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Sodium transport ATPase 1 (EC 3.6.3.7)

 ATN1_YEAST              Reviewed;        1091 AA.
P13587; D6VS28;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
20-JUN-2018, entry version 187.
RecName: Full=Sodium transport ATPase 1;
EC=3.6.3.7;
Name=ENA1; Synonyms=HOR6, PMR2, PMR2A; OrderedLocusNames=YDR040C;
ORFNames=YD6888.02C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2526682; DOI=10.1016/0092-8674(89)90410-8;
Rudolph H.K., Antebi A., Fink G.R., Buckley C.M., Dorman T.E.,
Levitre J., Davidow L.S., Mao J.-I., Moir D.T.;
"The yeast secretory pathway is perturbed by mutations in PMR1, a
member of a Ca2+ ATPase family.";
Cell 58:133-145(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=7664728;
Wieland J., Nitsche A.M., Strayle J., Steiner H., Rudolph H.K.;
"The PMR2 gene cluster encodes functionally distinct isoforms of a
putative Na+ pump in the yeast plasma membrane.";
EMBO J. 14:3870-3882(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 534-1091.
STRAIN=7305B;
PubMed=2046655; DOI=10.1007/BF00260720;
Martinez R., Latreille M.-T., Mirande M.;
"A PMR2 tandem repeat with a modified C-terminus is located downstream
from the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces
cerevisiae.";
Mol. Gen. Genet. 227:149-154(1991).
[6]
PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 534-1091.
STRAIN=ATCC 26109 / X2180;
PubMed=2903861;
Mirande M., Waller J.-P.;
"The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid
control of its expression and domain structure of the encoded
protein.";
J. Biol. Chem. 263:18443-18451(1988).
[7]
INDUCTION.
PubMed=8612770; DOI=10.1016/0014-5793(96)00157-3;
Marquez J.A., Serrano R.;
"Multiple transduction pathways regulate the sodium-extrusion gene
PMR2/ENA1 during salt stress in yeast.";
FEBS Lett. 382:89-92(1996).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9315618; DOI=10.1016/S0005-2736(97)00098-9;
Benito B., Quintero F.J., Rodriguez-Navarro A.;
"Overexpression of the sodium ATPase of Saccharomyces cerevisiae:
conditions for phosphorylation from ATP and Pi.";
Biochim. Biophys. Acta 1328:214-226(1997).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
-!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
of ATP coupled with the transport of the sodium or lithium ions to
allow salt tolerance. Is negatively modulated by SIS2/HAL3.
{ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Na(+)(In) = ADP + phosphate +
Na(+)(Out).
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}; Multi-
pass membrane protein {ECO:0000269|PubMed:14562095,
ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:9315618}.
-!- INDUCTION: By sodium ions. Induction at low salt concentrations
(0.3 M) is mediated by the high-osmolarity glycerol (HOG)-MAP
kinase pathway, a system activated by non-specific osmotic stress,
and by the protein kinase A pathway. At high salt concentrations
(0.8 M) is mediated by the protein phosphatase calcineurin, which
is specifically activated by sodium ions.
{ECO:0000269|PubMed:7664728, ECO:0000269|PubMed:8612770}.
-!- MISCELLANEOUS: Present with 688 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IID subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U24069; AAA65600.1; -; Genomic_DNA.
EMBL; Z54075; CAA90779.1; -; Genomic_DNA.
EMBL; Z74336; CAA98867.1; -; Genomic_DNA.
EMBL; X58626; CAA41479.1; -; Genomic_DNA.
EMBL; J04186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BK006938; DAA11888.1; -; Genomic_DNA.
PIR; S05788; PWBYR2.
RefSeq; NP_010325.1; NM_001180348.1.
ProteinModelPortal; P13587; -.
SMR; P13587; -.
BioGrid; 32095; 83.
DIP; DIP-4493N; -.
IntAct; P13587; 1.
STRING; 4932.YDR040C; -.
TCDB; 3.A.3.9.1; the p-type atpase (p-atpase) superfamily.
iPTMnet; P13587; -.
MaxQB; P13587; -.
PaxDb; P13587; -.
PRIDE; P13587; -.
EnsemblFungi; YDR040C; YDR040C; YDR040C.
GeneID; 851610; -.
KEGG; sce:YDR040C; -.
EuPathDB; FungiDB:YDR040C; -.
SGD; S000002447; ENA1.
GeneTree; ENSGT00910000144699; -.
HOGENOM; HOG000265621; -.
InParanoid; P13587; -.
KO; K01536; -.
OMA; WIIMATS; -.
OrthoDB; EOG092C0DMA; -.
BioCyc; YEAST:G3O-29654-MONOMER; -.
BRENDA; 3.6.3.7; 1113.
PRO; PR:P13587; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0008556; F:potassium-transporting ATPase activity; IMP:SGD.
GO; GO:0008554; F:sodium-exporting ATPase activity, phosphorylative mechanism; IDA:SGD.
GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
GO; GO:0006813; P:potassium ion transport; IMP:SGD.
GO; GO:0009268; P:response to pH; IGI:SGD.
GO; GO:0009651; P:response to salt stress; IDA:UniProtKB.
GO; GO:0006814; P:sodium ion transport; IGI:SGD.
GO; GO:0055085; P:transmembrane transport; IDA:SGD.
CDD; cd02086; P-type_ATPase_Na_ENA; 1.
Gene3D; 3.40.1110.10; -; 1.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR006414; P-type_ATPase_IID.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 2.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 2.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01523; ATPase-IID_K-Na; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 3.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
ATP-binding; Cell membrane; Complete proteome; Hydrolase;
Ion transport; Magnesium; Membrane; Nucleotide-binding;
Reference proteome; Sodium; Sodium transport; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 1091 Sodium transport ATPase 1.
/FTId=PRO_0000046242.
TOPO_DOM 1 63 Cytoplasmic. {ECO:0000255}.
TRANSMEM 64 84 Helical. {ECO:0000255}.
TOPO_DOM 85 90 Extracellular. {ECO:0000255}.
TRANSMEM 91 111 Helical. {ECO:0000255}.
TOPO_DOM 112 282 Cytoplasmic. {ECO:0000255}.
TRANSMEM 283 303 Helical. {ECO:0000255}.
TOPO_DOM 304 312 Extracellular. {ECO:0000255}.
TRANSMEM 313 333 Helical. {ECO:0000255}.
TOPO_DOM 334 815 Cytoplasmic. {ECO:0000255}.
TRANSMEM 816 836 Helical. {ECO:0000255}.
TOPO_DOM 837 848 Extracellular. {ECO:0000255}.
TRANSMEM 849 869 Helical. {ECO:0000255}.
TOPO_DOM 870 885 Cytoplasmic. {ECO:0000255}.
TRANSMEM 886 906 Helical. {ECO:0000255}.
TOPO_DOM 907 943 Extracellular. {ECO:0000255}.
TRANSMEM 944 964 Helical. {ECO:0000255}.
TOPO_DOM 965 991 Cytoplasmic. {ECO:0000255}.
TRANSMEM 992 1012 Helical. {ECO:0000255}.
TOPO_DOM 1013 1021 Extracellular. {ECO:0000255}.
TRANSMEM 1022 1042 Helical. {ECO:0000255}.
TOPO_DOM 1043 1091 Cytoplasmic. {ECO:0000255}.
ACT_SITE 369 369 4-aspartylphosphate intermediate.
{ECO:0000250}.
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


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