ATN1_YEAST
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 03-AUG-2022, entry version 213.
DE RecName: Full=Sodium transport ATPase 1;
DE EC=7.2.2.3 {ECO:0000269|PubMed:9315618};
GN Name=ENA1; Synonyms=HOR6, PMR2, PMR2A; OrderedLocusNames=YDR040C;
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, AND SUBCELLULAR LOCATION.
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 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 [11]
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).
CC -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis of
CC ATP coupled with the transport of the sodium or lithium ions to allow
CC salt tolerance. Is negatively modulated by SIS2/HAL3.
CC {ECO:0000269|PubMed:7664728, 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:0000269|PubMed:9315618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14634;
CC Evidence={ECO:0000269|PubMed:9315618};
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 -!- 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; 90.
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; P13587; -.
DR PRIDE; P13587; -.
DR EnsemblFungi; YDR040C_mRNA; YDR040C; YDR040C.
DR GeneID; 851610; -.
DR KEGG; sce:YDR040C; -.
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; YLNVAAM; -.
DR BioCyc; MetaCyc:G3O-29654-MON; -.
DR BioCyc; YEAST:G3O-29654-MON; -.
DR BRENDA; 7.2.2.3; 1113.
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:0016021; C:integral component of membrane; IBA:GO_Central.
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:0005388; F:P-type calcium transporter activity; IBA:GO_Central.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
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:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0042149; P:cellular response to glucose starvation; IMP:SGD.
DR GO; GO:0006972; P:hyperosmotic response; IGI:SGD.
DR GO; GO:0034220; P: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; -; 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; IPR006414; P-type_ATPase_IID.
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; TIGR01523; ATPase-IID_K-Na; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Ion transport; Magnesium; Membrane;
KW Nucleotide-binding; Reference proteome; Sodium; Sodium transport;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1091
FT /note="Sodium transport 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"
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
