Plasma membrane ATPase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P05030 (PMA1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 149. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Plasma membrane ATPase 1
EC=3.6.3.6

Alternative name(s):
Proton pump 1

Gene names

Name:	PMA1
Ordered Locus Names:	YGL008C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	918 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15). 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]

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Amyloid Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase Prion
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro regulation of pH Inferred from expression pattern PubMed 8929277. Source: SGD
Cellular_component	integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD membrane raft Inferred from direct assay PubMed 10716729 PubMed 15536122. Source: SGD mitochondrion Inferred from direct assay PubMed 16823961. Source: SGD plasma membrane Inferred from direct assay PubMed 11739806 PubMed 12469340 PubMed 16622836. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from direct assay PubMed 17912695. Source: SGD metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 918

918

Plasma membrane ATPase 1

PRO_0000046271

Regions

Topological domain

1 – 115

115

Cytoplasmic Potential

Transmembrane

116 – 136

Helical; Name=1; Potential

Topological domain

137 – 140

Extracellular Potential

Transmembrane

141 – 160

Helical; Name=2; Potential

Topological domain

161 – 291

131

Cytoplasmic Potential

Transmembrane

292 – 313

Helical; Name=3; Potential

Topological domain

314 – 325

Extracellular Potential

Transmembrane

326 – 347

Helical; Name=4; Potential

Topological domain

348 – 719

372

Cytoplasmic Potential

Transmembrane

720 – 738

Helical; Name=5; Potential

Topological domain

739 – 754

Extracellular Potential

Transmembrane

755 – 774

Helical; Name=6; Potential

Topological domain

775 – 824

Cytoplasmic Potential

Transmembrane

825 – 845

Helical; Name=7; Potential

Topological domain

846 – 857

Extracellular Potential

Transmembrane

858 – 874

Helical; Name=8; Potential

Topological domain

875 – 918

Cytoplasmic Potential

Compositional bias

5 – 17

Poly-Ser

Compositional bias

31 – 78

Asp/Glu-rich (acidic)

Compositional bias

39 – 44

Poly-Asp

Compositional bias

585 – 590

Poly-Gly

Sites

Active site

378

4-aspartylphosphate intermediate By similarity

Metal binding

634

Magnesium By similarity

Metal binding

638

Magnesium By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.14

Modified residue

Phosphoserine Ref.14

Modified residue

261

Phosphothreonine Ref.12

Modified residue

267

Phosphothreonine Ref.12

Modified residue

899

Phosphoserine Ref.11 Ref.12 Ref.14

Modified residue

911

Phosphoserine Ref.9 Ref.11 Ref.12

Modified residue

912

Phosphothreonine Ref.6 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14

Modified residue

918

Phosphothreonine Ref.11 Ref.14

Cross-link

555

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Cross-link

566

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Cross-link

644

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Experimental info

Mutagenesis

129

E → L or Q: Normal activity. Ref.5

Mutagenesis

200

D → N: Activity reduced to 23%. Ref.5

Mutagenesis

233

E → Q: Activity reduced to 33%. Ref.5

Mutagenesis

271

R → T: Normal activity. Ref.5

Mutagenesis

335

P → A: Activity reduced to 53%. Ref.5

Mutagenesis

378

D → E: Activity reduced to 67%. Ref.5

Mutagenesis

378

D → N: Activity reduced to 73%. Ref.5

Mutagenesis

378

D → T: Activity reduced to 49%. Ref.5

Mutagenesis

474

K → Q: Activity reduced to 19%. Ref.5

Mutagenesis

534

D → N: Activity reduced to 37%. Ref.5

Mutagenesis

560

D → N: Activity reduced to 24%. Ref.5

Mutagenesis

638

D → N: Activity reduced to 24%. Ref.5

Mutagenesis

848

N → D: Normal activity. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P05030 [UniParc].

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

FASTA

918

99,619

        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' referencesShow '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. Kleine K. Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[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]	"Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M. Nat. Biotechnol. 20:301-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-912, MASS SPECTROMETRY. Strain: 2124.
[7]	"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].
[8]	"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, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911 AND THR-912, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"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.
[11]	"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-899; SER-911; THR-912 AND THR-918, MASS SPECTROMETRY. Strain: ADR376.
[12]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-261; THR-267; SER-899; SER-911 AND THR-912, MASS SPECTROMETRY.
[13]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-912, MASS SPECTROMETRY.
[14]	"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-52; SER-61; SER-899; THR-912 AND THR-918, MASS SPECTROMETRY.
[15]	"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.
+	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.
PIR	PXBY1P. S64010.
RefSeq	NP_011507.1. NM_001180873.1.
3D structure databases
ProteinModelPortal	P05030.
SMR	P05030. Positions 2-916.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2537N.
IntAct	P05030. 7 interactions.
MINT	MINT-685556.
STRING	4932.YGL008C.
Protein family/group databases
TCDB	3.A.3.3.6. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PeptideAtlas	P05030.
PRIDE	P05030.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YGL008C; YGL008C; YGL008C.
GeneID	852876.
KEGG	sce:YGL008C.
Organism-specific databases
CYGD	YGL008c.
SGD	S000002976. PMA1.
Phylogenomic databases
GeneTree	ENSGT00550000075390.
HOGENOM	HOG000160005.
KO	K01535.
OMA	FGWWSQN.
OrthoDB	EOG4M68RQ.
Gene expression databases
ArrayExpress	P05030.
Genevestigator	P05030.
GermOnline	YGL008C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.1110.10. 2 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 2 hits.
InterPro	IPR004014. 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]
PANTHER	PTHR24093. PTHR24093. 1 hit.
Pfam	PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01647. ATPase-IIIA_H. 1 hit. TIGR01494. ATPase_P-type. 3 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	972514.

Entry information

Entry name

PMA1_YEAST

Accession

Primary (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:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome VII

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents