGION 24..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..100
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 73558 MW; E8B8F8B6FA7AA4D0 CRC64;
MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGGGGSGGG
AQHHHHPSRG ACTSHDPQSG RGSRRRRRPH PEKKKVHHRQ SSFPHCSDLM PSGSEEKILR
DLSEEDEEED DEEDEEEEGR FYYSEEDHGE ECSYTDLLAQ DDGGGGGGGS GGGGYSSVRY
SDCCERVVIN VSGLRFETQM KTLAQFPETL LGDPEKRTQY FDPLRNEYFF DRNRPSFDAI
LYYYQSGGRL KRPVNVPFDI FTEEVKFYQL GEEALLKFRE DEGFVREEED RALPENEFKK
QIWLLFEYPE SSSPARGIAI VSVLVILISI VIFCLETLPE FRDDRDLIMA LSTGGHGGLL
NDTSAPHPEN SGHTIFNDPF FIVETVCIVW FSFEFVVRCF ACPSQALFFK NIMNIIDIVS
ILPYFITLGT DLAQQQGGGN GQQQQAMSFA ILRIIRLVRV FRIFKLSRHS KGLQILGHTL
RASMRELGLL IFFLFIGVIL FSSAVYFAEA DEPTTHFQSI PDAFWWAVVT MTTVGYGDMK
PITVGGKIVG SLCAIAGVLT IALPVPVIVS NFNYFYHRET ENEEQTQLTQ NAVSCPYLPS
NLLKKFRSST SSSLGDKSEY LEMEEGVKES LCAKEKCQGK GDDSETDKNN CSNAKAVETD
V
//