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Identification
NameSodium transport ATPase 1
SynonymsNot Available
Gene NameENA1
Enzyme Class
Biological Properties
General FunctionInvolved in nucleotide binding
Specific FunctionThis 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
Cellular LocationCell membrane; Multi-pass membrane protein
SMPDB PathwaysNot Available
KEGG PathwaysNot Available
SMPDB ReactionsNot Available
KEGG ReactionsNot Available
Metabolites
YMDB IDNameView
YMDB00020SodiumShow
YMDB00109Adenosine triphosphateShow
YMDB00890waterShow
YMDB00907phosphateShow
YMDB00914ADPShow
GO Classification
Component
cell part
membrane
membrane part
intrinsic to membrane
integral to membrane
Function
hydrolase activity
substrate-specific transmembrane transporter activity
ion transmembrane transporter activity
ATPase activity, coupled to transmembrane movement of ions
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
hydrolase activity, acting on acid anhydrides
binding
hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
transporter activity
transmembrane transporter activity
Process
cellular nitrogen compound metabolic process
transport
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleoside phosphate metabolic process
ion transport
nucleotide metabolic process
purine nucleotide metabolic process
purine nucleotide biosynthetic process
cation transport
metabolic process
purine nucleoside triphosphate biosynthetic process
purine ribonucleoside triphosphate biosynthetic process
ATP biosynthetic process
nitrogen compound metabolic process
establishment of localization
Gene Properties
Chromosome Locationchromosome 4
LocusYDR040C
Gene Sequence>3276 bp ATGGGCGAAGGAACTACTAAGGAAAACAATAATGCAGAATTCAATGCTTATCACACGCTG ACTGCAGAAGAAGCCGCTGAATTCATAGGCACAAGTCTAACTGAAGGTTTGACCCAAGAT GAGTTCGTCCACAGATTGAAAACAGTGGGTGAGAACACATTGGGTGATGACACTAAAATT GATTACAAGGCAATGGTCCTCCATCAGGTATGTAATGCCATGATCATGGTCCTTCTAATA TCCATGATAATCTCGTTTGCCATGCATGATTGGATTACTGGTGGCGTTATTTCTTTTGTT ATCGCGGTCAATGTGCTCATTGGCCTAGTTCAAGAATATAAGGCTACCAAGACAATGAAC TCTTTGAAAAACTTGAGCTCTCCCAATGCTCATGTTATTAGGAACGGGAAAAGTGAGACT ATAAACTCAAAAGATGTGGTTCCAGGTGATATTTGTCTGGTGAAGGTCGGTGATACTATT CCTGCTGATTTGCGTTTAATTGAAACTAAGAATTTTGATACTGATGAATCACTACTGACC GGTGAATCTTTGCCTGTCTCCAAAGACGCCAACTTAGTGTTTGGAAAAGAAGAAGAAACC TCCGTGGGTGATCGTTTGAATTTAGCATTTTCTTCATCCGCCGTTGTCAAGGGAAGAGCC AAGGGTATTGTCATCAAGACAGCTTTGAATAGTGAAATTGGTAAAATTGCAAAATCTCTA CAAGGTGATTCAGGTCTCATTTCCCGCGATCCTAGTAAGTCGTGGTTACAGAATACATGG ATATCTACAAAGAAAGTTACTGGTGCATTTTTAGGTACAAATGTCGGTACGCCCCTGCAC AGGAAACTGTCTAAGTTGGCGGTATTGCTTTTCTGGATTGCCGTACTTTTTGCTATCATC GTCATGGCCTCTCAAAAGTTTGACGTAGATAAAAGGGTAGCTATCTATGCCATTTGTGTG GCCCTATCCATGATTCCCTCTTCATTAGTCGTTGTCTTGACCATCACCATGTCTGTTGGG GCTGCTGTTATGGTTTCTAGAAACGTTATTGTAAGAAAATTAGATTCTCTGGAAGCTTTA GGTGCCGTTAACGATATCTGTTCTGACAAGACCGGTACTCTTACACAGGGTAAAATGTTA GCGAGGCAAATTTGGATCCCTCGCTTTGGTACCATAACTATCTCGAATTCTGATGACCCC TTTAATCCCAATGAGGGCAACGTGAGTTTGATTCCAAGGTTTTCACCTTACGAATATTCT CATAATGAGGATGGTGACGTTGGTATTCTCCAGAATTTCAAGGATCGCCTATACGAAAAA GATTTACCAGAAGATATTGACATGGATCTATTTCAAAAATGGCTCGAAACCGCCACTTTG GCTAACATTGCTACTGTTTTCAAAGATGACGCAACTGACTGTTGGAAAGCTCATGGTGAC CCAACAGAAATTGCGATTCAAGTGTTTGCTACTAAGATGGACTTGCCTCACAATGCCCTT ACCGGTGAGAAATCGACTAATCAAAGTAATGAGAATGACCAATCCTCTCTTTCACAACAC AATGAGAAGCCTGGCAGTGCACAATTCGAACATATTGCTGAATTCCCATTCGACTCAACT GTGAAGCGAATGTCATCTGTCTACTACAACAATCACAACGAAACATATAATATTTATGGC AAGGGTGCTTTCGAAAGCATCATCAGTTGTTGCAGTTCTTGGTATGGTAAGGATGGTGTA AAAATCACACCATTGACCGATTGTGATGTCGAAACGATAAGGAAAAATGTTTACAGTCTA TCAAATGAGGGTTTAAGAGTCTTGGGTTTTGCCTCCAAATCTTTCACTAAAGATCAAGTG AATGACGATCAATTGAAAAACATTACTTCAAACAGGGCCACCGCAGAAAGTGATTTAGTT TTCCTAGGGTTGATTGGTATTTACGATCCACCCAGAAATGAGACTGCCGGTGCAGTCAAG AAGTTTCACCAAGCTGGTATTAACGTTCATATGTTAACTGGGGACTTTGTGGGTACAGCA AAGGCTATCGCTCAGGAGGTTGGCATCTTACCCACCAATTTGTACCATTACTCCCAAGAG ATTGTTGACAGTATGGTCATGACCGGATCTCAGTTTGACGGACTAAGTGAGGAGGAAGTG GACGATTTGCCCGTCTTACCTTTAGTTATTGCACGTTGCTCTCCGCAGACTAAGGTGAGA ATGATCGAAGCTTTACACCGTAGGAAGAAGTTCTGCACAATGACAGGTGACGGTGTTAAC GATTCTCCATCTCTAAAAATGGCCAATGTTGGTATTGCAATGGGTATTAATGGTTCAGAT GTTTCCAAAGAAGCGTCTGATATTGTTCTAAGCGATGACAATTTTGCTTCTATTTTGAAT GCTGTCGAAGAAGGTCGTAGGATGACGGATAACATTCAGAAGTTTGTCCTACAATTATTG GCAGAAAATGTTGCTCAGGCTTTGTATTTGATCATTGGTTTAGTATTCAGAGATGAGAAC GGAAAATCAGTATTTCCCTTATCACCAGTGGAAGTATTGTGGATTATTGTCGTCACCTCT TGTTTTCCTGCTATGGGGCTAGGTCTAGAAAAGGCTGCTCCAGATTTGATGGATAGACCT CCTCATGATTCAGAGGTTGGTATTTTCACGTGGGAGGTTATTATAGATACATTTGCATAT GGGATTATAATGACAGGGTCCTGTATGGCTTCATTTACTGGATCACTGTATGGAATAAAT AGTGGTAGATTGGGGCACGATTGTGATGGCACCTATAACAGCAGTTGTCGTGATGTTTAT AGATCACGTTCTGCGGCTTTCGCAACCATGACGTGGTGCGCTTTGATTCTGGCTTGGGAA GTGGTTGACATGAGAAGATCCTTTTTCAGAATGCATCCAGACACTGACAGCCCAGTCAAG GAATTTTTCAGAAGCATTTGGGGAAACCAGTTTTTGTTCTGGTCAATCATTTTTGGATTT GTGTCAGCCTTCCCCGTCGTCTATATTCCGGTTATTAATGATAAAGTGTTTTTGCATAAA CCAATTGGTGCTGAATGGGGTCTCGCCATTGCATTCACAATTGCATTCTGGATAGGTGCT GAACTTTACAAGTGTGGAAAGAGGCGCTATTTCAAAACTCAGAGAGCGCACAACCCGGAG AATGATTTGGAGAGTAACAATAAGCGCGATCCATTCGAAGCGTATAGTACTTCTACTACA ATCCATACAGAAGTTAATATTGGTATTAAACAATGA
Protein Properties
Pfam Domain Function
Protein Residues1091
Protein Molecular Weight120356.0
Protein Theoretical pI5.24
Signalling Regions
  • None
Transmembrane Regions
  • 64-84
  • 91-111
  • 283-303
  • 313-333
  • 816-836
  • 849-869
  • 886-906
  • 944-964
  • 992-1012
  • 1022-1042
Protein Sequence>Sodium transport ATPase 1 MGEGTTKENNNAEFNAYHTLTAEEAAEFIGTSLTEGLTQDEFVHRLKTVGENTLGDDTKI DYKAMVLHQVCNAMIMVLLISMIISFAMHDWITGGVISFVIAVNVLIGLVQEYKATKTMN SLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLT GESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSL QGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAII VMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEAL GAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYS HNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGD PTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDST VKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSL SNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVK KFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEV DDLPVLPLVIARCSPQTKVRMIEALHRRKKFCTMTGDGVNDSPSLKMANVGIAMGINGSD VSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDEN GKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPHDSEVGIFTWEVIIDTFAY GIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWE VVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHK PIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNPENDLESNNKRDPFEAYSTSTT IHTEVNIGIKQ
References
External Links
ResourceLink
Saccharomyces Genome Database ENA1
Uniprot IDP13587
Uniprot NameATN1_YEAST
GenBank Gene IDU24069
Genebank Protein ID790261
General Reference
  • 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. (1989). "The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family." Cell 58:133-145.2526682
  • Wieland, J., Nitsche, A. M., Strayle, J., Steiner, H., Rudolph, H. K. (1995). "The PMR2 gene cluster encodes functionally distinct isoforms of a putative Na+ pump in the yeast plasma membrane." EMBO J 14:3870-3882.7664728
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, 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., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Martinez, R., Latreille, M. T., Mirande, M. (1991). "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 227:149-154.2046655
  • Mirande, M., Waller, J. P. (1988). "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 263:18443-18451.2903861
  • Marquez, J. A., Serrano, R. (1996). "Multiple transduction pathways regulate the sodium-extrusion gene PMR2/ENA1 during salt stress in yeast." FEBS Lett 382:89-92.8612770
  • Benito, B., Quintero, F. J., Rodriguez-Navarro, A. (1997). "Overexpression of the sodium ATPase of Saccharomyces cerevisiae: conditions for phosphorylation from ATP and Pi." Biochim Biophys Acta 1328:214-226.9315618
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Kim, H., Melen, K., Osterberg, M., von Heijne, G. (2006). "A global topology map of the Saccharomyces cerevisiae membrane proteome." Proc Natl Acad Sci U S A 103:11142-11147.16847258
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358