ID   ATN1_YEAST              Reviewed;        1091 AA.
AC   P13587; D6VS28;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   27-MAR-2024, entry version 220.
DE   RecName: Full=Sodium/potassium exporting P-type ATPase 1 {ECO:0000305};
DE            EC=7.2.2.3 {ECO:0000305|PubMed:9315618};
GN   Name=ENA1 {ECO:0000312|SGD:S000002447};
GN   Synonyms=HOR6, PMR2 {ECO:0000303|PubMed:7664728}, PMR2A;
GN   OrderedLocusNames=YDR040C {ECO:0000312|SGD:S000002447};
GN   ORFNames=YD6888.02C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2526682; DOI=10.1016/0092-8674(89)90410-8;
RA   Rudolph H.K., Antebi A., Fink G.R., Buckley C.M., Dorman T.E., Levitre J.,
RA   Davidow L.S., Mao J.-I., Moir D.T.;
RT   "The yeast secretory pathway is perturbed by mutations in PMR1, a member of
RT   a Ca2+ ATPase family.";
RL   Cell 58:133-145(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=7664728; DOI=10.1002/j.1460-2075.1995.tb00059.x;
RA   Wieland J., Nitsche A.M., Strayle J., Steiner H., Rudolph H.K.;
RT   "The PMR2 gene cluster encodes functionally distinct isoforms of a putative
RT   Na+ pump in the yeast plasma membrane.";
RL   EMBO J. 14:3870-3882(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 534-1091.
RC   STRAIN=7305B;
RX   PubMed=2046655; DOI=10.1007/bf00260720;
RA   Martinez R., Latreille M.-T., Mirande M.;
RT   "A PMR2 tandem repeat with a modified C-terminus is located downstream from
RT   the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces cerevisiae.";
RL   Mol. Gen. Genet. 227:149-154(1991).
RN   [6]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 534-1091.
RC   STRAIN=ATCC 26109 / X2180;
RX   PubMed=2903861; DOI=10.1016/s0021-9258(19)81378-9;
RA   Mirande M., Waller J.-P.;
RT   "The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid
RT   control of its expression and domain structure of the encoded protein.";
RL   J. Biol. Chem. 263:18443-18451(1988).
RN   [7]
RP   INDUCTION.
RX   PubMed=8612770; DOI=10.1016/0014-5793(96)00157-3;
RA   Marquez J.A., Serrano R.;
RT   "Multiple transduction pathways regulate the sodium-extrusion gene
RT   PMR2/ENA1 during salt stress in yeast.";
RL   FEBS Lett. 382:89-92(1996).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX   PubMed=9315618; DOI=10.1016/s0005-2736(97)00098-9;
RA   Benito B., Quintero F.J., Rodriguez-Navarro A.;
RT   "Overexpression of the sodium ATPase of Saccharomyces cerevisiae:
RT   conditions for phosphorylation from ATP and Pi.";
RL   Biochim. Biophys. Acta 1328:214-226(1997).
RN   [9]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14617094; DOI=10.1046/j.1365-313x.2003.01883.x;
RA   Benito B., Rodriguez-Navarro A.;
RT   "Molecular cloning and characterization of a sodium-pump ATPase of the moss
RT   Physcomitrella patens.";
RL   Plant J. 36:382-389(2003).
RN   [11]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [12]
RP   TOPOLOGY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA   Kim H., Melen K., Oesterberg M., von Heijne G.;
RT   "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN   [13]
RP   FUNCTION.
RX   PubMed=19915539; DOI=10.1038/nchembio.243;
RA   Ruiz A., Gonzalez A., Munoz I., Serrano R., Abrie J.A., Strauss E.,
RA   Arino J.;
RT   "Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w
RT   in yeast CoA biosynthesis.";
RL   Nat. Chem. Biol. 5:920-928(2009).
RN   [14]
RP   FUNCTION.
RX   PubMed=22329368; DOI=10.1111/j.1567-1364.2012.00793.x;
RA   Zahradka J., Sychrova H.;
RT   "Plasma-membrane hyperpolarization diminishes the cation efflux via Nha1
RT   antiporter and Ena ATPase under potassium-limiting conditions.";
RL   FEMS Yeast Res. 12:439-446(2012).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the export of
CC       sodium and potassium from the cell (PubMed:22329368, PubMed:9315618,
CC       PubMed:7664728, PubMed:14617094). May export potassium less efficiently
CC       (PubMed:14617094). May transport other cations such as lithium
CC       (PubMed:7664728, PubMed:9315618). Sodium/potassium efflux ATPases are
CC       involved in salt tolerance and maintaining the membrane potential
CC       across the plasma membrane in high salinity (Na+) or alkaline (K+)
CC       environments (PubMed:22329368, PubMed:7664728, PubMed:9315618). Is
CC       negatively modulated by SIS2/HAL3 (PubMed:19915539).
CC       {ECO:0000269|PubMed:14617094, ECO:0000269|PubMed:19915539,
CC       ECO:0000269|PubMed:22329368, ECO:0000269|PubMed:7664728,
CC       ECO:0000269|PubMed:9315618}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Na(+)(in) = ADP + H(+) + Na(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:14633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.3;
CC         Evidence={ECO:0000305|PubMed:9315618};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634;
CC         Evidence={ECO:0000305|PubMed:9315618};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(in) = ADP + H(+) + K(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:75815, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:14617094};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P04191};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}.
CC   -!- INDUCTION: By sodium ions. Induction at low salt concentrations (0.3 M)
CC       is mediated by the high-osmolarity glycerol (HOG)-MAP kinase pathway, a
CC       system activated by non-specific osmotic stress, and by the protein
CC       kinase A pathway. At high salt concentrations (0.8 M) is mediated by
CC       the protein phosphatase calcineurin, which is specifically activated by
CC       sodium ions. {ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:8612770}.
CC   -!- PTM: The active site is phosphorylated in presence of sodium or
CC       potassium and in conditions of higher pH (PubMed:9315618). Not
CC       phosphorylated in presence of calcium ions (PubMed:9315618).
CC       {ECO:0000269|PubMed:9315618}.
CC   -!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IID subfamily. {ECO:0000305}.
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DR   EMBL; U24069; AAA65600.1; -; Genomic_DNA.
DR   EMBL; Z54075; CAA90779.1; -; Genomic_DNA.
DR   EMBL; Z74336; CAA98867.1; -; Genomic_DNA.
DR   EMBL; X58626; CAA41479.1; -; Genomic_DNA.
DR   EMBL; J04186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK006938; DAA11888.1; -; Genomic_DNA.
DR   PIR; S05788; PWBYR2.
DR   RefSeq; NP_010325.1; NM_001180348.1.
DR   AlphaFoldDB; P13587; -.
DR   SMR; P13587; -.
DR   BioGRID; 32095; 93.
DR   DIP; DIP-4493N; -.
DR   IntAct; P13587; 1.
DR   STRING; 4932.YDR040C; -.
DR   TCDB; 3.A.3.9.1; the p-type atpase (p-atpase) superfamily.
DR   iPTMnet; P13587; -.
DR   MaxQB; P13587; -.
DR   PaxDb; 4932-YDR040C; -.
DR   PeptideAtlas; P13587; -.
DR   EnsemblFungi; YDR040C_mRNA; YDR040C; YDR040C.
DR   GeneID; 851610; -.
DR   KEGG; sce:YDR040C; -.
DR   AGR; SGD:S000002447; -.
DR   SGD; S000002447; ENA1.
DR   VEuPathDB; FungiDB:YDR040C; -.
DR   eggNOG; KOG0202; Eukaryota.
DR   GeneTree; ENSGT00940000176395; -.
DR   HOGENOM; CLU_002360_4_1_1; -.
DR   InParanoid; P13587; -.
DR   OMA; PVQKDCD; -.
DR   OrthoDB; 203629at2759; -.
DR   BioCyc; MetaCyc:G3O-29654-MONOMER; -.
DR   BioCyc; YEAST:G3O-29654-MONOMER; -.
DR   BRENDA; 7.2.2.3; 1113.
DR   BioGRID-ORCS; 851610; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P13587; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P13587; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0140679; F:ABC-type sodium transporter activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0008554; F:P-type sodium transporter activity; IDA:SGD.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR   GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR   GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0034220; P:monoatomic ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; IMP:SGD.
DR   GO; GO:0009268; P:response to pH; IGI:SGD.
DR   GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; IGI:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR   CDD; cd02086; P-type_ATPase_Na_ENA; 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; 2.
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; IPR006414; P-type_ATPase_IID.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01523; ATPase-IID_K-Na; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 3.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF14; SODIUM TRANSPORT ATPASE 1-RELATED; 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   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
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   ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Potassium; Potassium transport;
KW   Reference proteome; Sodium; Sodium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..1091
FT                   /note="Sodium/potassium exporting P-type ATPase 1"
FT                   /id="PRO_0000046242"
FT   TOPO_DOM        1..63
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        85..90
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..282
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        283..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        304..312
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        313..333
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        334..815
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        816..836
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        837..848
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        849..869
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        870..885
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        886..906
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        907..943
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        944..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        965..991
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        992..1012
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1013..1021
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1022..1042
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1043..1091
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          499..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        369
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         369
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         371
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         371
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         483
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         561
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         606
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         673
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         674
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         675
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         738
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         757
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
FT   BINDING         760
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P04191"
SQ   SEQUENCE   1091 AA;  120357 MW;  6480DBCD92B555E6 CRC64;
     MGEGTTKENN NAEFNAYHTL TAEEAAEFIG TSLTEGLTQD EFVHRLKTVG ENTLGDDTKI
     DYKAMVLHQV CNAMIMVLLI SMIISFAMHD WITGGVISFV IAVNVLIGLV QEYKATKTMN
     SLKNLSSPNA HVIRNGKSET INSKDVVPGD ICLVKVGDTI PADLRLIETK NFDTDESLLT
     GESLPVSKDA NLVFGKEEET SVGDRLNLAF SSSAVVKGRA KGIVIKTALN SEIGKIAKSL
     QGDSGLISRD PSKSWLQNTW ISTKKVTGAF LGTNVGTPLH RKLSKLAVLL FWIAVLFAII
     VMASQKFDVD KRVAIYAICV ALSMIPSSLV VVLTITMSVG AAVMVSRNVI VRKLDSLEAL
     GAVNDICSDK TGTLTQGKML ARQIWIPRFG TITISNSDDP FNPNEGNVSL IPRFSPYEYS
     HNEDGDVGIL QNFKDRLYEK DLPEDIDMDL FQKWLETATL ANIATVFKDD ATDCWKAHGD
     PTEIAIQVFA TKMDLPHNAL TGEKSTNQSN ENDQSSLSQH NEKPGSAQFE HIAEFPFDST
     VKRMSSVYYN NHNETYNIYG KGAFESIISC CSSWYGKDGV KITPLTDCDV ETIRKNVYSL
     SNEGLRVLGF ASKSFTKDQV NDDQLKNITS NRATAESDLV FLGLIGIYDP PRNETAGAVK
     KFHQAGINVH MLTGDFVGTA KAIAQEVGIL PTNLYHYSQE IVDSMVMTGS QFDGLSEEEV
     DDLPVLPLVI ARCSPQTKVR MIEALHRRKK FCTMTGDGVN DSPSLKMANV GIAMGINGSD
     VSKEASDIVL SDDNFASILN AVEEGRRMTD NIQKFVLQLL AENVAQALYL IIGLVFRDEN
     GKSVFPLSPV EVLWIIVVTS CFPAMGLGLE KAAPDLMDRP PHDSEVGIFT WEVIIDTFAY
     GIIMTGSCMA SFTGSLYGIN SGRLGHDCDG TYNSSCRDVY RSRSAAFATM TWCALILAWE
     VVDMRRSFFR MHPDTDSPVK EFFRSIWGNQ FLFWSIIFGF VSAFPVVYIP VINDKVFLHK
     PIGAEWGLAI AFTIAFWIGA ELYKCGKRRY FKTQRAHNPE NDLESNNKRD PFEAYSTSTT
     IHTEVNIGIK Q
//