KCNA4_BOVIN
ID KCNA4_BOVIN Reviewed; 660 AA.
AC Q05037;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 4;
DE AltName: Full=BAK4;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.4;
GN Name=KCNA4;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Adrenal medulla;
RX PubMed=1505668; DOI=10.1016/0014-5793(92)81294-v;
RA Garcia-Guzman M., Calvo S., Cena V., Criado M.;
RT "Molecular cloning and permanent expression in a neuroblastoma cell line of
RT a fast inactivating potassium channel from bovine adrenal medulla.";
RL FEBS Lett. 308:283-289(1992).
RN [2]
RP SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=8110763; DOI=10.1021/bi00173a001;
RA Scott V.E., Muniz Z.M., Sewing S., Lichtinghagen R., Parcej D.N., Pongs O.,
RA Dolly J.O.;
RT "Antibodies specific for distinct Kv subunits unveil a heterooligomeric
RT basis for subtypes of alpha-dendrotoxin-sensitive K+ channels in bovine
RT brain.";
RL Biochemistry 33:1617-1623(1994).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes. Forms tetrameric potassium-
CC selective channels through which potassium ions pass in accordance with
CC their electrochemical gradient. The channel alternates between opened
CC and closed conformations in response to the voltage difference across
CC the membrane (PubMed:1505668). Can form functional homotetrameric
CC channels and heterotetrameric channels that contain variable
CC proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family
CC members as well; channel properties depend on the type of alpha
CC subunits that are part of the channel (By similarity). Channel
CC properties are modulated by cytoplasmic beta subunits that regulate the
CC subcellular location of the alpha subunits and promote rapid
CC inactivation. In vivo, membranes probably contain a mixture of
CC heteromeric potassium channel complexes, making it difficult to assign
CC currents observed in intact tissues to any particular potassium channel
CC family member. Homotetrameric KCNA4 forms a potassium channel that
CC opens in response to membrane depolarization, followed by rapid
CC spontaneous channel closure (PubMed:1505668). Likewise, a
CC heterotetrameric channel formed by KCNA1 and KCNA4 shows rapid
CC inactivation (By similarity). {ECO:0000250|UniProtKB:P15385,
CC ECO:0000269|PubMed:1505668}.
CC -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins
CC (By similarity). Interacts with KCNAB1 and KCNAB2 (By similarity).
CC Binds PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts
CC with SIGMAR1 (By similarity). Detected in a complex with KCNA1
CC (PubMed:8110763). Interacts with KCNA2 (By similarity). Part of a
CC complex containing KCNA1, KCNAB1 and LGI1 (By similarity). Interacts
CC (via cytoplasmic N-terminal domain) with KCNRG (By similarity).
CC {ECO:0000250|UniProtKB:P15385, ECO:0000250|UniProtKB:P22459,
CC ECO:0000269|PubMed:8110763}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1505668};
CC Multi-pass membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P15385}.
CC -!- TISSUE SPECIFICITY: Detected in cerebellum, corpus striatum,
CC hippocampus, cerebral cortex and brain stem (at protein level).
CC {ECO:0000269|PubMed:8110763}.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments. {ECO:0000250|UniProtKB:Q28527}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Kv1.4/KCNA4 sub-subfamily. {ECO:0000305}.
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DR EMBL; X57033; CAA40349.1; -; mRNA.
DR PIR; S24125; S24125.
DR AlphaFoldDB; Q05037; -.
DR BMRB; Q05037; -.
DR SMR; Q05037; -.
DR CORUM; Q05037; -.
DR STRING; 9913.ENSBTAP00000027710; -.
DR PaxDb; Q05037; -.
DR PRIDE; Q05037; -.
DR eggNOG; KOG1545; Eukaryota.
DR InParanoid; Q05037; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 1.20.5.600; -; 1.
DR Gene3D; 3.30.710.10; -; 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; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF07941; K_channel_TID; 1.
DR PRINTS; PR01511; KV14CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..660
FT /note="Potassium voltage-gated channel subfamily A member
FT 4"
FT /id="PRO_0000053980"
FT TOPO_DOM 1..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 313..334
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 335..378
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 379..400
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 401..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 412..432
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 433..447
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 448..468
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 469..483
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 484..505
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 506..519
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 520..531
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 532..539
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 540..546
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 547..575
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 576..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 24..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..483
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 636..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 532..537
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 658..660
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..99
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61423"
FT MOD_RES 607
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
