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P05030

- PMA1_YEAST

UniProt

P05030 - PMA1_YEAST

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Protein
Plasma membrane ATPase 1
Gene
PMA1, YGL008C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei378 – 37814-aspartylphosphate intermediate By similarity
Metal bindingi634 – 6341Magnesium By similarity
Metal bindingi638 – 6381Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hydrogen-exporting ATPase activity, phosphorylative mechanism Source: SGD
  3. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. ATP biosynthetic process Source: InterPro
  2. hydrogen ion transmembrane transport Source: GOC
  3. proteasome storage granule assembly Source: SGD
  4. proton transport Source: SGD
  5. regulation of pH Source: SGD
  6. transmembrane transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Prion

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30531-MONOMER.

Protein family/group databases

TCDBi3.A.3.3.6. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasma membrane ATPase 1 (EC:3.6.3.6)
Alternative name(s):
Proton pump 1
Gene namesi
Name:PMA1
Ordered Locus Names:YGL008C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGL008c.
SGDiS000002976. PMA1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 115115Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei116 – 13621Helical; Name=1; Reviewed prediction
Add
BLAST
Topological domaini137 – 1404Extracellular Reviewed prediction
Transmembranei141 – 16020Helical; Name=2; Reviewed prediction
Add
BLAST
Topological domaini161 – 291131Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei292 – 31322Helical; Name=3; Reviewed prediction
Add
BLAST
Topological domaini314 – 32512Extracellular Reviewed prediction
Add
BLAST
Transmembranei326 – 34722Helical; Name=4; Reviewed prediction
Add
BLAST
Topological domaini348 – 719372Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei720 – 73819Helical; Name=5; Reviewed prediction
Add
BLAST
Topological domaini739 – 75416Extracellular Reviewed prediction
Add
BLAST
Transmembranei755 – 77420Helical; Name=6; Reviewed prediction
Add
BLAST
Topological domaini775 – 82450Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei825 – 84521Helical; Name=7; Reviewed prediction
Add
BLAST
Topological domaini846 – 85712Extracellular Reviewed prediction
Add
BLAST
Transmembranei858 – 87417Helical; Name=8; Reviewed prediction
Add
BLAST
Topological domaini875 – 91844Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. membrane raft Source: SGD
  3. plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi129 – 1291E → L or Q: Normal activity. 1 Publication
Mutagenesisi200 – 2001D → N: Activity reduced to 23%. 1 Publication
Mutagenesisi233 – 2331E → Q: Activity reduced to 33%. 1 Publication
Mutagenesisi271 – 2711R → T: Normal activity. 1 Publication
Mutagenesisi335 – 3351P → A: Activity reduced to 53%. 1 Publication
Mutagenesisi378 – 3781D → E: Activity reduced to 67%. 1 Publication
Mutagenesisi378 – 3781D → N: Activity reduced to 73%. 1 Publication
Mutagenesisi378 – 3781D → T: Activity reduced to 49%. 1 Publication
Mutagenesisi474 – 4741K → Q: Activity reduced to 19%. 1 Publication
Mutagenesisi534 – 5341D → N: Activity reduced to 37%. 1 Publication
Mutagenesisi560 – 5601D → N: Activity reduced to 24%. 1 Publication
Mutagenesisi638 – 6381D → N: Activity reduced to 24%. 1 Publication
Mutagenesisi848 – 8481N → D: Normal activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 918918Plasma membrane ATPase 1
PRO_0000046271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphoserine1 Publication
Modified residuei175 – 1751Phosphothreonine1 Publication
Cross-linki555 – 555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki566 – 566Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki644 – 644Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei911 – 9111Phosphoserine2 Publications
Modified residuei912 – 9121Phosphothreonine2 Publications

Post-translational modificationi

Phosphorylated on multiple Ser and Thr residues.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05030.
PeptideAtlasiP05030.
PRIDEiP05030.

Expressioni

Gene expression databases

GenevestigatoriP05030.

Interactioni

Protein-protein interaction databases

BioGridi33238. 256 interactions.
DIPiDIP-2537N.
IntActiP05030. 6 interactions.
MINTiMINT-685556.
STRINGi4932.YGL008C.

Structurei

3D structure databases

ProteinModelPortaliP05030.
SMRiP05030. Positions 2-916.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 1713Poly-Ser
Add
BLAST
Compositional biasi31 – 7848Asp/Glu-rich (acidic)
Add
BLAST
Compositional biasi39 – 446Poly-Asp
Compositional biasi585 – 5906Poly-Gly

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00730000113900.
HOGENOMiHOG000160005.
KOiK01535.
OMAiFMVITAT.
OrthoDBiEOG789CKN.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProiIPR004014. 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]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view]
PRINTSiPR00119. CATATPASE.
PR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 2 hits.
TIGRFAMsiTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05030-1 [UniParc]FASTAAdd to Basket

« Hide

MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL    50
QSNHGVDDED SDNDGPVAAG EARPVPEEYL QTDPSYGLTS DEVLKRRKKY 100
GLNQMADEKE SLVVKFVMFF VGPIQFVMEA AAILAAGLSD WVDFGVICGL 150
LMLNAGVGFV QEFQAGSIVD ELKKTLANTA VVIRDGQLVE IPANEVVPGD 200
ILQLEDGTVI PTDGRIVTED CFLQIDQSAI TGESLAVDKH YGDQTFSSST 250
VKRGEGFMVV TATGDNTFVG RAAALVNKAA GGQGHFTEVL NGIGIILLVL 300
VIATLLLVWT ACFYRTNGIV RILRYTLGIT IIGVPVGLPA VVTTTMAVGA 350
AYLAKKQAIV QKLSAIESLA GVEILCSDKT GTLTKNKLSL HEPYTVEGVS 400
PDDLMLTACL AASRKKKGLD AIDKAFLKSL KQYPKAKDAL TKYKVLEFHP 450
FDPVSKKVTA VVESPEGERI VCVKGAPLFV LKTVEEDHPI PEDVHENYEN 500
KVAELASRGF RALGVARKRG EGHWEILGVM PCMDPPRDDT AQTVSEARHL 550
GLRVKMLTGD AVGIAKETCR QLGLGTNIYN AERLGLGGGG DMPGSELADF 600
VENADGFAEV FPQHKYRVVE ILQNRGYLVA MTGDGVNDAP SLKKADTGIA 650
VEGATDAARS AADIVFLAPG LSAIIDALKT SRQIFHRMYS YVVYRIALSL 700
HLEIFLGLWI AILDNSLDID LIVFIAIFAD VATLAIAYDN APYSPKPVKW 750
NLPRLWGMSI ILGIVLAIGS WITLTTMFLP KGGIIQNFGA MNGIMFLQIS 800
LTENWLIFIT RAAGPFWSSI PSWQLAGAVF AVDIIATMFT LFGWWSENWT 850
DIVTVVRVWI WSIGIFCVLG GFYYEMSTSE AFDRLMNGKP MKEKKSTRSV 900
EDFMAAMQRV STQHEKET 918
Length:918
Mass (Da):99,619
Last modified:November 1, 1995 - v2
Checksum:iAA1E93966B37E8E1
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03534 Genomic DNA. Translation: CAA27237.1.
Z72530 Genomic DNA. Translation: CAA96708.1.
BK006941 Genomic DNA. Translation: DAA08090.1.
PIRiS64010. PXBY1P.
RefSeqiNP_011507.1. NM_001180873.1.

Genome annotation databases

EnsemblFungiiYGL008C; YGL008C; YGL008C.
GeneIDi852876.
KEGGisce:YGL008C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03534 Genomic DNA. Translation: CAA27237.1 .
Z72530 Genomic DNA. Translation: CAA96708.1 .
BK006941 Genomic DNA. Translation: DAA08090.1 .
PIRi S64010. PXBY1P.
RefSeqi NP_011507.1. NM_001180873.1.

3D structure databases

ProteinModelPortali P05030.
SMRi P05030. Positions 2-916.
ModBasei Search...

Protein-protein interaction databases

BioGridi 33238. 256 interactions.
DIPi DIP-2537N.
IntActi P05030. 6 interactions.
MINTi MINT-685556.
STRINGi 4932.YGL008C.

Protein family/group databases

TCDBi 3.A.3.3.6. the p-type atpase (p-atpase) superfamily.

Proteomic databases

MaxQBi P05030.
PeptideAtlasi P05030.
PRIDEi P05030.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGL008C ; YGL008C ; YGL008C .
GeneIDi 852876.
KEGGi sce:YGL008C.

Organism-specific databases

CYGDi YGL008c.
SGDi S000002976. PMA1.

Phylogenomic databases

GeneTreei ENSGT00730000113900.
HOGENOMi HOG000160005.
KOi K01535.
OMAi FMVITAT.
OrthoDBi EOG789CKN.

Enzyme and pathway databases

BioCyci YEAST:G3O-30531-MONOMER.

Miscellaneous databases

NextBioi 972514.

Gene expression databases

Genevestigatori P05030.

Family and domain databases

Gene3Di 1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 2 hits.
InterProi 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 ]
Pfami PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF00702. Hydrolase. 1 hit.
[Graphical view ]
PRINTSi PR00119. CATATPASE.
PR00120. HATPASE.
SMARTi SM00831. Cation_ATPase_N. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 2 hits.
TIGRFAMsi TIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEi PS00154. ATPASE_E1_E2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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].

Entry informationi

Entry nameiPMA1_YEAST
AccessioniPrimary (citable) accession number: P05030
Secondary accession number(s): D6VUC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 (1 Publication).
There are two plasma membrane ATPases in yeast. This is the major isoform.
Present with 1260000 molecules/cell in log phase SD medium.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

External Data

Dasty 3

Similar proteinsi