Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P13587 (ATN1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium transport ATPase 1

EC=3.6.3.7
Gene names
Name:ENA1
Synonyms:HOR6, PMR2, PMR2A
Ordered Locus Names:YDR040C
ORF Names:YD6888.02C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1091 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.8

Catalytic activity

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

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.2 Ref.8 Ref.9.

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. Ref.2 Ref.7

Miscellaneous

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

Sequence similarities

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IID subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Nucleotide-binding
Sodium
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose starvation

Inferred from mutant phenotype PubMed 9383192. Source: SGD

hyperosmotic response

Inferred from genetic interaction Ref.7. Source: SGD

potassium ion transmembrane transport

Inferred from mutant phenotype PubMed 11932440. Source: GOC

potassium ion transport

Inferred from mutant phenotype PubMed 11932440. Source: SGD

response to pH

Inferred from genetic interaction PubMed 12453218. Source: SGD

response to salt stress

Inferred from direct assay Ref.7. Source: UniProtKB

sodium ion transmembrane transport

Inferred from direct assay Ref.8. Source: GOC

sodium ion transport

Inferred from genetic interaction PubMed 1657642. Source: SGD

transmembrane transport

Inferred from direct assay Ref.8. Source: SGD

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.8. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: InterPro

potassium-transporting ATPase activity

Inferred from mutant phenotype PubMed 11932440. Source: SGD

sodium-exporting ATPase activity, phosphorylative mechanism

Inferred from direct assay Ref.8. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10911091Sodium transport ATPase 1
PRO_0000046242

Regions

Topological domain1 – 6363Cytoplasmic Potential
Transmembrane64 – 8421Helical; Potential
Topological domain85 – 906Extracellular Potential
Transmembrane91 – 11121Helical; Potential
Topological domain112 – 282171Cytoplasmic Potential
Transmembrane283 – 30321Helical; Potential
Topological domain304 – 3129Extracellular Potential
Transmembrane313 – 33321Helical; Potential
Topological domain334 – 815482Cytoplasmic Potential
Transmembrane816 – 83621Helical; Potential
Topological domain837 – 84812Extracellular Potential
Transmembrane849 – 86921Helical; Potential
Topological domain870 – 88516Cytoplasmic Potential
Transmembrane886 – 90621Helical; Potential
Topological domain907 – 94337Extracellular Potential
Transmembrane944 – 96421Helical; Potential
Topological domain965 – 99127Cytoplasmic Potential
Transmembrane992 – 101221Helical; Potential
Topological domain1013 – 10219Extracellular Potential
Transmembrane1022 – 104221Helical; Potential
Topological domain1043 – 109149Cytoplasmic Potential

Sites

Active site36914-aspartylphosphate intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
P13587 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 6480DBCD92B555E6

FASTA1,091120,357
        10         20         30         40         50         60 
MGEGTTKENN NAEFNAYHTL TAEEAAEFIG TSLTEGLTQD EFVHRLKTVG ENTLGDDTKI 

        70         80         90        100        110        120 
DYKAMVLHQV CNAMIMVLLI SMIISFAMHD WITGGVISFV IAVNVLIGLV QEYKATKTMN 

       130        140        150        160        170        180 
SLKNLSSPNA HVIRNGKSET INSKDVVPGD ICLVKVGDTI PADLRLIETK NFDTDESLLT 

       190        200        210        220        230        240 
GESLPVSKDA NLVFGKEEET SVGDRLNLAF SSSAVVKGRA KGIVIKTALN SEIGKIAKSL 

       250        260        270        280        290        300 
QGDSGLISRD PSKSWLQNTW ISTKKVTGAF LGTNVGTPLH RKLSKLAVLL FWIAVLFAII 

       310        320        330        340        350        360 
VMASQKFDVD KRVAIYAICV ALSMIPSSLV VVLTITMSVG AAVMVSRNVI VRKLDSLEAL 

       370        380        390        400        410        420 
GAVNDICSDK TGTLTQGKML ARQIWIPRFG TITISNSDDP FNPNEGNVSL IPRFSPYEYS 

       430        440        450        460        470        480 
HNEDGDVGIL QNFKDRLYEK DLPEDIDMDL FQKWLETATL ANIATVFKDD ATDCWKAHGD 

       490        500        510        520        530        540 
PTEIAIQVFA TKMDLPHNAL TGEKSTNQSN ENDQSSLSQH NEKPGSAQFE HIAEFPFDST 

       550        560        570        580        590        600 
VKRMSSVYYN NHNETYNIYG KGAFESIISC CSSWYGKDGV KITPLTDCDV ETIRKNVYSL 

       610        620        630        640        650        660 
SNEGLRVLGF ASKSFTKDQV NDDQLKNITS NRATAESDLV FLGLIGIYDP PRNETAGAVK 

       670        680        690        700        710        720 
KFHQAGINVH MLTGDFVGTA KAIAQEVGIL PTNLYHYSQE IVDSMVMTGS QFDGLSEEEV 

       730        740        750        760        770        780 
DDLPVLPLVI ARCSPQTKVR MIEALHRRKK FCTMTGDGVN DSPSLKMANV GIAMGINGSD 

       790        800        810        820        830        840 
VSKEASDIVL SDDNFASILN AVEEGRRMTD NIQKFVLQLL AENVAQALYL IIGLVFRDEN 

       850        860        870        880        890        900 
GKSVFPLSPV EVLWIIVVTS CFPAMGLGLE KAAPDLMDRP PHDSEVGIFT WEVIIDTFAY 

       910        920        930        940        950        960 
GIIMTGSCMA SFTGSLYGIN SGRLGHDCDG TYNSSCRDVY RSRSAAFATM TWCALILAWE 

       970        980        990       1000       1010       1020 
VVDMRRSFFR MHPDTDSPVK EFFRSIWGNQ FLFWSIIFGF VSAFPVVYIP VINDKVFLHK 

      1030       1040       1050       1060       1070       1080 
PIGAEWGLAI AFTIAFWIGA ELYKCGKRRY FKTQRAHNPE NDLESNNKRD PFEAYSTSTT 

      1090 
IHTEVNIGIK Q 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRPWBYR2. S05788.
RefSeqNP_010325.1. NM_001180348.1.

3D structure databases

ProteinModelPortalP13587.
SMRP13587. Positions 16-1006.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32095. 35 interactions.
DIPDIP-4493N.
MINTMINT-524960.
STRING4932.YDR040C.

Protein family/group databases

TCDB3.A.3.9.1. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PeptideAtlasP13587.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR040C; YDR040C; YDR040C.
GeneID851610.
KEGGsce:YDR040C.

Organism-specific databases

CYGDYDR040c.
SGDS000002447. ENA1.

Phylogenomic databases

GeneTreeENSGT00560000076866.
HOGENOMHOG000265621.
OrthoDBEOG74BK1C.

Enzyme and pathway databases

BioCycYEAST:G3O-29654-MONOMER.

Gene expression databases

GenevestigatorP13587.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProIPR006068. 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]
PANTHERPTHR24093:SF105. PTHR24093:SF105. 1 hit.
PfamPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
SSF81660. SSF81660. 2 hits.
TIGRFAMsTIGR01523. ATPase-IID_K-Na. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969124.

Entry information

Entry nameATN1_YEAST
AccessionPrimary (citable) accession number: P13587
Secondary accession number(s): D6VS28
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families