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 27-MAR-2024, entry version 159. 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}, Kvlqt1 GN {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). KCNQ1-KCNE2 CC channel associates with Na(+)-coupled myo-inositol symporter in the CC apical membrane of choroid plexus epithelium and regulates the myo- CC inositol gradient between blood and cerebrospinal fluid with an impact CC on neuron excitability. {ECO:0000250|UniProtKB:P51787, CC ECO:0000250|UniProtKB:P97414, ECO:0000269|PubMed:11220365, CC 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). Interacts with SLC5A3; forms coregulatory channel- CC transporter complexes that modulate Na(+)-coupled myo-inositol influx CC through the transporter. {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}. Apical cell membrane CC {ECO:0000250|UniProtKB:P97414}; Multi-pass membrane protein CC {ECO:0000255}. Note=Colocalized with KCNE3 at the plasma membrane. Upon CC 17beta-oestradiol treatment, colocalizes with RAB5A at early endosome. CC Heterotetramer with KCNQ5 is highly retained at the endoplasmic CC reticulum and is localized outside of lipid raft microdomains. During CC the early stages of epithelial cell polarization induced by the calcium CC switch it is removed from the plasma membrane to the endoplasmic CC reticulum, where it is retained, and redistributed to the basolateral CC cell surface in a PI3K-dependent manner at a later stage. Colocalizes CC with SLC5A3 at the apical membrane of choroid plexus epithelium (By CC similarity). {ECO:0000250|UniProtKB:P51787, CC ECO:0000250|UniProtKB:P97414}. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyCosmos; Q9Z0N7; 1 site, No reported glycans. DR GlyGen; Q9Z0N7; 1 site. DR PhosphoSitePlus; Q9Z0N7; -. DR PaxDb; 10116-ENSRNOP00000027875; -. DR GeneID; 84020; -. DR KEGG; rno:84020; -. DR UCSC; RGD:621503; rat. DR AGR; RGD:621503; -. DR CTD; 3784; -. DR RGD; 621503; Kcnq1. DR eggNOG; KOG1419; Eukaryota. DR InParanoid; Q9Z0N7; -. DR OrthoDB; 2911641at2759; -. 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:0097546; C:ciliary base; ISO:RGD. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005769; C:early endosome; ISO:RGD. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD. DR GO; GO:0005770; C:late endosome; ISO:RGD. DR GO; GO:0098576; C:lumenal side of membrane; ISO:RGD. DR GO; GO:0005764; C:lysosome; ISO:RGD. DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB. DR GO; GO:0034702; C:monoatomic ion channel complex; ISO:RGD. 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: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: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:0022600; P:digestive system process; 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: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:0030644; P:intracellular chloride ion homeostasis; ISO:RGD. 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:0046676; P:negative regulation of insulin secretion; IDA: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: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: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:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; 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:0032868; P:response to insulin; 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; 1.10.287.70; -; 1. DR Gene3D; 6.10.140.1910; -; 2. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR47735:SF6; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 1; 1. DR PANTHER; PTHR47735; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF03520; KCNQ_channel; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01460; KCNQ1CHANNEL. DR PRINTS; PR01459; KCNQCHANNEL. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. 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 //