KCNQ1_RAT
ID KCNQ1_RAT Reviewed; 669 AA.
AC Q9Z0N7; O08655;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Potassium voltage-gated channel subfamily KQT member 1 {ECO:0000305};
DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit alpha KvLQT1 {ECO:0000305|PubMed:11220365};
DE AltName: Full=KQT-like 1 {ECO:0000250|UniProtKB:P51787};
DE AltName: Full=Voltage-gated potassium channel subunit Kv7.1 {ECO:0000250|UniProtKB:P51787};
GN Name=Kcnq1 {ECO:0000312|RGD:621503};
GN Synonyms=Kcna9 {ECO:0000250|UniProtKB:P51787},
GN Kvlqt1 {ECO:0000303|PubMed:11220365};
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], AND FUNCTION.
RC TISSUE=Colon;
RX PubMed=11220365; DOI=10.1007/s002320010045;
RA Kunzelmann K., Huebner M., Schreiber R., Levy-Holzman R., Garty H.,
RA Bleich M., Warth R., Slavik M., von Hahn T., Greger R.;
RT "Cloning and function of the rat colonic epithelial K+ channel KVLQT1.";
RL J. Membr. Biol. 179:155-164(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-352.
RC STRAIN=Sprague-Dawley;
RX PubMed=9314834; DOI=10.1161/01.res.81.4.533;
RA Takimoto K., Li D., Hershman K.M., Li P., Jackson E.K., Levitan E.S.;
RT "Decreased expression of Kv4.2 and novel Kv4.3 K+ channel subunit mRNAs in
RT ventricles of renovascular hypertensive rats.";
RL Circ. Res. 81:533-539(1997).
RN [3]
RP INTERACTION WITH KCNE3, AND FUNCTION.
RX PubMed=21911611; DOI=10.1113/jphysiol.2011.215772;
RA Alzamora R., O'Mahony F., Bustos V., Rapetti-Mauss R., Urbach V., Cid L.P.,
RA Sepulveda F.V., Harvey B.J.;
RT "Sexual dimorphism and oestrogen regulation of KCNE3 expression modulates
RT the functional properties of KCNQ1 K[+] channels.";
RL J. Physiol. (Lond.) 589:5091-5107(2011).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=23529131; DOI=10.1113/jphysiol.2013.251678;
RA Rapetti-Mauss R., O'Mahony F., Sepulveda F.V., Urbach V., Harvey B.J.;
RT "Oestrogen promotes KCNQ1 potassium channel endocytosis and postendocytic
RT trafficking in colonic epithelium.";
RL J. Physiol. (Lond.) 591:2813-2831(2013).
CC -!- FUNCTION: Potassium channel that plays an important role in a number of
CC tissues, including heart, inner ear, stomach and colon (By similarity).
CC Associates with KCNE beta subunits that modulates current kinetics (By
CC similarity) (PubMed:21911611). Induces a voltage-dependent by rapidly
CC activating and slowly deactivating potassium-selective outward current
CC (By similarity) (PubMed:11220365). Promotes also a delayed voltage
CC activated potassium current showing outward rectification
CC characteristic (PubMed:11220365). During beta-adrenergic receptor
CC stimulation participates in cardiac repolarization by associating with
CC KCNE1 to form the I(Ks) cardiac potassium current that increases the
CC amplitude and slows down the activation kinetics of outward potassium
CC current I(Ks) (By similarity) (PubMed:11220365). Muscarinic agonist
CC oxotremorine-M strongly suppresses KCNQ1/KCNE1 current (By similarity).
CC When associated with KCNE3, forms the potassium channel that is
CC important for cyclic AMP-stimulated intestinal secretion of chloride
CC ions (By similarity). This interaction with KCNE3 is reduced by 17beta-
CC estradiol, resulting in the reduction of currents (PubMed:21911611).
CC During conditions of increased substrate load, maintains the driving
CC force for proximal tubular and intestinal sodium ions absorption,
CC gastric acid secretion, and cAMP-induced jejunal chloride ions
CC secretion (By similarity). Allows the provision of potassium ions to
CC the luminal membrane of the secretory canaliculus in the resting state
CC as well as during stimulated acid secretion (By similarity). When
CC associated with KCNE2, forms a heterooligomer complex leading to
CC currents with an apparently instantaneous activation, a rapid
CC deactivation process and a linear current-voltage relationship and
CC decreases the amplitude of the outward current (By similarity). When
CC associated with KCNE4, inhibits voltage-gated potassium channel
CC activity (By similarity). When associated with KCNE5, this complex only
CC conducts current upon strong and continued depolarization (By
CC similarity). Also forms a heterotetramer with KCNQ5 that has a voltage-
CC gated potassium channel activity (By similarity). Binds with
CC phosphatidylinositol 4,5-bisphosphate (By similarity).
CC {ECO:0000250|UniProtKB:P51787, ECO:0000250|UniProtKB:P97414,
CC ECO:0000269|PubMed:11220365, ECO:0000269|PubMed:21911611}.
CC -!- SUBUNIT: Tetramer. Heterotetramer with KCNE1; targets to the membrane
CC raft. Interacts (via C-terminus) with CALM; forms a heterooctameric
CC structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent
CC manner. Interacts with AKAP9; targets protein kinase A (PKA) catalytic
CC and regulatory subunits and protein phosphatase 1 (PP1) to the KCNQ1-
CC KCNE1 complex, allowing PKA-mediated phosphorylation and increase of
CC delayed rectifier potassium channel activity. Interacts with KCNE2;
CC form a heterooligomer complex that targets to the membrane raft and
CC leading to currents with an apparently instantaneous activation, a
CC rapid deactivation process and a linear current-voltage relationship
CC and decreases the amplitude of the outward current. Interacts with
CC AP2M1; mediates estrogen-induced internalization via clathrin-coated
CC vesicles. Interacts with NEDD4L; promotes internalization and decreases
CC I(Ks) currents. Interacts with USP2; counteracts the NEDD4L-specific
CC down-regulation of I(Ks) and restore plasma membrane localization.
CC Heterotetramer with KCNQ5; has a voltage-gated potassium channel
CC activity (By similarity). Interacts with KCNE3; produces a current with
CC nearly instantaneous activation with a linear current-voltage
CC relationship and alters membrane raft localization (By similarity)
CC (PubMed:21911611). Interacts with KCNE4; impairs KCNQ1 localization in
CC lipid rafts and inhibits voltage-gated potassium channel activity.
CC Interacts with KCNE5; impairs KCNQ1 localization in lipid rafts and
CC only conducts current upon strong and continued depolarization (By
CC similarity). {ECO:0000250|UniProtKB:P51787,
CC ECO:0000269|PubMed:21911611}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P51787};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P51787}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P51787}. Early endosome
CC {ECO:0000269|PubMed:23529131}. Membrane raft
CC {ECO:0000250|UniProtKB:P51787}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P51787}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P51787}. Note=Colocalized with KCNE3 at the
CC plasma membrane. Upon 17beta-oestradiol treatment, colocalizes with
CC RAB5A at early endosome. Heterotetramer with KCNQ5 is highly retained
CC at the endoplasmic reticulum and is localized outside of lipid raft
CC microdomains. During the early stages of epithelial cell polarization
CC induced by the calcium switch it removed from plasma membrane to the
CC endoplasmic reticulum where it retained and it is redistributed to the
CC basolateral cell surface in a PI3K-dependent manner at a later stage.
CC {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The coiled-coil domain mediates tetramerization.
CC {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The segment S6 is involved in the inhibition of voltage-gated
CC potassium channel activity by KCNE4. {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The C-terminal assembly domain promotes self-interactiona;
CC allows functional channel. {ECO:0000250|UniProtKB:P51787}.
CC -!- DOMAIN: The C-terminal coiled-coil domain interacts with a single CALM
CC molecule via the first two membrane-proximal helical regions, with CALM
CC forming a clamp-like structure. Binding of CALM C-terminus to the first
CC helical region is calcium-independent but is essential for assembly of
CC the structure. Binding of CALM N-terminus to the second helical region
CC is calcium-dependent and regulates electrophysiological activity of the
CC channel. {ECO:0000250|UniProtKB:P51787}.
CC -!- PTM: Phosphorylation at Ser-27 by PKA; increases delayed rectifier
CC potassium channel activity of the KCNQ1-KCNE1 complex through a
CC macromolecular complex that includes PKA, PP1, and the targeting
CC protein AKAP9. {ECO:0000250|UniProtKB:P51787}.
CC -!- PTM: Ubiquitinated by NEDD4L; promotes internalization. The
CC ubiquitinylated form is internalized through a clathrin-mediated
CC endocytosis by interacting with AP2M1 and is recycled back to the cell
CC membrane via RAB4A and RAB11A. {ECO:0000250|UniProtKB:P51787}.
CC -!- PTM: Deubiquitinated by USP2; counteracts the NEDD4L-specific down-
CC regulation of I(Ks) and restores the membrane localization.
CC {ECO:0000250|UniProtKB:P51787}.
CC -!- SIMILARITY: Belongs to the potassium channel family. KQT (TC 1.A.1.15)
CC subfamily. Kv7.1/KCNQ1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51395.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ133685; CAB38863.1; -; mRNA.
DR EMBL; U92655; AAB51395.1; ALT_FRAME; mRNA.
DR RefSeq; NP_114462.1; NM_032073.1.
DR AlphaFoldDB; Q9Z0N7; -.
DR BMRB; Q9Z0N7; -.
DR SMR; Q9Z0N7; -.
DR BioGRID; 249886; 1.
DR STRING; 10116.ENSRNOP00000027875; -.
DR GlyGen; Q9Z0N7; 1 site.
DR PaxDb; Q9Z0N7; -.
DR PRIDE; Q9Z0N7; -.
DR GeneID; 84020; -.
DR KEGG; rno:84020; -.
DR UCSC; RGD:621503; rat.
DR CTD; 3784; -.
DR RGD; 621503; Kcnq1.
DR eggNOG; KOG1419; Eukaryota.
DR InParanoid; Q9Z0N7; -.
DR OrthoDB; 1168835at2759; -.
DR PhylomeDB; Q9Z0N7; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR Reactome; R-RNO-5576890; Phase 3 - rapid repolarisation.
DR Reactome; R-RNO-5576893; Phase 2 - plateau phase.
DR PRO; PR:Q9Z0N7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:1990794; C:basolateral part of cell; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0097546; C:ciliary base; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0034702; C:ion channel complex; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0034705; C:potassium channel complex; ISO:RGD.
DR GO; GO:0042383; C:sarcolemma; IDA:RGD.
DR GO; GO:0030133; C:transport vesicle; ISO:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:RGD.
DR GO; GO:0042589; C:zymogen granule membrane; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISO:RGD.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005267; F:potassium channel activity; IDA:RGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; ISO:RGD.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:0086089; F:voltage-gated potassium channel activity involved in atrial cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0071875; P:adrenergic receptor signaling pathway; ISO:RGD.
DR GO; GO:0086014; P:atrial cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0060117; P:auditory receptor cell development; ISO:RGD.
DR GO; GO:0061337; P:cardiac conduction; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0030644; P:cellular chloride ion homeostasis; ISO:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:RGD.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0055064; P:chloride ion homeostasis; ISO:RGD.
DR GO; GO:0072359; P:circulatory system development; ISO:RGD.
DR GO; GO:0090102; P:cochlea development; ISO:RGD.
DR GO; GO:0035934; P:corticosterone secretion; ISO:RGD.
DR GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; ISO:RGD.
DR GO; GO:0030218; P:erythrocyte differentiation; ISO:RGD.
DR GO; GO:0001696; P:gastric acid secretion; ISO:RGD.
DR GO; GO:0001698; P:gastrin-induced gastric acid secretion; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0006006; P:glucose metabolic process; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISS:UniProtKB.
DR GO; GO:0042472; P:inner ear morphogenesis; ISO:RGD.
DR GO; GO:0050892; P:intestinal absorption; IMP:UniProtKB.
DR GO; GO:0015705; P:iodide transport; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0086009; P:membrane repolarization; ISS:UniProtKB.
DR GO; GO:0086011; P:membrane repolarization during action potential; ISO:RGD.
DR GO; GO:0098914; P:membrane repolarization during atrial cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IDA:RGD.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR GO; GO:0060452; P:positive regulation of cardiac muscle contraction; ISO:RGD.
DR GO; GO:0060454; P:positive regulation of gastric acid secretion; IMP:RGD.
DR GO; GO:0010460; P:positive regulation of heart rate; ISO:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:RGD.
DR GO; GO:0055075; P:potassium ion homeostasis; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0060453; P:regulation of gastric acid secretion; ISS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:RGD.
DR GO; GO:0060306; P:regulation of membrane repolarization; ISO:RGD.
DR GO; GO:0032409; P:regulation of transporter activity; ISO:RGD.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; ISO:RGD.
DR GO; GO:0070293; P:renal absorption; ISS:UniProtKB.
DR GO; GO:0070294; P:renal sodium ion absorption; ISO:RGD.
DR GO; GO:0072347; P:response to anesthetic; IDA:RGD.
DR GO; GO:0071871; P:response to epinephrine; ISO:RGD.
DR GO; GO:0032868; P:response to insulin; ISO:RGD.
DR GO; GO:0035094; P:response to nicotine; ISO:RGD.
DR GO; GO:0007622; P:rhythmic behavior; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; ISO:RGD.
DR GO; GO:0035176; P:social behavior; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR GO; GO:0062094; P:stomach development; ISO:RGD.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:RGD.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR InterPro; IPR005827; K_chnl_volt-dep_KCQN1.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR PANTHER; PTHR11537:SF266; PTHR11537:SF266; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03520; KCNQ_channel; 1.
DR PRINTS; PR01460; KCNQ1CHANNEL.
DR PRINTS; PR01459; KCNQCHANNEL.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Endoplasmic reticulum; Endosome; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..669
FT /note="Potassium voltage-gated channel subfamily KQT member
FT 1"
FT /id="PRO_0000054027"
FT TOPO_DOM 1..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..147
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..225
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..248
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 300..320
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 321..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 370..382
FT /note="Interaction with CALM"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 515..529
FT /note="Interaction with CALM; calcium-dependent"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 535..572
FT /note="Interaction with KCNE1 C-terminus"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 588..616
FT /note="Interaction with AKAP9"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT REGION 589..620
FT /note="C-terminal assembly domain"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT COILED 585..621
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT MOTIF 312..317
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT MOD_RES 27
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P51787"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97414"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97414"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 170
FT /note="E -> K (in Ref. 2; AAB51395)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="S -> T (in Ref. 2; AAB51395)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="V -> L (in Ref. 2; AAB51395)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="V -> F (in Ref. 2; AAB51395)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 74579 MW; 2374CA1290020939 CRC64;
MDTASSPPNA ERKRAGWGRL LGARRGSAGL AKKCPFSLEL AEGGPTGGTV YAPIAPTGAP
GLAPPMSPPV SPVPAPADLG PRPRVSLDPR VSIYSTRRPL LARTHIQGRV YNFLERPTGW
KCFVYHFTVF LIVLVCLIFS VLSTIEQYAA LATGTLFWME IVLVVFFGTE YVVRLWSAGC
RSKYVGIWGR LRFARKPISI IDLIVVVASM VVLCVGSKGQ VFATSAIRGI RFLQILRMLH
VDRQGGTWRL LGSVVFIHRQ ELITTLYIGF LGLIFSSYFV YLAEKDAVNE SGRIEFGSYA
DALWWGVVTV TTIGYGDKVP QTWVGKTIAS CFSVFAISFF ALPAGILGSG FALKVQQKQR
QKHFNRQIPA AASLIQTAWR CYAAENPDSS TWKIYVRKPA RSHTLLSPSP KPKKSVMVKK
KKFKLDKDNG LSPGEKIFNV PHITCDPPED RRPDHFSIDG YDSSVRKSPT LLEVSTPHFL
RTNSFAEDLD LEGETLLTPI THVSQLRDHH RATIKVIRRM QYFVAKKKFQ QARKPYDVRD
VIEQYSQGHL NLMVRIKELQ RRLDQSIGKP SLFIPISEKS KDRGSNTIGA RLNRVEDKVT
QLDQRLVIIT DMLHQLLSLQ QGGPTCNNRS QVVASDERGS INPELFLPSN SLPTYEQLTV
PQTGPDEGS
