ID   KCNA6_MOUSE             Reviewed;         529 AA.
AC   Q61923;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 6;
DE   AltName: Full=MK1.6;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.6;
GN   Name=Kcna6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=1285906;
RA   Migeon M.B., Street V.A., Demas V.P., Tempel B.L.;
RT   "Cloning, sequence and chromosomal localization of MK1.6, a murine
RT   potassium channel gene.";
RL   Epilepsy Res. Suppl. 9:173-180(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 (By similarity). The channel alternates
CC       between opened and closed conformations in response to the voltage
CC       difference across the membrane (By similarity). Can form functional
CC       homotetrameric channels and heterotetrameric channels that contain
CC       variable proportions of KCNA1, KCNA2, KCNA4, KCNA6, and possibly other
CC       family 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 (By similarity). Homotetrameric channels display rapid
CC       activation and slow inactivation (By similarity).
CC       {ECO:0000250|UniProtKB:P17658, ECO:0000250|UniProtKB:P17659}.
CC   -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins
CC       (Probable). Interacts with KCNAB1 and KCNAB2 (By similarity).
CC       {ECO:0000250|UniProtKB:P17659, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17658};
CC       Multi-pass membrane protein {ECO:0000305}.
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.
CC   -!- DOMAIN: The transmembrane segment S4 functions as a voltage-sensor and
CC       is 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)
CC       (TC 1.A.1.2) subfamily. Kv1.6/KCNA6 sub-subfamily. {ECO:0000305}.
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DR   EMBL; M96688; AAA39772.1; -; mRNA.
DR   EMBL; BC048782; AAH48782.1; -; mRNA.
DR   EMBL; BC054804; AAH54804.1; -; mRNA.
DR   CCDS; CCDS20556.1; -.
DR   PIR; S09043; S09043.
DR   RefSeq; NP_038596.1; NM_013568.6.
DR   RefSeq; XP_006505701.1; XM_006505638.3.
DR   RefSeq; XP_006505702.1; XM_006505639.3.
DR   RefSeq; XP_011239530.1; XM_011241228.2.
DR   AlphaFoldDB; Q61923; -.
DR   SMR; Q61923; -.
DR   BioGRID; 200881; 1.
DR   STRING; 10090.ENSMUSP00000139481; -.
DR   iPTMnet; Q61923; -.
DR   PhosphoSitePlus; Q61923; -.
DR   SwissPalm; Q61923; -.
DR   MaxQB; Q61923; -.
DR   PaxDb; 10090-ENSMUSP00000107861; -.
DR   PeptideAtlas; Q61923; -.
DR   ProteomicsDB; 269450; -.
DR   ABCD; Q61923; 1 sequenced antibody.
DR   Antibodypedia; 3161; 138 antibodies from 22 providers.
DR   DNASU; 16494; -.
DR   Ensembl; ENSMUST00000040751.6; ENSMUSP00000036872.6; ENSMUSG00000038077.8.
DR   Ensembl; ENSMUST00000112242.2; ENSMUSP00000107861.2; ENSMUSG00000038077.8.
DR   Ensembl; ENSMUST00000185333.2; ENSMUSP00000139481.2; ENSMUSG00000038077.8.
DR   GeneID; 16494; -.
DR   KEGG; mmu:16494; -.
DR   UCSC; uc009dvd.2; mouse.
DR   AGR; MGI:96663; -.
DR   CTD; 3742; -.
DR   MGI; MGI:96663; Kcna6.
DR   VEuPathDB; HostDB:ENSMUSG00000038077; -.
DR   eggNOG; KOG1545; Eukaryota.
DR   GeneTree; ENSGT00940000162469; -.
DR   HOGENOM; CLU_011722_4_0_1; -.
DR   InParanoid; Q61923; -.
DR   OMA; STPHRVY; -.
DR   OrthoDB; 1478695at2759; -.
DR   PhylomeDB; Q61923; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 16494; 2 hits in 75 CRISPR screens.
DR   PRO; PR:Q61923; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q61923; Protein.
DR   Bgee; ENSMUSG00000038077; Expressed in cerebral cortex marginal layer and 133 other cell types or tissues.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0043679; C:axon terminus; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0005251; F:delayed rectifier 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   CDD; cd18407; BTB_POZ_KCNA6; 1.
DR   Gene3D; 1.10.287.70; -; 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; IPR004053; KCNA6.
DR   InterPro; IPR046988; KCNA6_BTB_POZ.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537:SF104; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY A MEMBER 6; 1.
DR   PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01513; KV16CHANNEL.
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.
DR   Genevisible; Q61923; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion channel; Ion transport; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..529
FT                   /note="Potassium voltage-gated channel subfamily A member
FT                   6"
FT                   /id="PRO_0000053991"
FT   TOPO_DOM        1..171
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        172..193
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        194..262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        263..284
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        285..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        296..316
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        317..337
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        338..358
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        359..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        374..395
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        396..409
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        410..421
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        422..429
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        430..436
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        437..465
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        466..529
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          203..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..373
FT                   /note="S4-S5 linker"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   REGION          488..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           422..427
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   MOTIF           527..529
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         511
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000305"
FT   LIPID           285
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   529 AA;  58674 MW;  336D78C069ABEADD CRC64;
     MRSEKSLTLA APGEVRGPEG EQQDAGEFQE AEGGGGCCSS ERLVINISGL RFETQLRTLS
     LFPDTLLGDP GRRVRFFDPL RNEYFFDRNR PSFDAILYYY QSGGRLRRPV NVPLDIFMEE
     IRFYQLGEEA LAAFREDEGC LPEGGEDEKP LPSQPFQRQV WLLFEYPESS GPARGIAIVS
     VLVILISIVI FCLETLPQFR ADGRGGSNEG SGTRLSPASR SHEEEDEDED SYAFPGSIPS
     GGLGTGGTSS LSTLGGSFFT DPFFLVETLC IVWFTFELLV RFSACPSKAA FFRNIMNIID
     LVAIFPYFIT LGTELVQRHE QQSVSGGSGQ NGQQAMSLAI LRVIRLVRVF RIFKLSRHSK
     GLQILGKTLQ ASMRELGLLI FFLFIGVILF SSAVYFAEAD DVDSLFPSIP DAFWWAVVTM
     TTVGYGDMYP MTVGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE QEEQGQYTHV
     TCGQPTPDLK ATDNGLGKPD FAEASRERRP SYLPTPHRAY AEKRMLTEV
//