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P13587

- ATN1_YEAST

UniProt

P13587 - ATN1_YEAST

Protein

Sodium transport ATPase 1

Gene

ENA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    Functioni

    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/HAL3.2 Publications

    Catalytic activityi

    ATP + H2O + Na+(In) = ADP + phosphate + Na+(Out).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei369 – 36914-aspartylphosphate intermediateBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: InterPro
    3. potassium-transporting ATPase activity Source: SGD
    4. sodium-exporting ATPase activity, phosphorylative mechanism Source: SGD

    GO - Biological processi

    1. cellular response to glucose starvation Source: SGD
    2. hyperosmotic response Source: SGD
    3. potassium ion transmembrane transport Source: GOC
    4. potassium ion transport Source: SGD
    5. response to pH Source: SGD
    6. response to salt stress Source: UniProtKB
    7. sodium ion transmembrane transport Source: GOC
    8. sodium ion transport Source: SGD
    9. transmembrane transport Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    ATP-binding, Magnesium, Nucleotide-binding, Sodium

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29654-MONOMER.

    Protein family/group databases

    TCDBi3.A.3.9.1. the p-type atpase (p-atpase) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sodium transport ATPase 1 (EC:3.6.3.7)
    Gene namesi
    Name:ENA1
    Synonyms:HOR6, PMR2, PMR2A
    Ordered Locus Names:YDR040C
    ORF Names:YD6888.02C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR040c.
    SGDiS000002447. ENA1.

    Subcellular locationi

    Cell membrane 3 Publications; Multi-pass membrane protein 3 Publications

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10911091Sodium transport ATPase 1PRO_0000046242Add
    BLAST

    Proteomic databases

    MaxQBiP13587.
    PeptideAtlasiP13587.

    Expressioni

    Inductioni

    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.2 Publications

    Gene expression databases

    GenevestigatoriP13587.

    Interactioni

    Protein-protein interaction databases

    BioGridi32095. 35 interactions.
    DIPiDIP-4493N.
    MINTiMINT-524960.
    STRINGi4932.YDR040C.

    Structurei

    3D structure databases

    ProteinModelPortaliP13587.
    SMRiP13587. Positions 16-1006.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6363CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini85 – 906ExtracellularSequence Analysis
    Topological domaini112 – 282171CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini304 – 3129ExtracellularSequence Analysis
    Topological domaini334 – 815482CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini837 – 84812ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini870 – 88516CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini907 – 94337ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini965 – 99127CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1013 – 10219ExtracellularSequence Analysis
    Topological domaini1043 – 109149CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei64 – 8421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei91 – 11121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei283 – 30321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei313 – 33321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei816 – 83621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei849 – 86921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei886 – 90621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei944 – 96421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei992 – 101221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei1022 – 104221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    GeneTreeiENSGT00560000076866.
    HOGENOMiHOG000265621.
    OMAiYENESCE.
    OrthoDBiEOG74BK1C.

    Family and domain databases

    Gene3Di1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 2 hits.
    InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR006414. ATPase_P-typ_Na/Ca.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view]
    PfamiPF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view]
    PRINTSiPR00119. CATATPASE.
    SMARTiSM00831. Cation_ATPase_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 2 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsiTIGR01523. ATPase-IID_K-Na. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P13587-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGEGTTKENN NAEFNAYHTL TAEEAAEFIG TSLTEGLTQD EFVHRLKTVG     50
    ENTLGDDTKI DYKAMVLHQV CNAMIMVLLI SMIISFAMHD WITGGVISFV 100
    IAVNVLIGLV QEYKATKTMN SLKNLSSPNA HVIRNGKSET INSKDVVPGD 150
    ICLVKVGDTI PADLRLIETK NFDTDESLLT GESLPVSKDA NLVFGKEEET 200
    SVGDRLNLAF SSSAVVKGRA KGIVIKTALN SEIGKIAKSL QGDSGLISRD 250
    PSKSWLQNTW ISTKKVTGAF LGTNVGTPLH RKLSKLAVLL FWIAVLFAII 300
    VMASQKFDVD KRVAIYAICV ALSMIPSSLV VVLTITMSVG AAVMVSRNVI 350
    VRKLDSLEAL GAVNDICSDK TGTLTQGKML ARQIWIPRFG TITISNSDDP 400
    FNPNEGNVSL IPRFSPYEYS HNEDGDVGIL QNFKDRLYEK DLPEDIDMDL 450
    FQKWLETATL ANIATVFKDD ATDCWKAHGD PTEIAIQVFA TKMDLPHNAL 500
    TGEKSTNQSN ENDQSSLSQH NEKPGSAQFE HIAEFPFDST VKRMSSVYYN 550
    NHNETYNIYG KGAFESIISC CSSWYGKDGV KITPLTDCDV ETIRKNVYSL 600
    SNEGLRVLGF ASKSFTKDQV NDDQLKNITS NRATAESDLV FLGLIGIYDP 650
    PRNETAGAVK KFHQAGINVH MLTGDFVGTA KAIAQEVGIL PTNLYHYSQE 700
    IVDSMVMTGS QFDGLSEEEV DDLPVLPLVI ARCSPQTKVR MIEALHRRKK 750
    FCTMTGDGVN DSPSLKMANV GIAMGINGSD VSKEASDIVL SDDNFASILN 800
    AVEEGRRMTD NIQKFVLQLL AENVAQALYL IIGLVFRDEN GKSVFPLSPV 850
    EVLWIIVVTS CFPAMGLGLE KAAPDLMDRP PHDSEVGIFT WEVIIDTFAY 900
    GIIMTGSCMA SFTGSLYGIN SGRLGHDCDG TYNSSCRDVY RSRSAAFATM 950
    TWCALILAWE VVDMRRSFFR MHPDTDSPVK EFFRSIWGNQ FLFWSIIFGF 1000
    VSAFPVVYIP VINDKVFLHK PIGAEWGLAI AFTIAFWIGA ELYKCGKRRY 1050
    FKTQRAHNPE NDLESNNKRD PFEAYSTSTT IHTEVNIGIK Q 1091
    Length:1,091
    Mass (Da):120,357
    Last modified:January 1, 1990 - v1
    Checksum:i6480DBCD92B555E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24069 Genomic DNA. Translation: AAA65600.1.
    Z54075 Genomic DNA. Translation: CAA90779.1.
    Z74336 Genomic DNA. Translation: CAA98867.1.
    X58626 Genomic DNA. Translation: CAA41479.1.
    J04186 Genomic DNA. No translation available.
    BK006938 Genomic DNA. Translation: DAA11888.1.
    PIRiS05788. PWBYR2.
    RefSeqiNP_010325.1. NM_001180348.1.

    Genome annotation databases

    EnsemblFungiiYDR040C; YDR040C; YDR040C.
    GeneIDi851610.
    KEGGisce:YDR040C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U24069 Genomic DNA. Translation: AAA65600.1 .
    Z54075 Genomic DNA. Translation: CAA90779.1 .
    Z74336 Genomic DNA. Translation: CAA98867.1 .
    X58626 Genomic DNA. Translation: CAA41479.1 .
    J04186 Genomic DNA. No translation available.
    BK006938 Genomic DNA. Translation: DAA11888.1 .
    PIRi S05788. PWBYR2.
    RefSeqi NP_010325.1. NM_001180348.1.

    3D structure databases

    ProteinModelPortali P13587.
    SMRi P13587. Positions 16-1006.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32095. 35 interactions.
    DIPi DIP-4493N.
    MINTi MINT-524960.
    STRINGi 4932.YDR040C.

    Protein family/group databases

    TCDBi 3.A.3.9.1. the p-type atpase (p-atpase) superfamily.

    Proteomic databases

    MaxQBi P13587.
    PeptideAtlasi P13587.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR040C ; YDR040C ; YDR040C .
    GeneIDi 851610.
    KEGGi sce:YDR040C.

    Organism-specific databases

    CYGDi YDR040c.
    SGDi S000002447. ENA1.

    Phylogenomic databases

    GeneTreei ENSGT00560000076866.
    HOGENOMi HOG000265621.
    OMAi YENESCE.
    OrthoDBi EOG74BK1C.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29654-MONOMER.

    Miscellaneous databases

    NextBioi 969124.

    Gene expression databases

    Genevestigatori P13587.

    Family and domain databases

    Gene3Di 1.20.1110.10. 2 hits.
    2.70.150.10. 2 hits.
    3.40.1110.10. 2 hits.
    InterProi IPR006068. ATPase_P-typ_cation-transptr_C.
    IPR004014. ATPase_P-typ_cation-transptr_N.
    IPR023299. ATPase_P-typ_cyto_domN.
    IPR006414. ATPase_P-typ_Na/Ca.
    IPR018303. ATPase_P-typ_P_site.
    IPR023298. ATPase_P-typ_TM_dom.
    IPR008250. ATPase_P-typ_transduc_dom_A.
    IPR001757. Cation_transp_P_typ_ATPase.
    IPR023214. HAD-like_dom.
    [Graphical view ]
    Pfami PF00689. Cation_ATPase_C. 1 hit.
    PF00690. Cation_ATPase_N. 1 hit.
    PF00122. E1-E2_ATPase. 1 hit.
    PF00702. Hydrolase. 1 hit.
    [Graphical view ]
    PRINTSi PR00119. CATATPASE.
    SMARTi SM00831. Cation_ATPase_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56784. SSF56784. 2 hits.
    SSF81660. SSF81660. 2 hits.
    TIGRFAMsi TIGR01523. ATPase-IID_K-Na. 1 hit.
    TIGR01494. ATPase_P-type. 3 hits.
    PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family."
      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.
      Cell 58:133-145(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane."
      Wieland J., Nitsche A.M., Strayle J., Steiner H., Rudolph H.K.
      EMBO J. 14:3870-3882(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      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.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "A PMR2 tandem repeat with a modified C-terminus is located downstream from the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces cerevisiae."
      Martinez R., Latreille M.-T., Mirande M.
      Mol. Gen. Genet. 227:149-154(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 534-1091.
      Strain: 7305B.
    6. "The yeast lysyl-tRNA synthetase gene. Evidence for general amino acid control of its expression and domain structure of the encoded protein."
      Mirande M., Waller J.-P.
      J. Biol. Chem. 263:18443-18451(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 534-1091.
      Strain: ATCC 26109 / X2180.
    7. "Multiple transduction pathways regulate the sodium-extrusion gene PMR2/ENA1 during salt stress in yeast."
      Marquez J.A., Serrano R.
      FEBS Lett. 382:89-92(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Overexpression of the sodium ATPase of Saccharomyces cerevisiae: conditions for phosphorylation from ATP and Pi."
      Benito B., Quintero F.J., Rodriguez-Navarro A.
      Biochim. Biophys. Acta 1328:214-226(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    10. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    11. "A global topology map of the Saccharomyces cerevisiae membrane proteome."
      Kim H., Melen K., Oesterberg M., von Heijne G.
      Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
      Strain: ATCC 208353 / W303-1A.

    Entry informationi

    Entry nameiATN1_YEAST
    AccessioniPrimary (citable) accession number: P13587
    Secondary accession number(s): D6VS28
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 688 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3