ID   AT1A1_MOUSE             Reviewed;        1023 AA.
AC   Q8VDN2; Q91Z09;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 190.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
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   [2]
RP   PROTEIN SEQUENCE OF 55-61; 75-91; 163-173; 178-194; 213-240; 256-264;
RP   360-377; 414-444; 446-458; 477-494; 536-551; 597-605; 613-625; 630-658;
RP   662-683; 699-774 AND 941-950.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   INTERACTION WITH FXYD1.
RX   PubMed=17283221; DOI=10.1096/fj.06-7269com;
RA   Pavlovic D., Fuller W., Shattock M.J.;
RT   "The intracellular region of FXYD1 is sufficient to regulate cardiac Na/K
RT   ATPase.";
RL   FASEB J. 21:1539-1546(2007).
RN   [4]
RP   INTERACTION WITH FXYD3.
RX   PubMed=15743908; DOI=10.1091/mbc.e04-10-0878;
RA   Crambert G., Li C., Claeys D., Geering K.;
RT   "FXYD3 (Mat-8), a new regulator of Na,K-ATPase.";
RL   Mol. Biol. Cell 16:2363-2371(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH SCN7A, SUBCELLULAR LOCATION, AND REGION.
RX   PubMed=17408578; DOI=10.1016/j.neuron.2007.03.014;
RA   Shimizu H., Watanabe E., Hiyama T.Y., Nagakura A., Fujikawa A., Okado H.,
RA   Yanagawa Y., Obata K., Noda M.;
RT   "Glial Nax channels control lactate signaling to neurons for brain [Na+]
RT   sensing.";
RL   Neuron 54:59-72(2007).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA   Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in naive
RT   and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-668 AND SER-675, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-9 AND LYS-21, SUCCINYLATION
RP   [LARGE SCALE ANALYSIS] AT LYS-661, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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 (By similarity). Could
CC       also be part of an osmosensory signaling pathway that senses body-fluid
CC       sodium levels and controls salt intake behavior as well as voluntary
CC       water intake to regulate sodium homeostasis (PubMed:17408578).
CC       {ECO:0000250|UniProtKB:P05023, ECO:0000269|PubMed:17408578}.
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       (PubMed:17283221). Interacts with regulatory subunit FXYD3
CC       (PubMed:15743908). Interacts with SIK1 (By similarity). Interacts with
CC       SLC35G1 and STIM1 (By similarity). Interacts with CLN3; this
CC       interaction regulates the sodium/potassium-transporting ATPase complex
CC       localization at the plasma membrane (By similarity). Interacts with
CC       SCN7A; activates ATP1A1 P-type sodium:potassium-exchanging transporter
CC       activity which indirectly signals to nearby neurons to regulate sodium
CC       homeostasis (PubMed:17408578). {ECO:0000250|UniProtKB:P05023,
CC       ECO:0000250|UniProtKB:P06685, ECO:0000269|PubMed:15743908,
CC       ECO:0000269|PubMed:17283221, ECO:0000269|PubMed:17408578}.
CC   -!- INTERACTION:
CC       Q8VDN2; P11881: Itpr1; NbExp=3; IntAct=EBI-444536, EBI-541478;
CC       Q8VDN2; O35157: Slc8a1; NbExp=4; IntAct=EBI-444536, EBI-8351080;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17408578};
CC       Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell membrane, sarcolemma
CC       {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P06685}.
CC       Melanosome {ECO:0000250|UniProtKB:P05023}.
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   -!- 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; BC010319; AAH10319.1; -; mRNA.
DR   EMBL; BC021496; AAH21496.1; -; mRNA.
DR   EMBL; BC023794; AAH23794.1; -; mRNA.
DR   EMBL; BC025618; AAH25618.1; -; mRNA.
DR   EMBL; BC025627; AAH25627.1; -; mRNA.
DR   EMBL; BC025811; AAH25811.1; -; mRNA.
DR   EMBL; BC032187; AAH32187.1; -; mRNA.
DR   EMBL; BC033435; AAH33435.1; -; mRNA.
DR   EMBL; BC033471; AAH33471.1; -; mRNA.
DR   EMBL; BC042435; AAH42435.1; -; mRNA.
DR   CCDS; CCDS17683.1; -.
DR   RefSeq; NP_659149.1; NM_144900.2.
DR   AlphaFoldDB; Q8VDN2; -.
DR   BMRB; Q8VDN2; -.
DR   SMR; Q8VDN2; -.
DR   BioGRID; 198243; 36.
DR   ComplexPortal; CPX-126; Sodium:potassium-exchanging ATPase complex.
DR   DIP; DIP-31885N; -.
DR   IntAct; Q8VDN2; 24.
DR   MINT; Q8VDN2; -.
DR   STRING; 10090.ENSMUSP00000039657; -.
DR   GlyGen; Q8VDN2; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q8VDN2; -.
DR   MetOSite; Q8VDN2; -.
DR   PhosphoSitePlus; Q8VDN2; -.
DR   SwissPalm; Q8VDN2; -.
DR   EPD; Q8VDN2; -.
DR   jPOST; Q8VDN2; -.
DR   MaxQB; Q8VDN2; -.
DR   PaxDb; 10090-ENSMUSP00000039657; -.
DR   PeptideAtlas; Q8VDN2; -.
DR   ProteomicsDB; 277119; -.
DR   Pumba; Q8VDN2; -.
DR   Antibodypedia; 4542; 940 antibodies from 40 providers.
DR   DNASU; 11928; -.
DR   Ensembl; ENSMUST00000036493.8; ENSMUSP00000039657.7; ENSMUSG00000033161.11.
DR   GeneID; 11928; -.
DR   KEGG; mmu:11928; -.
DR   UCSC; uc008qrj.2; mouse.
DR   AGR; MGI:88105; -.
DR   CTD; 476; -.
DR   MGI; MGI:88105; Atp1a1.
DR   VEuPathDB; HostDB:ENSMUSG00000033161; -.
DR   eggNOG; KOG0203; Eukaryota.
DR   GeneTree; ENSGT00940000154840; -.
DR   HOGENOM; CLU_002360_3_0_1; -.
DR   InParanoid; Q8VDN2; -.
DR   OMA; QQPPIFN; -.
DR   OrthoDB; 203629at2759; -.
DR   PhylomeDB; Q8VDN2; -.
DR   TreeFam; TF312838; -.
DR   Reactome; R-MMU-5578775; Ion homeostasis.
DR   Reactome; R-MMU-936837; Ion transport by P-type ATPases.
DR   BioGRID-ORCS; 11928; 22 hits in 78 CRISPR screens.
DR   ChiTaRS; Atp1a1; mouse.
DR   PRO; PR:Q8VDN2; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q8VDN2; Protein.
DR   Bgee; ENSMUSG00000033161; Expressed in vestibular membrane of cochlear duct and 305 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005901; C:caveola; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0005768; C:endosome; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0014704; C:intercalated disc; ISO:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; ISO:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR   GO; GO:0031090; C:organelle membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR   GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; ISO:MGI.
DR   GO; GO:0036126; C:sperm flagellum; ISO:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:BHF-UCL.
DR   GO; GO:0043531; F:ADP binding; ISO:MGI.
DR   GO; GO:0030506; F:ankyrin binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IDA:MGI.
DR   GO; GO:0016791; F:phosphatase activity; IMP:MGI.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR   GO; GO:0030955; F:potassium ion binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0051087; F:protein-folding chaperone binding; ISO:MGI.
DR   GO; GO:0031402; F:sodium ion binding; ISO:MGI.
DR   GO; GO:1990239; F:steroid hormone binding; ISO:MGI.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:MGI.
DR   GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI.
DR   GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; NAS:ComplexPortal.
DR   GO; GO:0060047; P:heart contraction; IMP:MGI.
DR   GO; GO:0030007; P:intracellular potassium ion homeostasis; ISO:MGI.
DR   GO; GO:0006883; P:intracellular sodium ion homeostasis; ISO:MGI.
DR   GO; GO:0060081; P:membrane hyperpolarization; ISO:MGI.
DR   GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR   GO; GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; IMP:MGI.
DR   GO; GO:0045822; P:negative regulation of heart contraction; IMP:MGI.
DR   GO; GO:0045823; P:positive regulation of heart contraction; IMP:MGI.
DR   GO; GO:0045989; P:positive regulation of striated muscle contraction; IMP:MGI.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:MGI.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR   GO; GO:0086004; P:regulation of cardiac muscle cell contraction; ISO:MGI.
DR   GO; GO:0002028; P:regulation of sodium ion transport; ISS:UniProtKB.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR   GO; GO:0036376; P:sodium ion export across plasma membrane; ISO:MGI.
DR   GO; GO:0006814; P:sodium ion transport; ISO:MGI.
DR   GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR   CDD; cd02608; P-type_ATPase_Na-K_like; 1.
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; 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; 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.
DR   Genevisible; Q8VDN2; MM.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell membrane; Cell projection;
KW   Direct protein sequencing; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Sodium; Sodium transport;
KW   Sodium/potassium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   PROPEP          1..5
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000002485"
FT   CHAIN           6..1023
FT                   /note="Sodium/potassium-transporting ATPase subunit alpha-
FT                   1"
FT                   /id="PRO_0000002486"
FT   TOPO_DOM        6..96
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        118..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        292..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..319
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..775
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        776..798
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        799..801
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        802..824
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        825..849
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        850..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        873..915
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        916..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        937..952
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        953..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        974..979
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        980..1000
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1001..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:0000269|PubMed:17408578"
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:0007744|PubMed:23806337"
FT   MOD_RES         10
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P06685"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P06685"
FT   MOD_RES         21
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:21183079"
FT   MOD_RES         260
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
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:0000250|UniProtKB:P05023"
FT   MOD_RES         661
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         668
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         943
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250|UniProtKB:P06685"
SQ   SEQUENCE   1023 AA;  112982 MW;  1E806D3FDFC5AD80 CRC64;
     MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
     RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRSA
     TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
     NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
     NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
     FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
     LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWFA
     LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI EVCCGSVMEM REKYSKIVEI
     PFNSTNKYQL SIHKNPNASE PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
     AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDDVNFPV DNLCFVGLIS MIDPPRAAVP
     DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA
     KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
     DSPALKKADI GVAMGIVGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
     TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
     TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWVNDVED
     SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
     ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE
     TYY
//