AT1A1_HUMAN
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 03-AUG-2022, entry version 247.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE Short=Na(+)/K(+) ATPase alpha-1 subunit;
DE EC=7.2.2.13;
DE AltName: Full=Sodium pump subunit alpha-1;
DE Flags: Precursor;
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).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC {ECO:0000269|PubMed:29499166, ECO:0000269|PubMed:30388404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC EC=7.2.2.13;
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. Interacts with regulatory subunit FXYD1
CC (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).
CC {ECO:0000250|UniProtKB:P06685, ECO:0000269|PubMed:1380674,
CC ECO:0000269|PubMed:21454534, ECO:0000269|PubMed:22084111,
CC ECO:0000305|PubMed:18621045}.
CC -!- INTERACTION:
CC P05023; P05026: ATP1B1; NbExp=2; IntAct=EBI-358778, EBI-714630;
CC P05023; P13693: TPT1; NbExp=5; IntAct=EBI-358778, EBI-1783169;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:7711835};
CC Multi-pass membrane protein {ECO:0000255}. 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 -!- 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 2DD (CMT2DD) [MIM:618036]: A
CC dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the
CC peripheral nervous system, characterized by progressive weakness and
CC atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group
CC are characterized by signs of axonal degeneration in the absence of
CC obvious myelin alterations, normal or slightly reduced nerve conduction
CC velocities, and progressive distal muscle weakness and atrophy.
CC {ECO:0000269|PubMed:29499166}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Hypomagnesemia, seizures, and intellectual disability 2
CC (HOMGSMR2) [MIM:618314]: An autosomal dominant disease characterized by
CC generalized seizures in infancy, severe hypomagnesemia, and renal
CC magnesium wasting. Seizures persist despite magnesium supplementation
CC and are associated with significant intellectual disability.
CC {ECO:0000269|PubMed:30388404}. Note=The disease is caused by variants
CC affecting the gene represented in this 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}.
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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_000701.7. [P05023-1]
DR RefSeq; NP_001153705.1; NM_001160233.1. [P05023-4]
DR RefSeq; NP_001153706.1; NM_001160234.1. [P05023-3]
DR RefSeq; XP_016856849.1; XM_017001360.1. [P05023-3]
DR RefSeq; XP_016856850.1; XM_017001361.1. [P05023-3]
DR AlphaFoldDB; P05023; -.
DR BMRB; P05023; -.
DR SMR; P05023; -.
DR BioGRID; 106966; 344.
DR ComplexPortal; CPX-125; Sodium:potassium-exchanging ATPase complex.
DR DIP; DIP-38196N; -.
DR IntAct; P05023; 141.
DR MINT; P05023; -.
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; DB01244; Bepridil.
DR DrugBank; DB09020; Bisacodyl.
DR DrugBank; DB01158; Bretylium.
DR DrugBank; DB01188; Ciclopirox.
DR DrugBank; DB01078; Deslanoside.
DR DrugBank; DB01119; Diazoxide.
DR DrugBank; DB01396; Digitoxin.
DR DrugBank; DB00390; Digoxin.
DR DrugBank; DB00903; Etacrynic acid.
DR DrugBank; DB00774; Hydroflumethiazide.
DR DrugBank; DB06157; Istaroxime.
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; 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; 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 GlyGen; P05023; 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 EPD; P05023; -.
DR jPOST; P05023; -.
DR MassIVE; P05023; -.
DR MaxQB; P05023; -.
DR PaxDb; P05023; -.
DR PeptideAtlas; P05023; -.
DR PRIDE; P05023; -.
DR ProteomicsDB; 26208; -.
DR ProteomicsDB; 51768; -. [P05023-1]
DR ProteomicsDB; 51769; -. [P05023-2]
DR ProteomicsDB; 6547; -.
DR Antibodypedia; 4542; 739 antibodies from 40 providers.
DR DNASU; 476; -.
DR Ensembl; ENST00000295598.10; ENSP00000295598.5; ENSG00000163399.16. [P05023-1]
DR Ensembl; ENST00000369496.8; ENSP00000358508.4; ENSG00000163399.16. [P05023-3]
DR Ensembl; ENST00000537345.5; ENSP00000445306.1; ENSG00000163399.16. [P05023-4]
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 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 neXtProt; NX_P05023; -.
DR OpenTargets; ENSG00000163399; -.
DR Orphanet; 521414; Autosomal dominant Charcot-Marie-Tooth disease type 2DD.
DR Orphanet; 85142; NON RARE IN EUROPE: Aldosterone-producing adenoma.
DR Orphanet; 564178; Primary hypomagnesemia-refractory seizures-intellectual disability syndrome.
DR PharmGKB; PA62; -.
DR VEuPathDB; HostDB:ENSG00000163399; -.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000154840; -.
DR HOGENOM; CLU_002360_4_3_1; -.
DR InParanoid; P05023; -.
DR OMA; CYIAYSV; -.
DR OrthoDB; 100699at2759; -.
DR PhylomeDB; P05023; -.
DR TreeFam; TF312838; -.
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 BioGRID-ORCS; 476; 636 hits in 1108 CRISPR screens.
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 211 other tissues.
DR ExpressionAtlas; P05023; baseline and differential.
DR Genevisible; P05023; HS.
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:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
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; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; IPI:BHF-UCL.
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:0046982; F:protein heterodimerization activity; ISS:ARUK-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: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:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IC:ComplexPortal.
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:0031947; P:negative regulation of glucocorticoid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0045823; P:positive regulation of heart contraction; IEA:Ensembl.
DR GO; GO:0045989; P:positive regulation of striated muscle contraction; IEA:Ensembl.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:Ensembl.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
DR GO; GO:0002026; P:regulation of the force of heart contraction; IEA:Ensembl.
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:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Cell membrane;
KW Cell projection; Charcot-Marie-Tooth disease; Direct protein sequencing;
KW Epilepsy; Intellectual disability; Ion transport; Magnesium; Membrane;
KW Metal-binding; Neurodegeneration; Neuropathy; Nucleotide-binding;
KW Phosphoprotein; Potassium; Potassium transport; Primary hypomagnesemia;
KW Reference proteome; Sodium; Sodium transport; Sodium/potassium transport;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..5
FT /id="PRO_0000002483"
FT CHAIN 6..1023
FT /note="Sodium/potassium-transporting ATPase subunit alpha-
FT 1"
FT /id="PRO_0000002484"
FT TOPO_DOM 6..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..131
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..338
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 339..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..792
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 793..802
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 803..823
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 824..843
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 844..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..918
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 919..938
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 939..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 952..970
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 971..985
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 986..1006
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1007..1023
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 COMPBIAS 13..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"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 717
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
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 /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; unknown pathological
FT significance; dbSNP:rs1553192086)"
FT /evidence="ECO:0000269|PubMed:29499166"
FT /id="VAR_081040"
FT VARIANT 597
FT /note="A -> T (in CMT2DD; unknown pathological
FT 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; unknown pathological
FT significance; dbSNP:rs1553192091)"
FT /evidence="ECO:0000269|PubMed:29499166"
FT /id="VAR_081043"
FT VARIANT 601
FT /note="D -> F (in CMT2DD; unknown pathological
FT significance; requires 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"
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
