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Potassium voltage-gated channel subfamily A member 4 (BAK4) (Voltage-gated potassium channel subunit Kv1.4)

 KCNA4_BOVIN             Reviewed;         660 AA.
Q05037;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
28-FEB-2018, entry version 115.
RecName: Full=Potassium voltage-gated channel subfamily A member 4;
AltName: Full=BAK4;
AltName: Full=Voltage-gated potassium channel subunit Kv1.4;
Name=KCNA4;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Adrenal medulla;
PubMed=1505668; DOI=10.1016/0014-5793(92)81294-V;
Garcia-Guzman M., Calvo S., Cena V., Criado M.;
"Molecular cloning and permanent expression in a neuroblastoma cell
line of a fast inactivating potassium channel from bovine adrenal
medulla.";
FEBS Lett. 308:283-289(1992).
[2]
SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=8110763; DOI=10.1021/bi00173a001;
Scott V.E., Muniz Z.M., Sewing S., Lichtinghagen R., Parcej D.N.,
Pongs O., Dolly J.O.;
"Antibodies specific for distinct Kv subunits unveil a
heterooligomeric basis for subtypes of alpha-dendrotoxin-sensitive K+
channels in bovine brain.";
Biochemistry 33:1617-1623(1994).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes. Forms
tetrameric potassium-selective channels through which potassium
ions pass in accordance with their electrochemical gradient. The
channel alternates between opened and closed conformations in
response to the voltage difference across the membrane
(PubMed:1505668). Can form functional homotetrameric channels and
heterotetrameric channels that contain variable proportions of
KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as
well; channel properties depend on the type of alpha subunits that
are part of the channel (By similarity). Channel properties are
modulated by cytoplasmic beta subunits that regulate the
subcellular location of the alpha subunits and promote rapid
inactivation. In vivo, membranes probably contain a mixture of
heteromeric potassium channel complexes, making it difficult to
assign currents observed in intact tissues to any particular
potassium channel family member. Homotetrameric KCNA4 forms a
potassium channel that opens in response to membrane
depolarization, followed by rapid spontaneous channel closure
(PubMed:1505668). Likewise, a heterotetrameric channel formed by
KCNA1 and KCNA4 shows rapid inactivation (By similarity).
{ECO:0000250|UniProtKB:P15385, ECO:0000269|PubMed:1505668}.
-!- SUBUNIT: Homotetramer and heterotetramer of potassium channel
proteins (By similarity). Interacts with KCNAB1 and KCNAB2 (By
similarity). Binds PDZ domains of DLG1, DLG2 and DLG4 (By
similarity). Interacts with SIGMAR1 (By similarity). Detected in a
complex with KCNA1 (PubMed:8110763). Interacts with KCNA2 (By
similarity). Part of a complex containing KCNA1, KCNAB1 and LGI1
(By similarity). Interacts (via cytoplasmic N-terminal domain)
with KCNRG (By similarity). {ECO:0000250|UniProtKB:P15385,
ECO:0000250|UniProtKB:P22459, ECO:0000269|PubMed:8110763}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1505668};
Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
{ECO:0000250|UniProtKB:P15385}.
-!- TISSUE SPECIFICITY: Detected in cerebellum, corpus striatum,
hippocampus, cerebral cortex and brain stem (at protein level).
{ECO:0000269|PubMed:8110763}.
-!- DOMAIN: The N-terminus may be important in determining the rate of
inactivation of the channel while the tail may play a role in
modulation of channel activity and/or targeting of the channel to
specific subcellular compartments. {ECO:0000250|UniProtKB:Q28527}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
(TC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X57033; CAA40349.1; -; mRNA.
PIR; S24125; S24125.
UniGene; Bt.309; -.
ProteinModelPortal; Q05037; -.
SMR; Q05037; -.
STRING; 9913.ENSBTAP00000027710; -.
PaxDb; Q05037; -.
PRIDE; Q05037; -.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
HOVERGEN; HBG052230; -.
InParanoid; Q05037; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
Gene3D; 1.20.120.350; -; 1.
Gene3D; 1.20.5.600; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR020467; K_chnl_volt-dep_Kv1.4.
InterPro; IPR012897; K_chnl_volt-dep_Kv1.4_TID.
InterPro; IPR037065; K_chnl_volt-dep_Kv1.4_TID_sf.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF07941; K_channel_TID; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01511; KV14CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Cell membrane; Cell projection; Complete proteome; Glycoprotein;
Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 660 Potassium voltage-gated channel subfamily
A member 4.
/FTId=PRO_0000053980.
TOPO_DOM 1 312 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 313 334 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 335 378 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 379 400 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 401 411 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 412 432 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 433 447 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 448 468 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 469 483 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 484 505 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 506 519 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 520 531 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 532 539 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 540 546 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 547 575 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 576 660 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 470 483 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 532 537 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 658 660 PDZ-binding. {ECO:0000250}.
COMPBIAS 38 50 Poly-Ala.
COMPBIAS 53 59 Poly-Gly.
COMPBIAS 62 65 Poly-His.
COMPBIAS 83 87 Poly-Arg.
COMPBIAS 131 137 Poly-Glu.
COMPBIAS 162 173 Poly-Gly.
COMPBIAS 441 444 Poly-Gln.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:Q61423}.
MOD_RES 607 607 Phosphoserine; by PKA. {ECO:0000250}.
CARBOHYD 360 360 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 660 AA; 73513 MW; A1FAEE59677929D5 CRC64;
MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGGGGSGGS
QHHHHPSRGA CTSHDPQSGR GSRRRRRPHP EKKKVHHRQS SFPHCSDLMP SGSEEKILRD
LSEEDEEEDD EEDEEEEGRF YYSEEDHGEE CSYTDLLAQD DGGGGGGGSG GGGYSSVRYS
DCCERVVINV SGLRFETQMK TLAQFPETLL GDPEKRTQYF DPLRNEYFFD RNRPSFDAIL
YYYQSGGRLK RPVNVPFDIF TEEVKFYQLG EEALLKFRED EGFVREEEDR ALPENEFKKQ
IWLLFEYPES SSPARGIAIV SVLVILISIV IFCLETLPEF RDDRDLIMAL STGGHGGLLN
DTSAPHPENS GHTIFNDPFF IVETVCIVWF SFEFVVRCFA CPSQALFFKN IMNIIDIVSI
LPYFITLGTD LAQQQGGGNG QQQQAMSFAI LRIIRLVRVF RIFKLSRHSK GLQILGHTLR
ASMRELGLLI FFLFIGVILF SSAVYFAEAD EPTTHFQSIP DAFWWAVVTM TTVGYGDMKP
ITVGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE NEEQTQLTQN AVSCPYLPSN
LLKKFRSSTS SSLGDKSEYL EMEEGVKESL CAKEKCQGKG DDSETDKNNV SNAKAVETDV


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