ID AT1A1_HUMAN Reviewed; 1023 AA. AC P05023; B2RBR6; B7Z2T5; B7Z3U6; F5H3A1; Q16689; Q6LDM4; Q9UCN1; Q9UJ20; AC Q9UJ21; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 02-SEP-2026, entry version 266. DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1; DE Short=Na(+)/K(+) ATPase alpha-1 subunit; DE EC=7.2.2.13 {ECO:0000269|PubMed:35803952}; DE AltName: Full=Sodium pump subunit alpha-1; GN Name=ATP1A1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2430951; DOI=10.1093/oxfordjournals.jbchem.a121726; RA Kawakami K., Ohta T., Nojima H., Nagano K.; RT "Primary structure of the alpha-subunit of human Na,K-ATPase deduced from RT cDNA sequence."; RL J. Biochem. 100:389-397(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Retinal pigment epithelium; RX PubMed=7536695; DOI=10.1016/0378-1119(94)00812-7; RA Ruiz A., Bhat S.P., Bok D.; RT "Characterization and quantification of full-length and truncated Na,K- RT ATPase alpha 1 and beta 1 RNA transcripts expressed in human retinal RT pigment epithelium."; RL Gene 155:179-184(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Cervix, and Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61. RX PubMed=1970326; DOI=10.1016/0888-7543(90)90475-a; RA Shull M.M., Pugh D.G., Lingrel J.B.; RT "The human Na, K-ATPase alpha 1 gene: characterization of the 5'-flanking RT region and identification of a restriction fragment length polymorphism."; RL Genomics 6:451-460(1990). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-148. RC TISSUE=Placenta; RA Zhang J.-S., Yang J.X., Fang M.W., Lu S.D.; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 168-189 AND 213-244. RX PubMed=3035563; DOI=10.1073/pnas.84.12.4039; RA Shull M.M., Lingrel J.B.; RT "Multiple genes encode the human Na+,K+-ATPase catalytic subunit."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4039-4043(1987). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 198-943 (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=2891135; DOI=10.1073/pnas.84.22.7901; RA Chehab F.F., Kan Y.W., Law M.L., Hartz J., Kao F.T., Blostein R.; RT "Human placental Na+,K+-ATPase alpha subunit: cDNA cloning, tissue RT expression, DNA polymorphism, and chromosomal localization."; RL Proc. Natl. Acad. Sci. U.S.A. 84:7901-7905(1987). RN [11] RP PROTEIN SEQUENCE OF 199-216, AND INTERACTION WITH HLA-DR1. RX PubMed=1380674; DOI=10.1038/358764a0; RA Chicz R.M., Urban R.G., Lane W.S., Gorga J.C., Stern L.J., Vignali D.A.A., RA Strominger J.L.; RT "Predominant naturally processed peptides bound to HLA-DR1 are derived from RT MHC-related molecules and are heterogeneous in size."; RL Nature 358:764-768(1992). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-341 AND 420-444. RX PubMed=3036582; DOI=10.1016/0014-5793(87)80677-4; RA Sverdlov E.D., Monastyrskaya G.S., Broude N.E., Ushkaryov Y.A., RA Allikmets R.L., Melkov A.M., Smirnov Y.V., Malyshev I.V., Dulubova I.E., RA Petrukhin K.E., Gryshin A.V., Kiyatkin N.I., Kostina M.B., Sverdlov V.E., RA Modyanov N.N., Ovchinnikov Y.A.; RT "The family of human Na+,K+-ATPase genes. No less than five genes and/or RT pseudogenes related to the alpha-subunit."; RL FEBS Lett. 217:275-278(1987). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] OF 471-619. RA Ovchinnikov Y.A., Monastyrskaya G.S., Arsenyan S.G., Broude N.E., RA Petrukhin K.E., Grishin A.V., Arzamazova N.M., Severtsova I.V., RA Modyanov N.N.; RT "Amino acid sequence of the 17-kilodalton fragment of the cytoplasmic RT region of the alpha-subunit of NA+,K+-ATPase."; RL Dokl. Biochem. 288:270-272(1986). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=7711835; DOI=10.3109/09687689409160435; RA Hundal H.S., Maxwell D.L., Ahmed A., Darakhshan F., Mitsumoto Y., Klip A.; RT "Subcellular distribution and immunocytochemical localization of Na,K- RT ATPase subunit isoforms in human skeletal muscle."; RL Mol. Membr. Biol. 11:255-262(1994). RN [15] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [16] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Melanoma; RX PubMed=17081065; DOI=10.1021/pr060363j; RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.; RT "Proteomic and bioinformatic characterization of the biogenesis and RT function of melanosomes."; RL J. Proteome Res. 5:3135-3144(2006). RN [17] RP INTERACTION WITH CLN3. RX PubMed=18621045; DOI=10.1016/j.yexcr.2008.06.016; RA Uusi-Rauva K., Luiro K., Tanhuanpaeae K., Kopra O., Martin-Vasallo P., RA Kyttaelae A., Jalanko A.; RT "Novel interactions of CLN3 protein link Batten disease to dysregulation of RT fodrin-Na+, K+ ATPase complex."; RL Exp. Cell Res. 314:2895-2905(2008). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-542, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP INTERACTION WITH FXYD3. RX PubMed=21454534; DOI=10.1074/jbc.m110.184101; RA Bibert S., Liu C.C., Figtree G.A., Garcia A., Hamilton E.J., Marassi F.M., RA Sweadner K.J., Cornelius F., Geering K., Rasmussen H.H.; RT "FXYD proteins reverse inhibition of the Na+-K+ pump mediated by RT glutathionylation of its beta1 subunit."; RL J. Biol. Chem. 286:18562-18572(2011). RN [22] RP INTERACTION WITH SLC35G1 AND STIM1. RX PubMed=22084111; DOI=10.1073/pnas.1117231108; RA Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.; RT "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to RT multiple transporters."; RL Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [26] RP INVOLVEMENT IN CMT2DD, VARIANTS CMT2DD ARG-48; THR-592; THR-597; ALA-600; RP THR-600; PHE-601 AND ALA-811, CHARACTERIZATION OF VARIANTS CMT2DD ARG-48; RP ALA-600 AND ALA-811, AND FUNCTION. RX PubMed=29499166; DOI=10.1016/j.ajhg.2018.01.023; RA Lassuthova P., Rebelo A.P., Ravenscroft G., Lamont P.J., Davis M.R., RA Manganelli F., Feely S.M., Bacon C., Brozkova D.S., Haberlova J., RA Mazanec R., Tao F., Saghira C., Abreu L., Courel S., Powell E., Buglo E., RA Bis D.M., Baxter M.F., Ong R.W., Marns L., Lee Y.C., Bai Y., Isom D.G., RA Barro-Soria R., Chung K.W., Scherer S.S., Larsson H.P., Laing N.G., RA Choi B.O., Seeman P., Shy M.E., Santoro L., Zuchner S.; RT "Mutations in ATP1A1 Cause Dominant Charcot-Marie-Tooth Type 2."; RL Am. J. Hum. Genet. 102:505-514(2018). RN [27] RP INVOLVEMENT IN HOMGSMR2, VARIANTS HOMGSMR2 ARG-302; ARG-303 AND ARG-859, RP CHARACTERIZATION OF VARIANTS HOMGSMR2 ARG-302; ARG-303 AND ARG-859, AND RP FUNCTION. RX PubMed=30388404; DOI=10.1016/j.ajhg.2018.10.004; RA Schlingmann K.P., Bandulik S., Mammen C., Tarailo-Graovac M., Holm R., RA Baumann M., Koenig J., Lee J.J.Y., Droegemoeller B., Imminger K., RA Beck B.B., Altmueller J., Thiele H., Waldegger S., Van't Hoff W., Kleta R., RA Warth R., van Karnebeek C.D.M., Vilsen B., Bockenhauer D., Konrad M.; RT "Germline de novo mutations in ATP1A1 cause renal hypomagnesemia, RT refractory seizures, and intellectual disability."; RL Am. J. Hum. Genet. 103:808-816(2018). RN [28] {ECO:0007744|PDB:7E1Z, ECO:0007744|PDB:7E20, ECO:0007744|PDB:7E21} RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) OF 1-1023 IN COMPLEX WITH RP AT1B1; FXYD2; NA(+); K(+) AND MG(2+). RX PubMed=35803952; DOI=10.1038/s41467-022-31602-y; RA Guo Y., Zhang Y., Yan R., Huang B., Ye F., Wu L., Chi X., Shi Y., Zhou Q.; RT "Cryo-EM structures of recombinant human sodium-potassium pump determined RT in three different states."; RL Nat. Commun. 13:3957-3957(2022). RN [29] {ECO:0007744|PDB:9KCG, ECO:0007744|PDB:9KCI, ECO:0007744|PDB:9KCJ, ECO:0007744|PDB:9KCK, ECO:0007744|PDB:9KCL, ECO:0007744|PDB:9KCM, ECO:0007744|PDB:9KCR} RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF 39-1023 IN COMPLEX RP WITH MG(2+). RA Dou Y., Abe K., Suzuki J.; RT "Structural basis of a sodium pump quaternary complex leading phospholipid RT scrambling in the living cell."; RL Submitted (NOV-2024) to the PDB data bank. CC -!- FUNCTION: Catalytic subunit of the Na(+)/K(+)-ATPase pump that CC hydrolyzes ATP to exchange ions across the plasma membrane, exporting 3 CC Na(+) and importing 2 K(+) per cycle against electrochemical gradients CC (PubMed:29499166, PubMed:30388404, PubMed:35803952). It undergoes ATP- CC driven conformational changes that allow alternating binding and CC release of Na(+) and K(+) ions across the membrane (PubMed:35803952). CC This process maintains essential Na(+) and K(+) gradients for membrane CC potential and cellular function. Could also be part of an osmosensory CC signaling pathway that senses body-fluid sodium levels and controls CC salt intake behavior as well as voluntary water intake to regulate CC sodium homeostasis (By similarity). {ECO:0000250|UniProtKB:Q8VDN2, CC ECO:0000269|PubMed:29499166, ECO:0000269|PubMed:30388404, CC ECO:0000269|PubMed:35803952}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 K(+)(out) + 3 Na(+)(in) + ATP + H2O = 2 K(+)(in) + 3 CC Na(+)(out) + ADP + phosphate + H(+); Xref=Rhea:RHEA:18353, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, CC ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; EC=7.2.2.13; CC Evidence={ECO:0000269|PubMed:35803952}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:35803952}; CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an CC additional regulatory subunit, called FXYD. There are four, three and CC seven isoforms for the alpha, beta and regulatory subunits, CC respectively, among which the expression of the alpha isoforms is CC tissue-specific (PubMed:35803952). The particular alpha/beta/FXYD CC combination in each tissue defines the pump's kinetic and regulatory CC properties. Interacts with ATP1B1 (PubMed:35803952). Interacts with CC regulatory subunit FXYD2 (PubMed:35803952). Interacts with regulatory CC subunit FXYD1 (By similarity). Interacts with regulatory subunit FXYD3 CC (PubMed:21454534). Interacts with SIK1 (By similarity). Binds the HLA CC class II histocompatibility antigen DR1 (PubMed:1380674). Interacts CC with SLC35G1 and STIM1 (PubMed:22084111). Interacts with CLN3; this CC interaction regulates the sodium/potassium-transporting ATPase complex CC localization at the plasma membrane (Probable). Interacts with SCN7A; CC activates ATP1A1 P-type sodium:potassium-exchanging transporter CC activity which indirectly signals to nearby neurons to regulate sodium CC homeostasis (By similarity). {ECO:0000250|UniProtKB:P06685, CC ECO:0000250|UniProtKB:Q08DA1, ECO:0000250|UniProtKB:Q8VDN2, CC ECO:0000269|PubMed:1380674, ECO:0000269|PubMed:21454534, CC ECO:0000269|PubMed:22084111, ECO:0000269|PubMed:35803952, CC ECO:0000305|PubMed:18621045}. CC -!- INTERACTION: CC P05023; P05026: ATP1B1; NbExp=16; IntAct=EBI-358778, EBI-714630; CC P05023; Q92597: NDRG1; NbExp=2; IntAct=EBI-358778, EBI-716486; CC P05023; P13693: TPT1; NbExp=5; IntAct=EBI-358778, EBI-1783169; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; CC Multi-pass membrane protein {ECO:0000269|PubMed:35803952}. Basolateral CC cell membrane {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane CC protein {ECO:0000269|PubMed:35803952}. Cell membrane, sarcolemma CC {ECO:0000269|PubMed:7711835}; Multi-pass membrane protein CC {ECO:0000269|PubMed:35803952}. Cell projection, axon CC {ECO:0000250|UniProtKB:P06685}. Melanosome CC {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in CC melanosome fractions from stage I to stage IV. CC {ECO:0000269|PubMed:17081065}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=Long; CC IsoId=P05023-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P05023-2; Sequence=VSP_000415, VSP_000416; CC Name=3; CC IsoId=P05023-3; Sequence=VSP_044242; CC Name=4; CC IsoId=P05023-4; Sequence=VSP_047309; CC -!- DOMAIN: Undergoes ATP-driven conformational changes associated with a CC transient phosphorylation that shifts the pump conformation from CC inward-facing (E1) to outward-facing state (E2). In the inward-facing CC state (E1), it binds three Na(+) ions from the cytoplasm and becomes CC phosphorylated at the active site Asp, triggering a structural shift. CC In the outward-facing state (E2), Na(+) is released outside the cell, CC two K(+) ions bind, and dephosphorylation of the active site Asp CC restores the inward-facing conformation, allowing K(+) release into the CC cytoplasm and completion of the cycle. {ECO:0000269|PubMed:35803952}. CC -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity. CC Phosphorylation of Ser-943 by PKA modulates the response of ATP1A1 to CC PKC. Dephosphorylation by protein phosphatase 2A (PP2A) following CC increases in intracellular sodium, leading to increase catalytic CC activity (By similarity). {ECO:0000250}. CC -!- DISEASE: Charcot-Marie-Tooth disease, axonal, type 2DD (CMT2DD) CC [MIM:618036]: A dominant axonal form of Charcot-Marie-Tooth disease, a CC disorder of the peripheral nervous system, characterized by progressive CC weakness and atrophy, initially of the peroneal muscles and later of CC the distal muscles of the arms. Charcot-Marie-Tooth disease is CC classified in two main groups on the basis of electrophysiologic CC properties and histopathology: primary peripheral demyelinating CC neuropathies (designated CMT1 when they are dominantly inherited) and CC primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 CC group are characterized by signs of axonal degeneration in the absence CC of obvious myelin alterations, normal or slightly reduced nerve CC conduction velocities, and progressive distal muscle weakness and CC atrophy. {ECO:0000269|PubMed:29499166}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Hypomagnesemia, seizures, and impaired intellectual CC development 2 (HOMGSMR2) [MIM:618314]: An autosomal dominant disease CC characterized by generalized seizures in infancy, severe CC hypomagnesemia, and renal magnesium wasting. Seizures persist despite CC magnesium supplementation and are associated with significant CC intellectual disability. {ECO:0000269|PubMed:30388404}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3) CC family. Type IIC subfamily. {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; D00099; BAA00061.1; -; mRNA. DR EMBL; X04297; CAA27840.1; -; mRNA. DR EMBL; U16798; AAC50131.1; -; mRNA. DR EMBL; AK295095; BAH11971.1; -; mRNA. DR EMBL; AK296362; BAH12332.1; -; mRNA. DR EMBL; AK314777; BAG37313.1; -; mRNA. DR EMBL; AL136376; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471122; EAW56644.1; -; Genomic_DNA. DR EMBL; BC003077; AAH03077.1; -; mRNA. DR EMBL; BC001330; AAH01330.1; -; mRNA. DR EMBL; BC050359; AAH50359.1; -; mRNA. DR EMBL; M30310; AAA51801.1; -; Genomic_DNA. DR EMBL; M30309; AAA51801.1; JOINED; Genomic_DNA. DR EMBL; L76938; AAA92713.1; -; Genomic_DNA. DR EMBL; M16793; AAD56251.1; -; mRNA. DR EMBL; M16794; AAD56252.1; -; mRNA. DR EMBL; J03007; AAA51803.1; -; mRNA. DR EMBL; M27572; AAA35573.1; -; Genomic_DNA. DR EMBL; M27579; AAA35574.2; -; Genomic_DNA. DR EMBL; X03757; CAA27390.1; -; mRNA. DR CCDS; CCDS53351.1; -. [P05023-4] DR CCDS; CCDS53352.1; -. [P05023-3] DR CCDS; CCDS887.1; -. [P05023-1] DR PIR; A24414; A24414. DR RefSeq; NP_000692.2; NM_000701.8. [P05023-1] DR RefSeq; NP_001153705.1; NM_001160233.2. [P05023-4] DR RefSeq; NP_001153706.1; NM_001160234.2. [P05023-3] DR PDB; 7E1Z; EM; 3.20 A; A=1-1023. DR PDB; 7E20; EM; 2.70 A; A=1-1023. DR PDB; 7E21; EM; 2.90 A; A=1-1023. DR PDB; 9KCG; EM; 3.10 A; A=39-1023. DR PDB; 9KCI; EM; 2.90 A; A=39-1023. DR PDB; 9KCJ; EM; 3.10 A; A=39-1023. DR PDB; 9KCK; EM; 2.90 A; A=39-1023. DR PDB; 9KCL; EM; 2.90 A; A=39-1023. DR PDB; 9KCM; EM; 2.90 A; A=39-1023. DR PDB; 9KCR; EM; 3.20 A; A=39-1023. DR AlphaFoldDB; P05023; -. DR BMRB; P05023; -. DR EMDB; EMD-30947; -. DR EMDB; EMD-30948; -. DR EMDB; EMD-30949; -. DR EMDB; EMD-62250; -. DR EMDB; EMD-62252; -. DR EMDB; EMD-62253; -. DR EMDB; EMD-62254; -. DR EMDB; EMD-62255; -. DR EMDB; EMD-62256; -. DR EMDB; EMD-62260; -. DR SMR; P05023; -. DR BioGRID; 106966; 615. DR ComplexPortal; CPX-125; Sodium:potassium-exchanging ATPase complex, FXYD2 variant. DR ComplexPortal; CPX-8009; Sodium:potassium-exchanging ATPase complex, FXYD1 variant. DR ComplexPortal; CPX-8141; Sodium:potassium-exchanging ATPase complex, FXYD3 variant. DR ComplexPortal; CPX-8142; Sodium:potassium-exchanging ATPase complex, FXYD4 variant. DR ComplexPortal; CPX-8143; Sodium:potassium-exchanging ATPase complex, FXYD5 variant. DR ComplexPortal; CPX-8144; Sodium:potassium-exchanging ATPase complex, FXYD6 variant. DR ComplexPortal; CPX-8146; Sodium:potassium-exchanging ATPase complex, FXYD7 variant. DR CORUM; P05023; -. DR DIP; DIP-38196N; -. DR FunCoup; P05023; 2069. DR IntAct; P05023; 214. DR MINT; P05023; -. DR NDEx; IQUERY-CP-ATP1A1; 4 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000445306; -. DR BindingDB; P05023; -. DR ChEMBL; CHEMBL1807; -. DR DrugBank; DB00511; Acetyldigitoxin. DR DrugBank; DB01430; Almitrine. DR DrugBank; DB01370; Aluminium. DR DrugBank; DB14517; Aluminium phosphate. DR DrugBank; DB14518; Aluminum acetate. DR DrugBank; DB06697; Artemether. DR DrugBank; DB01244; Bepridil. DR DrugBank; DB09020; Bisacodyl. DR DrugBank; DB01158; Bretylium. DR DrugBank; DB01161; Chloroprocaine. DR DrugBank; DB01188; Ciclopirox. DR DrugBank; DB01078; Deslanoside. DR DrugBank; DB04177; Digitoxigenin. DR DrugBank; DB01396; Digitoxin. DR DrugBank; DB00390; Digoxin. DR DrugBank; DB00903; Etacrynic acid. DR DrugBank; DB00774; Hydroflumethiazide. DR DrugBank; DB06157; Istaroxime. DR DrugBank; DB06708; Lumefantrine. DR DrugBank; DB13996; Magnesium acetate. DR DrugBank; DB01378; Magnesium cation. DR DrugBank; DB13749; Magnesium gluconate. DR DrugBank; DB14515; Magnesium lactate. DR DrugBank; DB14514; Magnesium levulinate. DR DrugBank; DB12843; Oleandrin. DR DrugBank; DB01250; Olsalazine. DR DrugBank; DB01092; Ouabain. DR DrugBank; DB14500; Potassium. DR DrugBank; DB14498; Potassium acetate. DR DrugBank; DB01345; Potassium cation. DR DrugBank; DB13620; Potassium gluconate. DR DrugBank; DB14499; Potassium sulfate. DR DrugBank; DB12350; Rostafuroxin. DR DrugBank; DB09479; Rubidium Rb-82. DR DrugBank; DB16690; Tegoprazan. DR DrugBank; DB01021; Trichlormethiazide. DR DrugCentral; P05023; -. DR TCDB; 3.A.3.1.1; the p-type atpase (p-atpase) superfamily. DR CarbonylDB; P05023; -. DR GlyCosmos; P05023; 1 site, 1 glycan. DR GlyGen; P05023; 2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site). DR iPTMnet; P05023; -. DR MetOSite; P05023; -. DR PhosphoSitePlus; P05023; -. DR SwissPalm; P05023; -. DR BioMuta; ATP1A1; -. DR DMDM; 114374; -. DR jPOST; P05023; -. DR MassIVE; P05023; -. DR PaxDb; 9606-ENSP00000445306; -. DR PeptideAtlas; P05023; -. DR ProteomicsDB; 26208; -. DR ProteomicsDB; 51768; -. [P05023-1] DR ProteomicsDB; 51769; -. [P05023-2] DR ProteomicsDB; 6547; -. DR Pumba; P05023; -. DR Antibodypedia; 4542; 760 antibodies from 44 providers. DR DNASU; 476; -. DR Ensembl; ENST00000295598.10; ENSP00000295598.5; ENSG00000163399.17. [P05023-1] DR Ensembl; ENST00000369496.8; ENSP00000358508.4; ENSG00000163399.17. [P05023-3] DR Ensembl; ENST00000537345.5; ENSP00000445306.1; ENSG00000163399.17. [P05023-4] DR Ensembl; ENST00000897938.1; ENSP00000567997.1; ENSG00000163399.17. [P05023-1] DR GeneID; 476; -. DR KEGG; hsa:476; -. DR MANE-Select; ENST00000295598.10; ENSP00000295598.5; NM_000701.8; NP_000692.2. DR UCSC; uc001ege.5; human. [P05023-1] DR AGR; HGNC:799; -. DR ClinPGx; PA62; -. DR CTD; 476; -. DR DisGeNET; 476; -. DR GeneCards; ATP1A1; -. DR HGNC; HGNC:799; ATP1A1. DR HPA; ENSG00000163399; Tissue enhanced (parathyroid). DR MalaCards; ATP1A1; -. DR MIM; 182310; gene. DR MIM; 618036; phenotype. DR MIM; 618314; phenotype. DR OpenTargets; ENSG00000163399; -. DR Orphanet; 521414; Autosomal dominant Charcot-Marie-Tooth disease type 2DD. DR Orphanet; 564178; Primary hypomagnesemia-refractory seizures-intellectual disability syndrome. DR VEuPathDB; HostDB:ENSG00000163399; -. DR eggNOG; KOG0203; Eukaryota. DR GeneTree; ENSGT00940000154840; -. DR HOGENOM; CLU_002360_4_3_1; -. DR InParanoid; P05023; -. DR OMA; QQPPIFN; -. DR OrthoDB; 3352408at2759; -. DR PAN-GO; P05023; 8 GO annotations based on evolutionary models. DR PhylomeDB; P05023; -. DR BRENDA; 7.2.2.13; 2681. DR BRENDA; 7.2.2.3; 2681. DR PathwayCommons; P05023; -. DR Reactome; R-HSA-5578775; Ion homeostasis. DR Reactome; R-HSA-936837; Ion transport by P-type ATPases. DR Reactome; R-HSA-9679191; Potential therapeutics for SARS. DR SignaLink; P05023; -. DR SIGNOR; P05023; -. DR Agora; ENSG00000163399; -. DR BioGRID-ORCS; 476; 666 hits in 1200 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; ATP1A1; human. DR GeneWiki; ATPase,_Na%2B/K%2B_transporting,_alpha_1; -. DR GenomeRNAi; 476; -. DR Pharos; P05023; Tclin. DR PRO; PR:P05023; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P05023; protein. DR Bgee; ENSG00000163399; Expressed in renal medulla and 213 other cell types or tissues. DR ExpressionAtlas; P05023; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:BHF-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:BHF-UCL. DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042470; C:melanosome; EXP:UniProtKB. DR GO; GO:0016020; C:membrane; ISS:UniProtKB. DR GO; GO:0045121; C:membrane raft; ISS:ARUK-UCL. DR GO; GO:0031090; C:organelle membrane; IGI:ARUK-UCL. DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0042383; C:sarcolemma; ISS:BHF-UCL. DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL. DR GO; GO:0036126; C:sperm flagellum; IDA:ARUK-UCL. DR GO; GO:0030315; C:T-tubule; IGI:ARUK-UCL. DR GO; GO:0005524; F:ATP binding; ISS:BHF-UCL. DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProt. DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:BHF-UCL. DR GO; GO:0016791; F:phosphatase activity; IEA:Ensembl. DR GO; GO:0030955; F:potassium ion binding; ISS:BHF-UCL. DR GO; GO:0051087; F:protein-folding chaperone binding; IPI:BHF-UCL. DR GO; GO:0031402; F:sodium ion binding; ISS:BHF-UCL. DR GO; GO:1990239; F:steroid hormone binding; IDA:BHF-UCL. DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl. DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; TAS:BHF-UCL. DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL. DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:BHF-UCL. DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; NAS:ComplexPortal. DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IDA:BHF-UCL. DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IDA:BHF-UCL. DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL. DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; IC:BHF-UCL. DR GO; GO:0007231; P:osmosensory signaling pathway; IEA:Ensembl. DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL. DR GO; GO:0071805; P:potassium ion transmembrane transport; IGI:ARUK-UCL. DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central. DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB. DR GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL. DR GO; GO:1903416; P:response to glycoside; IDA:BHF-UCL. DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL. DR GO; GO:0035725; P:sodium ion transmembrane transport; IGI:ARUK-UCL. DR CDD; cd02608; P-type_ATPase_Na-K_like; 1. DR FunFam; 1.20.1110.10:FF:000163; -; 1. DR FunFam; 2.70.150.10:FF:000106; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 3.40.1110.10:FF:000001; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 3.40.50.1000:FF:000004; Sodium/potassium-transporting ATPase subunit alpha; 1. DR FunFam; 1.20.1110.10:FF:000095; Sodium/potassium-transporting ATPase subunit alpha-1; 2. DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1. DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1. DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C. DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N. DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf. DR InterPro; IPR059000; ATPase_P-type_domA. DR InterPro; IPR050510; Cation_transp_ATPase_P-type. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR005775; P-type_ATPase_IIC. DR InterPro; IPR001757; P_typ_ATPase. DR InterPro; IPR044492; P_typ_ATPase_HD_dom. DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 2. DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1. DR PANTHER; PTHR43294:SF9; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-1; 1. DR Pfam; PF13246; Cation_ATPase; 1. DR Pfam; PF00689; Cation_ATPase_C; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00121; NAKATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1. DR SFLD; SFLDF00027; p-type_atpase; 1. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1. DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell membrane; Cell projection; Charcot-Marie-Tooth disease; KW Direct protein sequencing; Epilepsy; Intellectual disability; KW Ion transport; Magnesium; Membrane; Metal-binding; Neurodegeneration; KW Neuropathy; Nucleotide-binding; Phosphoprotein; Potassium; KW Potassium transport; Primary hypomagnesemia; Proteomics identification; KW Reference proteome; Sodium; Sodium transport; Sodium/potassium transport; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..1023 FT /note="Sodium/potassium-transporting ATPase subunit alpha- FT 1" FT /id="PRO_0000002484" FT TOPO_DOM 1..91 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 92..116 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 117..127 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 128..148 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 149..290 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 291..312 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 313..318 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 319..342 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 343..772 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 773..795 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 796..803 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 804..822 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 823..844 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 845..870 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 871..917 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 918..938 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 939..951 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT TRANSMEM 952..970 FT /note="Helical" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 971..984 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 985..1008 FT /note="Helical" FT /evidence="ECO:0000255, ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT TOPO_DOM 1009..1023 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REGION 1..39 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 82..84 FT /note="Phosphoinositide-3 kinase binding" FT /evidence="ECO:0000250" FT REGION 216..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 596..717 FT /note="Mediates interaction with SCN7A" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT COMPBIAS 1..11 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 28..39 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 376 FT /note="4-aspartylphosphate intermediate" FT /evidence="ECO:0000250|UniProtKB:P19156" FT BINDING 329 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 330 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 332 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 334 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 376 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:35803952, ECO:0000269|Ref.29, FT ECO:0007744|PDB:7E20, ECO:0007744|PDB:9KCI, FT ECO:0007744|PDB:9KCK" FT BINDING 378 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 378 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:35803952, ECO:0000269|Ref.29, FT ECO:0007744|PDB:7E20, ECO:0007744|PDB:9KCI, FT ECO:0007744|PDB:9KCK" FT BINDING 450 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 453 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 482 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 484 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 487 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 551 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 617 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 618 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 692 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000250|UniProtKB:P05024" FT BINDING 717 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|PubMed:35803952, ECO:0000269|Ref.29, FT ECO:0007744|PDB:7E20, ECO:0007744|PDB:9KCI, FT ECO:0007744|PDB:9KCK" FT BINDING 721 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000269|Ref.29, ECO:0007744|PDB:9KCG" FT BINDING 747 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 778 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="3" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 779 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 781 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="3" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 782 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="1" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 782 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="3" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 783 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 786 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /note="covalent" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 811 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 811 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 814 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="3" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 815 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="2" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 815 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="3" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT BINDING 930 FT /ligand="Na(+)" FT /ligand_id="ChEBI:CHEBI:29101" FT /ligand_label="3" FT /ligand_note="in E1-3Na state" FT /evidence="ECO:0000269|PubMed:35803952, FT ECO:0007744|PDB:7E20" FT MOD_RES 9 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 10 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P06685" FT MOD_RES 16 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 21 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 40 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06685" FT MOD_RES 47 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06685" FT MOD_RES 228 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 260 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 452 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06685" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06685" FT MOD_RES 542 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 661 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 668 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 675 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8VDN2" FT MOD_RES 943 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000250|UniProtKB:P06685" FT VAR_SEQ 1..31 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_044242" FT VAR_SEQ 2..4 FT /note="GKG -> AFK (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047309" FT VAR_SEQ 638..681 FT /note="NETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDI -> SGPM FT SRGKSWSSPATQPSSSVSWWCSGPTWSSVRPGGIRSSSRG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7536695" FT /id="VSP_000415" FT VAR_SEQ 682..1023 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7536695" FT /id="VSP_000416" FT VARIANT 47 FT /note="S -> I (in dbSNP:rs12564026)" FT /id="VAR_048374" FT VARIANT 48 FT /note="L -> R (in CMT2DD; no effect on Na(+)-dependent FT currents; dbSNP:rs1553190285)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081039" FT VARIANT 302 FT /note="L -> R (in HOMGSMR2; results in altered sodium and FT potassium transport as shown by in vitro functional FT expression of the homologous rat variant; FT dbSNP:rs1557785499)" FT /evidence="ECO:0000269|PubMed:30388404" FT /id="VAR_081937" FT VARIANT 303 FT /note="G -> R (in HOMGSMR2; results in altered sodium and FT potassium transport as shown by in vitro functional FT expression of the homologous rat variant; FT dbSNP:rs1557785503)" FT /evidence="ECO:0000269|PubMed:30388404" FT /id="VAR_081938" FT VARIANT 592 FT /note="I -> T (in CMT2DD; uncertain significance; FT dbSNP:rs1553192086)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081040" FT VARIANT 597 FT /note="A -> T (in CMT2DD; uncertain significance)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081041" FT VARIANT 600 FT /note="P -> A (in CMT2DD; shows fewer Na(+)-dependent FT currents than wild-type protein; dbSNP:rs1553192091)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081042" FT VARIANT 600 FT /note="P -> T (in CMT2DD; uncertain significance; FT dbSNP:rs1553192091)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081043" FT VARIANT 601 FT /note="D -> F (in CMT2DD; uncertain significance; requires FT 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081044" FT VARIANT 811 FT /note="D -> A (in CMT2DD; shows fewer Na(+)-dependent FT currents than wild-type protein; dbSNP:rs1553192783)" FT /evidence="ECO:0000269|PubMed:29499166" FT /id="VAR_081045" FT VARIANT 859 FT /note="M -> R (in HOMGSMR2; results in altered sodium and FT potassium transport as shown by in vitro functional FT expression of the homologous rat variant; FT dbSNP:rs781629728)" FT /evidence="ECO:0000269|PubMed:30388404" FT /id="VAR_081939" FT CONFLICT 248 FT /note="N -> S (in Ref. 3; BAG37313)" FT /evidence="ECO:0000305" FT CONFLICT 323 FT /note="F -> L (in Ref. 3; BAH11971)" FT /evidence="ECO:0000305" FT CONFLICT 475 FT /note="A -> T (in Ref. 13; CAA27390)" FT /evidence="ECO:0000305" FT CONFLICT 499 FT /note="S -> A (in Ref. 13; CAA27390)" FT /evidence="ECO:0000305" FT CONFLICT 502 FT /note="Q -> R (in Ref. 13; CAA27390)" FT /evidence="ECO:0000305" FT CONFLICT 523 FT /note="L -> I (in Ref. 13; CAA27390)" FT /evidence="ECO:0000305" FT CONFLICT 892 FT /note="D -> G (in Ref. 3; BAH11971)" FT /evidence="ECO:0000305" FT HELIX 31..34 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 50..54 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 65..75 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 88..93 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 95..97 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 100..119 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 120..122 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 128..149 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 157..161 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 182..184 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 190..194 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 197..199 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 201..209 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 211..214 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 225..227 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 240..243 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 251..260 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 262..264 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 266..276 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 283..305 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 309..312 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 317..329 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 336..352 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 353..355 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 363..366 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 372..376 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 377..381 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 387..391 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 404..407 FT /evidence="ECO:0007829|PDB:7E21" FT HELIX 416..427 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 442..444 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 451..463 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 468..473 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 476..480 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 481..483 FT /evidence="ECO:0007829|PDB:7E1Z" FT TURN 484..486 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 488..493 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 496..500 FT /evidence="ECO:0007829|PDB:7E21" FT STRAND 502..509 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 511..514 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 515..517 FT /evidence="ECO:0007829|PDB:7E21" FT STRAND 521..523 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 526..528 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 532..546 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 547..549 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 551..558 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 562..564 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 567..569 FT /evidence="ECO:0007829|PDB:7E1Z" FT STRAND 573..575 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 587..592 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 599..608 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 612..616 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 621..631 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 641..647 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 652..654 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 661..666 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 668..671 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 675..684 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 686..692 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 695..707 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 712..716 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 719..721 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 722..727 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 728..737 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 740..744 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 747..750 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 756..781 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 784..795 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 798..800 FT /evidence="ECO:0007829|PDB:7E21" FT HELIX 805..809 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 810..814 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 816..820 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 821..824 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 825..828 FT /evidence="ECO:0007829|PDB:7E1Z" FT HELIX 831..833 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 835..838 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 839..842 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 847..850 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 851..857 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 858..876 FT /evidence="ECO:0007829|PDB:7E20" FT TURN 880..885 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 887..891 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 908..936 FT /evidence="ECO:0007829|PDB:7E20" FT STRAND 940..942 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 944..947 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 952..970 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 974..977 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 982..984 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 985..989 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 992..1011 FT /evidence="ECO:0007829|PDB:7E20" FT HELIX 1016..1021 FT /evidence="ECO:0007829|PDB:7E20" SQ SEQUENCE 1023 AA; 112896 MW; F3C6FDE04FB3F667 CRC64; MGKGVGRDKY EPAAVSEQGD KKGKKGKKDR DMDELKKEVS MDDHKLSLDE LHRKYGTDLS RGLTSARAAE ILARDGPNAL TPPPTTPEWI KFCRQLFGGF SMLLWIGAIL CFLAYSIQAA TEEEPQNDNL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI NAEEVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAAEIEH FIHIITGVAV FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWLA LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI ELCCGSVKEM RERYAKIVEI PFNSTNKYQL SIHKNPNTSE PQHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN AYLELGGLGE RVLGFCHLFL PDEQFPEGFQ FDTDDVNFPI DNLCFVGLIS MIDPPRAAVP DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA KACVVHGSDL KDMTSEQLDD ILKYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP IHLLGLRVDW DDRWINDVED SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY CPGMGVALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE TYY //