ID SL9A1_MOUSE Reviewed; 820 AA. AC Q61165; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 191. DE RecName: Full=Sodium/hydrogen exchanger 1; DE AltName: Full=Na(+)/H(+) exchanger 1; DE Short=NHE-1; DE AltName: Full=Solute carrier family 9 member 1; GN Name=Slc9a1; Synonyms=Nhe1; 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; RX PubMed=11931388; DOI=10.1023/a:1017984311138; RA Dewey M.J., Ennis T.M., Bowman L.H.; RT "cDNA cloning and expression of the mouse Na/H antiporter (NHE-1) and a RT potential splice variant."; RL Mol. Biol. Rep. 28:111-117(2001). RN [2] RP TISSUE SPECIFICITY, AND VARIANT SWE 442-LYS--GLN-820 DEL. RX PubMed=9335342; DOI=10.1016/s0092-8674(01)80016-7; RA Cox G.A., Lutz C.M., Yang C.L., Biemesderfer D., Bronson R.T., Fu A., RA Aronson P.S., Noebels J.L., Frankel W.N.; RT "Sodium/hydrogen exchanger gene defect in slow-wave epilepsy mutant mice."; RL Cell 91:139-148(1997). RN [3] RP DISRUPTION PHENOTYPE. RX PubMed=10199808; DOI=10.1152/ajpcell.1999.276.4.c788; RA Bell S.M., Schreiner C.M., Schultheis P.J., Miller M.L., Evans R.L., RA Vorhees C.V., Shull G.E., Scott W.J.; RT "Targeted disruption of the murine Nhe1 locus induces ataxia, growth RT retardation, and seizures."; RL Am. J. Physiol. 276:C788-C795(1999). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain cortex; RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200; RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., RA Panse C., Schlapbach R., Mansuy I.M.; RT "Qualitative and quantitative analyses of protein phosphorylation in naive RT and stimulated mouse synaptosomal preparations."; RL Mol. Cell. Proteomics 6:283-293(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-609 AND SER-707, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=19369449; DOI=10.1152/ajpcell.00062.2009; RA Damkier H.H., Prasad V., Huebner C.A., Praetorius J.; RT "Nhe1 is a luminal Na+/H+ exchanger in mouse choroid plexus and is targeted RT to the basolateral membrane in Ncbe/Nbcn2-null mice."; RL Am. J. Physiol. 296:C1291-C1300(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697 AND SER-707, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200; RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; RT "Large scale localization of protein phosphorylation by use of electron RT capture dissociation mass spectrometry."; RL Mol. Cell. Proteomics 8:904-912(2009). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-606; THR-607; RP SER-609; SER-697; SER-701; SER-707; SER-727; SER-730; SER-733; THR-755; RP SER-790 AND SER-792, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; 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: Electroneutral Na(+) /H(+) antiporter that extrudes Na(+) in CC exchange for external protons driven by the inward sodium ion chemical CC gradient, protecting cells from acidification that occurs from CC metabolism (By similarity). Exchanges intracellular H(+) ions for CC extracellular Na(+) in 1:1 stoichiometry (By similarity). Plays a key CC role in maintening intracellular pH neutral and cell volume, and thus CC is important for cell growth, proliferation, migration and survival. In CC addition, can transport lithium Li(+) and functions also as a CC Na(+)/Li(+) antiporter. SLC9A1 also functions in membrane anchoring and CC organization of scaffolding complexes that coordinate signaling inputs CC (By similarity). {ECO:0000250|UniProtKB:P19634, CC ECO:0000250|UniProtKB:P26431}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(out) + Na(+)(in) = H(+)(in) + Na(+)(out); CC Xref=Rhea:RHEA:29419, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101; CC Evidence={ECO:0000250|UniProtKB:P19634}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H(+)(in) + Li(+)(out) = H(+)(out) + Li(+)(in); CC Xref=Rhea:RHEA:72407, ChEBI:CHEBI:15378, ChEBI:CHEBI:49713; CC Evidence={ECO:0000250|UniProtKB:P19634}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Li(+)(in) + Na(+)(out) = Li(+)(out) + Na(+)(in); CC Xref=Rhea:RHEA:72415, ChEBI:CHEBI:29101, ChEBI:CHEBI:49713; CC Evidence={ECO:0000250|UniProtKB:P19634}; CC -!- ACTIVITY REGULATION: Activated at acidic pHs. Inhibited by cariporide CC and eniporide. Inhibited by amiloride and 5-amino-substituted CC derivatives. Phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) and CC phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) bind and CC differentially regulate SLC9A1 activity. CC {ECO:0000250|UniProtKB:P19634}. CC -!- SUBUNIT: Homodimer; dimerization is crucial for its function (By CC similarity). Oligomer (By similarity). Interacts with CALM1 in a CC calcium-dependent manner (By similarity). Interacts with TESC (By CC similarity). Interacts (via the juxtamembrane region of the cytoplasmic CC C-terminal domain) with CHP1; the interaction occurs at the plasma CC membrane in a calcium-dependent manner (By similarity). Interacts with CC CHP2; the interaction occurs in a calcium-dependent manner (By CC similarity). Interacts with EZR; regulates the cytoskeletal CC interactions of SLC9A1 and promotes stress fiber formation (By CC similarity). {ECO:0000250|UniProtKB:P19634, CC ECO:0000250|UniProtKB:P26431}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19634}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P19634}. Basolateral CC cell membrane {ECO:0000250|UniProtKB:P48762}; Multi-pass membrane CC protein {ECO:0000250|UniProtKB:P19634}. Note=Localized basolaterally in CC every epithelial cell, except in the choroid plexus where SLC9A1 is CC expressed luminally. {ECO:0000269|PubMed:19369449}. CC -!- TISSUE SPECIFICITY: Expressed in kidney, brain and stomach. CC {ECO:0000269|PubMed:9335342}. CC -!- PTM: O-glycosylated. {ECO:0000250|UniProtKB:P19634}. CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome. CC Ubiquitination is reduced by CHP1. {ECO:0000250|UniProtKB:P26431}. CC -!- PTM: Palmitoylated; may play a major role in SLC9A1 regulation. CC {ECO:0000250|UniProtKB:P26431}. CC -!- PTM: Phosphorylation at Thr-784 increases SLC9A1 activity. Specifically CC dephosphorylated at Thr-784 by PPP3CA that negatively regulates SLC9A1 CC activity. Phosphorylation at Ser-652 by AKT1 reduces SLC9A1 binding to CC CALM1. {ECO:0000250|UniProtKB:P19634}. CC -!- DISEASE: Note=Defects in Slc9a1 is the cause of slow-wave epilepsy CC (swe) phenotype (PubMed:9335342). Mutant mice display slow-wave CC epilepsy, with a neurological syndrome including ataxia and a unique CC epilepsy phenotype consisting of 3/sec absence and tonic-clonic CC seizures. Mutants show selective neuronal death in the cerebellum and CC brainstem. Mice display also several other significant abnormalities in CC growth and development, and less than half of the mutant homozygous CC animals survived to weaning. Most died by 35-40 days (PubMed:9335342). CC {ECO:0000269|PubMed:9335342}. CC -!- DISRUPTION PHENOTYPE: Deficient mice exhibit a decreased rate of CC postnatal growth that is first evident at 2 week of age. At this time, CC deficient animals also begin to exhibit ataxia and epileptic-like CC seizures. Approximately 67% of the mutants die before weaning. CC {ECO:0000269|PubMed:10199808}. CC -!- MISCELLANEOUS: Predicted models used for more than 20 years predicted CC 10-12 transmembrane segments. Recently, the stucture of SLC9A1 has been CC solved and reveals that SLC9A1 posseses 13 transmembranes. CC {ECO:0000250|UniProtKB:P19634}. CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 (CPA1) CC transporter (TC 2.A.36) family. {ECO:0000305}. CC -!- CAUTION: The interacting region with TESC is conflicting: In human, it CC has been reported that SLC9A1 interacts with TESC via the juxtamembrane CC region of the cytoplasmic C-terminal domain, including residues 507- CC 549. However, another publication has reported interaction with TESC CC via residues 637-820, the region of the cytoplasmic C-terminus more CC distal to the membrane. {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; U51112; AAA92976.1; -; mRNA. DR CCDS; CCDS38903.1; -. DR RefSeq; NP_058677.1; NM_016981.2. DR AlphaFoldDB; Q61165; -. DR BMRB; Q61165; -. DR SMR; Q61165; -. DR BioGRID; 203321; 14. DR IntAct; Q61165; 1. DR STRING; 10090.ENSMUSP00000030669; -. DR GlyConnect; 2723; 1 N-Linked glycan (1 site). DR GlyCosmos; Q61165; 2 sites, 1 glycan. DR GlyGen; Q61165; 2 sites, 1 N-linked glycan (1 site). DR iPTMnet; Q61165; -. DR PhosphoSitePlus; Q61165; -. DR SwissPalm; Q61165; -. DR jPOST; Q61165; -. DR MaxQB; Q61165; -. DR PaxDb; 10090-ENSMUSP00000030669; -. DR ProteomicsDB; 261375; -. DR Pumba; Q61165; -. DR Antibodypedia; 30723; 311 antibodies from 37 providers. DR DNASU; 20544; -. DR Ensembl; ENSMUST00000030669.8; ENSMUSP00000030669.8; ENSMUSG00000028854.10. DR GeneID; 20544; -. DR KEGG; mmu:20544; -. DR UCSC; uc008vcs.1; mouse. DR AGR; MGI:102462; -. DR CTD; 6548; -. DR MGI; MGI:102462; Slc9a1. DR VEuPathDB; HostDB:ENSMUSG00000028854; -. DR eggNOG; KOG1966; Eukaryota. DR GeneTree; ENSGT00940000156338; -. DR HOGENOM; CLU_005912_4_1_1; -. DR InParanoid; Q61165; -. DR OMA; MMRTKEP; -. DR OrthoDB; 1065060at2759; -. DR PhylomeDB; Q61165; -. DR TreeFam; TF317212; -. DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation. DR Reactome; R-MMU-425986; Sodium/Proton exchangers. DR BioGRID-ORCS; 20544; 2 hits in 78 CRISPR screens. DR ChiTaRS; Slc9a1; mouse. DR PRO; PR:Q61165; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q61165; Protein. DR Bgee; ENSMUSG00000028854; Expressed in epithelium of stomach and 239 other cell types or tissues. DR ExpressionAtlas; Q61165; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0090533; C:cation-transporting ATPase complex; ISO:MGI. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0014704; C:intercalated disc; ISO:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0045121; C:membrane raft; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IEA:GOC. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0042383; C:sarcolemma; ISO:MGI. DR GO; GO:0030315; C:T-tubule; ISO:MGI. DR GO; GO:1990351; C:transporter complex; IDA:MGI. DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0043167; F:ion binding; ISO:MGI. DR GO; GO:0005543; F:phospholipid binding; ISO:MGI. DR GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central. DR GO; GO:0030346; F:protein phosphatase 2B binding; ISO:MGI. DR GO; GO:0015385; F:sodium:proton antiporter activity; IDA:MGI. DR GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI. DR GO; GO:0071468; P:cellular response to acidic pH; ISS:UniProtKB. DR GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl. DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl. DR GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl. DR GO; GO:0071872; P:cellular response to epinephrine stimulus; ISO:MGI. DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0030214; P:hyaluronan catabolic process; ISO:MGI. DR GO; GO:0006883; P:intracellular sodium ion homeostasis; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:0045760; P:positive regulation of action potential; ISO:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; ISO:MGI. DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI. DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI. DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; ISO:MGI. DR GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; ISO:MGI. DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISO:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI. DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central. DR GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; ISO:MGI. DR GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:MGI. DR GO; GO:0051453; P:regulation of intracellular pH; ISO:MGI. DR GO; GO:0006885; P:regulation of pH; IDA:MGI. DR GO; GO:0002026; P:regulation of the force of heart contraction; ISO:MGI. DR GO; GO:0086092; P:regulation of the force of heart contraction by cardiac conduction; ISO:MGI. DR GO; GO:0010447; P:response to acidic pH; IMP:MGI. DR GO; GO:0035994; P:response to muscle stretch; ISO:MGI. DR GO; GO:0014070; P:response to organic cyclic compound; ISO:MGI. DR GO; GO:0036376; P:sodium ion export across plasma membrane; ISS:UniProtKB. DR GO; GO:0098719; P:sodium ion import across plasma membrane; ISO:MGI. DR GO; GO:0006814; P:sodium ion transport; IDA:MGI. DR GO; GO:0048863; P:stem cell differentiation; IMP:MGI. DR Gene3D; 6.10.140.1330; -; 1. DR Gene3D; 6.10.250.1040; -; 1. DR Gene3D; 6.10.250.2020; -; 1. DR InterPro; IPR006153; Cation/H_exchanger. DR InterPro; IPR018422; Cation/H_exchanger_CPA1. DR InterPro; IPR004709; NaH_exchanger. DR InterPro; IPR001970; NHE-1-like. DR InterPro; IPR032103; NHE_CaM-bd. DR NCBIfam; TIGR00840; b_cpa1; 1. DR PANTHER; PTHR10110; SODIUM/HYDROGEN EXCHANGER; 1. DR PANTHER; PTHR10110:SF59; SODIUM_HYDROGEN EXCHANGER 1; 1. DR Pfam; PF00999; Na_H_Exchanger; 1. DR Pfam; PF16644; NEXCaM_BD; 1. DR PRINTS; PR01084; NAHEXCHNGR. DR PRINTS; PR01085; NAHEXCHNGR1. DR Genevisible; Q61165; MM. PE 1: Evidence at protein level; KW Antiport; Calmodulin-binding; Cell membrane; Glycoprotein; Ion transport; KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome; KW Sodium; Sodium transport; Transmembrane; Transmembrane helix; Transport; KW Ubl conjugation. FT CHAIN 1..820 FT /note="Sodium/hydrogen exchanger 1" FT /id="PRO_0000052348" FT TOPO_DOM 1..102 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 103..125 FT /note="Helical; Name=1" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 126..134 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 135..152 FT /note="Helical; Name=2" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 153..162 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 163..180 FT /note="Helical; Name=3" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 181..190 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 191..219 FT /note="Helical; Name=4" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 220..226 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 227..253 FT /note="Helical; Name=5" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 254..256 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 257..287 FT /note="Helical; Name=6" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 288..291 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 292..326 FT /note="Helical; Name=7" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 327..332 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 333..345 FT /note="Helical; Name=8" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 346..354 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 355..375 FT /note="Helical; Name=9" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 376..377 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 378..408 FT /note="Helical; Name=10" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 409..414 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 415..442 FT /note="Helical; Name=11" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 443..448 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 449..473 FT /note="Helical; Name=12" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 474..479 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 480..509 FT /note="Helical; Name=13" FT /evidence="ECO:0000250|UniProtKB:P19634" FT TOPO_DOM 510..820 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 40..74 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 507..549 FT /note="Interaction with TESC" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 513..520 FT /note="PI(4,5)P2-binding region" FT /evidence="ECO:0000250|UniProtKB:P26431" FT REGION 519..549 FT /note="Interaction with CHP2" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 544..549 FT /note="Confers pH-dependent PI(4,5)P2 binding" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 556..564 FT /note="PI(4,5)P2-binding region" FT /evidence="ECO:0000250|UniProtKB:P26431" FT REGION 637..820 FT /note="Interaction with CALM1" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 637..820 FT /note="Interaction with TESC" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 688..691 FT /note="Interaction with PPP3CA" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 719..724 FT /note="Interaction with PPP3CA" FT /evidence="ECO:0000250|UniProtKB:P19634" FT REGION 748..820 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 777..799 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 165 FT /note="Channel pore-lining" FT /evidence="ECO:0000250" FT MOD_RES 603 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 606 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 607 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 609 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 652 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P19634" FT MOD_RES 697 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19131326, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 701 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 707 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079" FT MOD_RES 727 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 730 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 733 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 755 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 784 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P19634" FT MOD_RES 790 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 792 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 801 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26431" FT VARIANT 442..820 FT /note="Missing (in swe)" FT /evidence="ECO:0000269|PubMed:9335342" SQ SEQUENCE 820 AA; 91468 MW; 0589C4D08DD348BE CRC64; MMLRWSGVWG FHPPRIFPSL LVVVALVGLL PVLRSHGLQH SPTASTIRGS EPPRERSIGD VTTAPSEPLH RPDDHNLTNL IIEHGGKPSR KAFPVLDIDY PHVRTPFEIS LWILLACLMK IGFHVIPTIS SIVPESCLLI VVGLLVGGLI KGVGETPPFL QSDVFFLFLL PPIILDAGYF LPLRQFTENL GTILIFAVVG TLWNAFFLGG LLYAVCLVGG EQINNIGLLD TLLFGSIISA VDPVAVLAVF EEIHINELLH ILVFGESLLN DAVTVVLYHL FEEFASYDSV GISDIFLGFL SFFVVALGGV FVGVVYGVIA AFTSRFTSHI RVIEPLFVFL YSYMAYLSAE LFHLSGIMAL IASGVVMRPY VEANISHKSH TTIKYFLKMW SSVSETLIFI FLGVSTVAGS HQWNWTFVIS TLLFCLIARV LGVLVLTWFI NKFRIVKLTP KDQFIIAYGG LRGAIAFSLG YLLDKKHFPM CDLFLTAIIT VIFFTVFVQG MTIRPLVDLL AVKKKQETKR SINEEIHTQF LDHLLTGIED ICGHYGHHHW KDKLNRFNKK YVKKCLIAGE RSKEPQLIAF YHKMEMKQAI ELVESGGMGK IPSAVSTVSM QNIHPKAVTS DRILPALSKD KEEEIRKILR SNLQKTRQRL RSYNRHTLVA DPYEEAWNQM LLRRQKARQL EQKITNYLTV PAHKLDSPTL SRARIGSDPL AYEPKADLPV ITIDPASPQS PESVDLVNEE LKGKVLGLNR GPRVTPEEEE EDEDGIIMIR SKEPSSPGTD DVFTPGSSDS PSSQRIQRCL SDPGPHPEPG EGEPFIPKGQ //