KCNA6_RAT
ID KCNA6_RAT Reviewed; 530 AA.
AC P17659; P19025;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Potassium voltage-gated channel subfamily A member 6;
DE AltName: Full=RCK2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv1.6;
DE AltName: Full=Voltage-gated potassium channel subunit Kv2;
GN Name=Kcna6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain cortex;
RX PubMed=2347305; DOI=10.1002/j.1460-2075.1990.tb08299.x;
RA Grupe A., Schroeter K.H., Ruppersberg J.P., Stocker M., Drewes T.,
RA Beckh S., Pongs O.;
RT "Cloning and expression of a human voltage-gated potassium channel. A novel
RT member of the RCK potassium channel family.";
RL EMBO J. 9:1749-1756(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Brain;
RX PubMed=2361015; DOI=10.1016/0896-6273(90)90146-7;
RA Swanson R., Marshall J., Smith J., Williams J., Boyle M.B., Folander K.,
RA Luneau C.J., Antanavage J., Oliva C., Buhrow S.A., Bennett C., Stein R.B.,
RA Kaczmarek L.M.;
RT "Cloning and expression of cDNA and genomic clones encoding three delayed
RT rectifier potassium channels in rat brain.";
RL Neuron 4:929-939(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
RX PubMed=1993474; DOI=10.1016/0014-5793(91)80082-e;
RA Kirsch G.E., Drewe J.A., Verma S., Brown A.M., Joho R.H.;
RT "Electrophysiological characterization of a new member of the RCK family of
RT rat brain K+ channels.";
RL FEBS Lett. 278:55-60(1991).
RN [4]
RP INTERACTION WITH KCNAB1 AND KCNAB2.
RX PubMed=9334400; DOI=10.1523/jneurosci.17-21-08246.1997;
RA Rhodes K.J., Strassle B.W., Monaghan M.M., Bekele-Arcuri Z., Matos M.F.,
RA Trimmer J.S.;
RT "Association and colocalization of the Kvbeta1 and Kvbeta2 beta-subunits
RT with Kv1 alpha-subunits in mammalian brain K+ channel complexes.";
RL J. Neurosci. 17:8246-8258(1997).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15618540; DOI=10.1161/01.res.0000154070.06421.25;
RA Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K., Chen T.,
RA Cole W.;
RT "Heteromultimeric Kv1 channels contribute to myogenic control of arterial
RT diameter.";
RL Circ. Res. 96:216-224(2005).
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. Can form functional homotetrameric channels and
CC heterotetrameric channels that contain variable proportions of KCNA1,
CC KCNA2, KCNA4, KNCA5, KCNA6, and possibly other family members as well;
CC channel properties depend on the type of alpha subunits that are part
CC of the channel (PubMed:1993474, PubMed:15618540). Channel properties
CC are modulated by cytoplasmic beta subunits that regulate the
CC subcellular location of the alpha subunits and promote rapid
CC inactivation (Probable). Homotetrameric channels display rapid
CC activation and slow inactivation (PubMed:1993474).
CC {ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:1993474, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer and heterotetramer of potassium channel proteins
CC (Probable). Interacts with KCNAB1 and KCNAB2 (PubMed:9334400).
CC {ECO:0000269|PubMed:9334400, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1993474};
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 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. Kv1.6/KCNA6 sub-subfamily. {ECO:0000305}.
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DR EMBL; X17621; CAA35622.1; -; mRNA.
DR EMBL; M27159; AAA41499.1; ALT_SEQ; Genomic_DNA.
DR PIR; JH0167; JH0167.
DR AlphaFoldDB; P17659; -.
DR SMR; P17659; -.
DR CORUM; P17659; -.
DR STRING; 10116.ENSRNOP00000067348; -.
DR BindingDB; P17659; -.
DR ChEMBL; CHEMBL4105906; -.
DR GuidetoPHARMACOLOGY; 543; -.
DR iPTMnet; P17659; -.
DR PhosphoSitePlus; P17659; -.
DR PaxDb; P17659; -.
DR PRIDE; P17659; -.
DR ABCD; P17659; 1 sequenced antibody.
DR UCSC; RGD:62083; rat.
DR RGD; 62083; Kcna6.
DR eggNOG; KOG1545; Eukaryota.
DR InParanoid; P17659; -.
DR PhylomeDB; P17659; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:P17659; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA: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; 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; IPR004053; KCNA6.
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 PANTHER; PTHR11537:SF104; PTHR11537:SF104; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01513; KV16CHANNEL.
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; 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..530
FT /note="Potassium voltage-gated channel subfamily A member
FT 6"
FT /id="PRO_0000053992"
FT TRANSMEM 172..193
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 264..285
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 297..317
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 339..359
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 375..396
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 411..422
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 423..430
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 438..466
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..374
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 423..428
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:0000250|UniProtKB:Q61923"
FT MOD_RES 222
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000255"
FT MOD_RES 512
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000305"
FT MOD_RES 528
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000255"
FT LIPID 286
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CONFLICT 241
FT /note="S -> L (in Ref. 3; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="R -> G (in Ref. 2; AAA41499)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 58884 MW; 30A9774B66CF1DA5 CRC64;
MRSEKSLTLA APGEVRGPEG EQQDAGEFQE AEGGGGCCSS ERLVINISGL RYETQLRTLS
LFPDTLLGDP GRRVRFFDPL RNEYFFDRNR PSFDAILYYY QSGGRLRRPV NVPLDIFMEE
IRFYQLGDEA LAAFREDEGC LPEGGEDEKP LPSQPFQRQV WLLFEYPESS GPARGIAIVS
VLVILISIVI FCLETLPQFR ADGRGGSNEG SGTRMSPASR GSHEEEDEDE DSYAFPGSIP
SGGLGTGGTS SFSTLGGSFF TDPFFLVETL CIVWFTFELL VRFSACPSKA AFFRNIMNII
DLVAIFPYFI TLGTELVQRH EQQPVSGGSG QNRQQAMSLA ILRVIRLVRV FRIFKLSRHS
KGLQILGKTL QASMRELGLL IFFLFIGVIL FSSAVYFAEA DDVDSLFPSI PDAFWWAVVT
MTTVGYGDMY PMTVGGKIVG SLCAIAGVLT IALPVPVIVS NFNYFYHRET EQEEQGQYTH
VTCGQPTPDL KATDNGLGKP DFAEASRERR SSYLPTPHRA YAEKRMLTEV
