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Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)

 KCNQ2_RAT               Reviewed;         852 AA.
O88943;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
27-SEP-2017, entry version 138.
RecName: Full=Potassium voltage-gated channel subfamily KQT member 2 {ECO:0000305};
AltName: Full=KQT-like 2;
AltName: Full=Potassium channel subunit alpha KvLQT2;
AltName: Full=Voltage-gated potassium channel subunit Kv7.2;
Name=Kcnq2 {ECO:0000312|RGD:621504};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
TISSUE=Brain;
Derst C., Preisig-Mueller R., Hennighausen A., Daut J.;
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Brain;
PubMed=11038262; DOI=10.1016/S0169-328X(00)00146-7;
Jow F., Wang K.-W.;
"Cloning and functional expression of rKCNQ2 K(+) channel from rat
brain.";
Brain Res. Mol. Brain Res. 80:269-278(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, FUNCTION,
SUBCELLULAR LOCATION, AND SUBUNIT.
TISSUE=Brain, and Sympathetic ganglion;
PubMed=11230508; DOI=10.1111/j.1469-7793.2001.0347i.x;
Pan Z., Selyanko A.A., Hadley J.K., Brown D.A., Dixon J.E.,
McKinnon D.;
"Alternative splicing of KCNQ2 potassium channel transcripts
contributes to the functional diversity of M-currents.";
J. Physiol. (Lond.) 531:347-358(2001).
[4]
TISSUE SPECIFICITY.
PubMed=9836639; DOI=10.1126/science.282.5395.1890;
Wang H.-S., Pan Z., Shi W., Brown B.S., Wymore R.S., Cohen I.S.,
Dixon J.E., McKinnon D.;
"KCNQ2 and KCNQ3 potassium channel subunits: molecular correlates of
the M-channel.";
Science 282:1890-1893(1998).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-489; SER-655; SER-781
AND SER-783, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Associates with KCNQ3 to form a potassium channel with
essentially identical properties to the channel underlying the
native M-current, a slowly activating and deactivating potassium
conductance which plays a critical role in determining the
subthreshold electrical excitability of neurons as well as the
responsiveness to synaptic inputs. Therefore, it is important in
the regulation of neuronal excitability. KCNQ2 current is blocked
by barium and tetraethylammonium whereas 4-aminopyridine and
charybdotoxin have no effect on KCNQ2 current. Tyrosine kinase
inhibitors genistein or herbimycin a markedly down-regulate KCNQ2
current. As the native M-channel, the potassium channel composed
of KCNQ2 and KCNQ3 is also suppressed by activation of the
muscarinic acetylcholine receptor CHRM1.
{ECO:0000269|PubMed:11038262, ECO:0000269|PubMed:11230508}.
-!- SUBUNIT: Heterotetramer with KCNQ3; form the heterotetrameric M
potassium channel (PubMed:11230508). Interacts with calmodulin;
the interaction is calcium-independent, constitutive and
participates to the proper assembly of a functional
heterotetrameric M channel. May associate with KCNE2 (By
similarity). {ECO:0000250|UniProtKB:O43526,
ECO:0000269|PubMed:11230508}.
-!- INTERACTION:
P62161:Calm3; NbExp=4; IntAct=EBI-7900557, EBI-397530;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11038262,
ECO:0000269|PubMed:11230508}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=9;
Comment=Splice isoforms fell into three classes, those that
contain an in frame exon 16 (Isoforms A-I) those that contain an
out-of-frame exon 16 due to an alternative splice junction in
exon 14 and those that terminate prematurely to exon 16. Only
the forms containing an in frame exon 16 are able to form
functional channels. A similar splice pattern is also produced
for splice variants that contain an out-of-frame exon 16. A wide
variety of different truncated isoforms were isolated for splice
variants that terminate prematurely to exon 16.;
Name=A;
IsoId=O88943-1; Sequence=Displayed;
Name=B;
IsoId=O88943-2; Sequence=VSP_001009, VSP_001011;
Name=C;
IsoId=O88943-3; Sequence=VSP_001007;
Name=D;
IsoId=O88943-4; Sequence=VSP_001008, VSP_001010;
Name=E;
IsoId=O88943-5; Sequence=VSP_001008;
Name=F;
IsoId=O88943-6; Sequence=VSP_001007, VSP_001008, VSP_001010;
Name=G;
IsoId=O88943-7; Sequence=VSP_001011;
Name=H;
IsoId=O88943-8; Sequence=VSP_001007, VSP_001008;
Name=I;
IsoId=O88943-9; Sequence=VSP_001010;
-!- TISSUE SPECIFICITY: Expressed in brain and sympathetic ganglia. In
brain, expressed in cortex, hippocampus, and cerebellum. In
sympathetic ganglia, expressed at lower levels in celiac ganglia
and superior mesenteric ganglia than in superior cervical ganglia.
{ECO:0000269|PubMed:9836639}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position. {ECO:0000250}.
-!- PTM: KCNQ2/KCNQ3 heteromeric current can be increased by
intracellular cyclic AMP, an effect that depends on
phosphorylation of Ser-52 in the N-terminal region.
{ECO:0000250|UniProtKB:O43526}.
-!- MISCELLANEOUS: When coexpressed with KCNQ3 subunit in CHO cells or
Xenopus oocytes, isoform B was found to have significantly
different deactivation-activation kinetics. The kinetics was 2.5
times more slowly than the kinetics of other isoforms. The
presence of exon 15a in isoform B accounts for the slow
deactivation-activation kinetics. Alternative splicing of the
KCNQ2 gene may contribute to the variation in M-current kinetics
seen in vivo.
-!- SIMILARITY: Belongs to the potassium channel family. KQT (TC
1.A.1.15) subfamily. Kv7.2/KCNQ2 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF087453; AAC36722.1; -; mRNA.
RefSeq; NP_579856.1; NM_133322.1. [O88943-1]
UniGene; Rn.33317; -.
ProteinModelPortal; O88943; -.
BioGrid; 251003; 2.
IntAct; O88943; 1.
MINT; MINT-8393842; -.
STRING; 10116.ENSRNOP00000043732; -.
BindingDB; O88943; -.
ChEMBL; CHEMBL5530; -.
iPTMnet; O88943; -.
PhosphoSitePlus; O88943; -.
SwissPalm; O88943; -.
PaxDb; O88943; -.
PRIDE; O88943; -.
GeneID; 170848; -.
KEGG; rno:170848; -.
UCSC; RGD:621504; rat. [O88943-1]
CTD; 3785; -.
RGD; 621504; Kcnq2.
eggNOG; KOG1419; Eukaryota.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000220839; -.
HOVERGEN; HBG059014; -.
InParanoid; O88943; -.
KO; K04927; -.
PRO; PR:O88943; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
InterPro; IPR020969; Ankyrin-G_BS.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
InterPro; IPR003947; K_chnl_volt-dep_KCNQ2.
InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
InterPro; IPR028325; VG_K_chnl.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF03520; KCNQ_channel; 1.
Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01461; KCNQ2CHANNEL.
PRINTS; PR01459; KCNQCHANNEL.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Ion channel;
Ion transport; Membrane; Phosphoprotein; Potassium; Potassium channel;
Potassium transport; Reference proteome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 852 Potassium voltage-gated channel subfamily
KQT member 2.
/FTId=PRO_0000054032.
TOPO_DOM 1 91 Cytoplasmic. {ECO:0000255}.
TRANSMEM 92 112 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 113 122 Extracellular. {ECO:0000255}.
TRANSMEM 123 143 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 144 166 Cytoplasmic. {ECO:0000255}.
TRANSMEM 167 187 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 188 197 Extracellular. {ECO:0000255}.
TRANSMEM 198 221 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 222 231 Cytoplasmic. {ECO:0000255}.
TRANSMEM 232 252 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 253 264 Extracellular. {ECO:0000255}.
INTRAMEM 265 285 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 286 291 Extracellular. {ECO:0000255}.
TRANSMEM 292 312 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 313 852 Cytoplasmic. {ECO:0000255}.
REGION 317 522 Mediates interaction with calmodulin.
{ECO:0000250|UniProtKB:O43526}.
MOTIF 277 282 Selectivity filter. {ECO:0000250}.
MOD_RES 52 52 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:O43526}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z351}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z351}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z351}.
MOD_RES 458 458 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z351}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z351}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 655 655 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 783 783 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
VAR_SEQ 373 382 Missing (in isoform C, isoform F and
isoform H). {ECO:0000305}.
/FTId=VSP_001007.
VAR_SEQ 416 416 S -> SKGRPCRGCLCGCRPGHSS (in isoform D,
isoform E, isoform F and isoform H).
{ECO:0000305}.
/FTId=VSP_001008.
VAR_SEQ 417 428 Missing (in isoform B). {ECO:0000305}.
/FTId=VSP_001009.
VAR_SEQ 491 491 Missing (in isoform D, isoform F and
isoform I). {ECO:0000305}.
/FTId=VSP_001010.
VAR_SEQ 571 571 R -> RIDMIVGPPPPSTPRHKKYPTKGPTAPSRESPQYSP
R (in isoform B and isoform G).
{ECO:0000305}.
/FTId=VSP_001011.
SEQUENCE 852 AA; 93949 MW; 82A5FE462A5F259A CRC64;
MVQKSRNGGV YPGTSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR GSVLSKPRTG
GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK
SSEGALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASI
AVLAAGSQGN VFATSALRSL RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF
LCLILASFLV YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI
GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QSAWRFYATN LSRTDLHSTW
QYYERTVTVP MISSQTQTYG ASRLIPPLNQ LEMLRNLKSK SGLTFRKEPQ PEPSPSQKVS
LKDRVFSSPR GVAAKGKGSP QAQTVRRSPS ADQSLDDSPS KVPKSWSFGD RSRARQAFRI
KGAASRQNSE EASLPGEDIV EDNKSCNCEF VTEDLTPGLK VSIRAVCVMR FLVSKRKFKE
SLRPYDVMDV IEQYSAGHLD MLSRIKSLQS RVDQIVGRGP TITDKDRTKG PAETELPEDP
SMMGRLGKVE KQVLSMEKKL DFLVSIYTQR MGIPPAETEA YFGAKEPEPA PPYHSPEDSR
DHADKHGCII KIVRSTSSTG QRKYAAPPVM PPAECPPSTS WQQSHQRHGT SPVGDHGSLV
RIPPPPAHER SLSAYSGGNR ASTEFLRLEG TPACRPSEAA LRDSDTSISI PSVDHEELER
SFSGFSISQS KENLNALASC YAAVAPCAKV RPYIAEGESD TDSDLCTPCG PPPRSATGEG
PFGDVAWAGP RK


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