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P05030 (PMA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 158. 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:
Plasma membrane ATPase 1

EC=3.6.3.6
Alternative name(s):
Proton pump 1
Gene names
Name:PMA1
Ordered Locus Names:YGL008C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The plasma membrane ATPase of plants and fungi is a hydrogen ion pump. The proton gradient it generates drives the active transport of nutrients by H+-symport. The resulting external acidification and/or internal alkinization may mediate growth responses.

Catalytic activity

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

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Phosphorylated on multiple Ser and Thr residues.

Miscellaneous

The prion state [GAR+] is provoked by the interaction of the two proteins STD1 and PMA1. It involves a complex between a small fraction of the cellular complement of PMA1, and STD1, a much lower-abundance protein, and it is transmissible by non-Mendelian, cytoplasmic inheritance. [GAR+] makes cells resistant to the glucose-associated repression of alternative carbon sources. In contrast to other prion forms, [GAR+] cannot be cured by GdnHCl or by inactivation of the molecular chaperone HSP104 (Ref.11).

There are two plasma membrane ATPases in yeast. This is the major isoform.

Present with 1260000 molecules/cell in log phase SD medium.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Plasma membrane ATPase 1
PRO_0000046271

Regions

Topological domain1 – 115115Cytoplasmic Potential
Transmembrane116 – 13621Helical; Name=1; Potential
Topological domain137 – 1404Extracellular Potential
Transmembrane141 – 16020Helical; Name=2; Potential
Topological domain161 – 291131Cytoplasmic Potential
Transmembrane292 – 31322Helical; Name=3; Potential
Topological domain314 – 32512Extracellular Potential
Transmembrane326 – 34722Helical; Name=4; Potential
Topological domain348 – 719372Cytoplasmic Potential
Transmembrane720 – 73819Helical; Name=5; Potential
Topological domain739 – 75416Extracellular Potential
Transmembrane755 – 77420Helical; Name=6; Potential
Topological domain775 – 82450Cytoplasmic Potential
Transmembrane825 – 84521Helical; Name=7; Potential
Topological domain846 – 85712Extracellular Potential
Transmembrane858 – 87417Helical; Name=8; Potential
Topological domain875 – 91844Cytoplasmic Potential
Compositional bias5 – 1713Poly-Ser
Compositional bias31 – 7848Asp/Glu-rich (acidic)
Compositional bias39 – 446Poly-Asp
Compositional bias585 – 5906Poly-Gly

Sites

Active site37814-aspartylphosphate intermediate By similarity
Metal binding6341Magnesium By similarity
Metal binding6381Magnesium By similarity

Amino acid modifications

Modified residue611Phosphoserine Ref.10
Modified residue1751Phosphothreonine Ref.12
Modified residue9111Phosphoserine Ref.9 Ref.12
Modified residue9121Phosphothreonine Ref.9 Ref.12
Cross-link555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link566Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7
Cross-link644Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.7

Experimental info

Mutagenesis1291E → L or Q: Normal activity. Ref.5
Mutagenesis2001D → N: Activity reduced to 23%. Ref.5
Mutagenesis2331E → Q: Activity reduced to 33%. Ref.5
Mutagenesis2711R → T: Normal activity. Ref.5
Mutagenesis3351P → A: Activity reduced to 53%. Ref.5
Mutagenesis3781D → E: Activity reduced to 67%. Ref.5
Mutagenesis3781D → N: Activity reduced to 73%. Ref.5
Mutagenesis3781D → T: Activity reduced to 49%. Ref.5
Mutagenesis4741K → Q: Activity reduced to 19%. Ref.5
Mutagenesis5341D → N: Activity reduced to 37%. Ref.5
Mutagenesis5601D → N: Activity reduced to 24%. Ref.5
Mutagenesis6381D → N: Activity reduced to 24%. Ref.5
Mutagenesis8481N → D: Normal activity. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P05030 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: AA1E93966B37E8E1

FASTA91899,619
        10         20         30         40         50         60 
MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL QSNHGVDDED 

        70         80         90        100        110        120 
SDNDGPVAAG EARPVPEEYL QTDPSYGLTS DEVLKRRKKY GLNQMADEKE SLVVKFVMFF 

       130        140        150        160        170        180 
VGPIQFVMEA AAILAAGLSD WVDFGVICGL LMLNAGVGFV QEFQAGSIVD ELKKTLANTA 

       190        200        210        220        230        240 
VVIRDGQLVE IPANEVVPGD ILQLEDGTVI PTDGRIVTED CFLQIDQSAI TGESLAVDKH 

       250        260        270        280        290        300 
YGDQTFSSST VKRGEGFMVV TATGDNTFVG RAAALVNKAA GGQGHFTEVL NGIGIILLVL 

       310        320        330        340        350        360 
VIATLLLVWT ACFYRTNGIV RILRYTLGIT IIGVPVGLPA VVTTTMAVGA AYLAKKQAIV 

       370        380        390        400        410        420 
QKLSAIESLA GVEILCSDKT GTLTKNKLSL HEPYTVEGVS PDDLMLTACL AASRKKKGLD 

       430        440        450        460        470        480 
AIDKAFLKSL KQYPKAKDAL TKYKVLEFHP FDPVSKKVTA VVESPEGERI VCVKGAPLFV 

       490        500        510        520        530        540 
LKTVEEDHPI PEDVHENYEN KVAELASRGF RALGVARKRG EGHWEILGVM PCMDPPRDDT 

       550        560        570        580        590        600 
AQTVSEARHL GLRVKMLTGD AVGIAKETCR QLGLGTNIYN AERLGLGGGG DMPGSELADF 

       610        620        630        640        650        660 
VENADGFAEV FPQHKYRVVE ILQNRGYLVA MTGDGVNDAP SLKKADTGIA VEGATDAARS 

       670        680        690        700        710        720 
AADIVFLAPG LSAIIDALKT SRQIFHRMYS YVVYRIALSL HLEIFLGLWI AILDNSLDID 

       730        740        750        760        770        780 
LIVFIAIFAD VATLAIAYDN APYSPKPVKW NLPRLWGMSI ILGIVLAIGS WITLTTMFLP 

       790        800        810        820        830        840 
KGGIIQNFGA MNGIMFLQIS LTENWLIFIT RAAGPFWSSI PSWQLAGAVF AVDIIATMFT 

       850        860        870        880        890        900 
LFGWWSENWT DIVTVVRVWI WSIGIFCVLG GFYYEMSTSE AFDRLMNGKP MKEKKSTRSV 

       910 
EDFMAAMQRV STQHEKET 

« Hide

References

« Hide 'large scale' references
[1]"Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases."
Serrano R., Kielland-Brandt M.C., Fink G.R.
Nature 319:689-693(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. expand/collapse author list , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"The ATP binding site of the yeast plasma membrane proton-translocating ATPase."
Davis C.B., Smith K.E., Campbell B.N. Jr., Hammes G.G.
J. Biol. Chem. 265:1300-1305(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 556-566.
[5]"Dissection of functional domains of the yeast proton-pumping ATPase by directed mutagenesis."
Portillo F., Serrano R.
EMBO J. 7:1793-1798(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF GLU-129; ASP-200; GLU-233; ARG-271; PRO-335; ASP-378; LYS-474; ASP-534; ASP-560; ASP-638 AND ASN-848.
[6]"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].
[7]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-555; LYS-566 AND LYS-644.
[8]"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.
[9]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"A heritable switch in carbon source utilization driven by an unusual yeast prion."
Brown J.C., Lindquist S.
Genes Dev. 23:2320-2332(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PRION IDENTIFICATION, INTERACTION WITH STD1.
[12]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-175; SER-911 AND THR-912, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03534 Genomic DNA. Translation: CAA27237.1.
Z72530 Genomic DNA. Translation: CAA96708.1.
BK006941 Genomic DNA. Translation: DAA08090.1.
PIRPXBY1P. S64010.
RefSeqNP_011507.1. NM_001180873.1.

3D structure databases

ProteinModelPortalP05030.
SMRP05030. Positions 2-916.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33238. 255 interactions.
DIPDIP-2537N.
IntActP05030. 6 interactions.
MINTMINT-685556.
STRING4932.YGL008C.

Protein family/group databases

TCDB3.A.3.3.6. the p-type atpase (p-atpase) superfamily.

Proteomic databases

PeptideAtlasP05030.
PRIDEP05030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYGL008C; YGL008C; YGL008C.
GeneID852876.
KEGGsce:YGL008C.

Organism-specific databases

CYGDYGL008c.
SGDS000002976. PMA1.

Phylogenomic databases

GeneTreeENSGT00730000113900.
HOGENOMHOG000160005.
KOK01535.
OMADQTFSSS.
OrthoDBEOG789CKN.

Enzyme and pathway databases

BioCycYEAST:G3O-30531-MONOMER.

Gene expression databases

GenevestigatorP05030.

Family and domain databases

Gene3D1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProIPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
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.
IPR006534. H+_ATPase_P-typ_IIIA.
IPR023214. HAD-like_dom.
[Graphical view]
PfamPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSPR00119. CATATPASE.
PR00120. HATPASE.
SMARTSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 2 hits.
TIGRFAMsTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio972514.

Entry information

Entry namePMA1_YEAST
AccessionPrimary (citable) accession number: P05030
Secondary accession number(s): D6VUC9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1995
Last modified: April 16, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome VII

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

Yeast

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

SIMILARITY comments

Index of protein domains and families