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P19657 (PMA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 132. 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
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 2
EC=3.6.3.6
Alternative name(s):
Proton pump 2
Gene names
Name:PMA2
Ordered Locus Names:YPL036W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length947 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.

Miscellaneous

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

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 – 947947Plasma membrane ATPase 2
PRO_0000046272

Regions

Topological domain1 – 144144Cytoplasmic Potential
Transmembrane145 – 16521Helical; Name=1; Potential
Topological domain166 – 1694Extracellular Potential
Transmembrane170 – 18920Helical; Name=2; Potential
Topological domain190 – 320131Cytoplasmic Potential
Transmembrane321 – 34222Helical; Name=3; Potential
Topological domain343 – 35311Extracellular Potential
Transmembrane354 – 37623Helical; Name=4; Potential
Topological domain377 – 748372Cytoplasmic Potential
Transmembrane749 – 76719Helical; Name=5; Potential
Topological domain768 – 78316Extracellular Potential
Transmembrane784 – 80320Helical; Name=6; Potential
Topological domain804 – 85350Cytoplasmic Potential
Transmembrane854 – 87421Helical; Name=7; Potential
Topological domain875 – 88612Extracellular Potential
Transmembrane887 – 90317Helical; Name=8; Potential
Topological domain904 – 94744Cytoplasmic Potential
Compositional bias33 – 4715Poly-Ser
Compositional bias62 – 9130Asp/Glu-rich (acidic)

Sites

Active site40714-aspartylphosphate intermediate By similarity
Metal binding6631Magnesium By similarity
Metal binding6671Magnesium By similarity

Amino acid modifications

Modified residue5361Phosphoserine Ref.6
Modified residue9261Phosphothreonine Ref.6
Modified residue9411Phosphothreonine Ref.4 Ref.6

Experimental info

Sequence conflict9441E → D in AAA83387. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19657 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: 24CF0D3EAFD1E9D5

FASTA947102,172
        10         20         30         40         50         60 
MSSTEAKQYK EKPSKEYLHA SDGDDPANNS AASSSSSSST STSASSSAAA VPRKAAAASA 

        70         80         90        100        110        120 
ADDSDSDEDI DQLIDELQSN YGEGDESGEE EVRTDGVHAG QRVVPEKDLS TDPAYGLTSD 

       130        140        150        160        170        180 
EVARRRKKYG LNQMAEENES LIVKFLMFFV GPIQFVMEAA AILAAGLSDW VDVGVICALL 

       190        200        210        220        230        240 
LLNASVGFIQ EFQAGSIVDE LKKTLANTAT VIRDGQLIEI PANEVVPGEI LQLESGTIAP 

       250        260        270        280        290        300 
ADGRIVTEDC FLQIDQSAIT GESLAAEKHY GDEVFSSSTV KTGEAFMVVT ATGDNTFVGR 

       310        320        330        340        350        360 
AAALVGQASG VEGHFTEVLN GIGIILLVLV IATLLLVWTA CFYRTVGIVS ILRYTLGITI 

       370        380        390        400        410        420 
IGVPVGLPAV VTTTMAVGAA YLAKKQAIVQ KLSAIESLAG VEILCSDKTG TLTKNKLSLH 

       430        440        450        460        470        480 
EPYTVEGVSP DDLMLTACLA ASRKKKGLDA IDKAFLKSLI EYPKAKDALT KYKVLEFHPF 

       490        500        510        520        530        540 
DPVSKKVTAV VESPEGERIV CVKGAPLFVL KTVEEDHPIP EDVHENYENK VAELASRGFR 

       550        560        570        580        590        600 
ALGVARKRGE GHWEILGVMP CMDPPRDDTA QTINEARNLG LRIKMLTGDA VGIAKETCRQ 

       610        620        630        640        650        660 
LGLGTNIYNA ERLGLGGGGD MPGSELADFV ENADGFAEVF PQHKYRVVEI LQNRGYLVAM 

       670        680        690        700        710        720 
TGDGVNDAPS LKKADTGIAV EGATDAARSA ADIVFLAPGL SAIIDALKTS RQIFHRMYSY 

       730        740        750        760        770        780 
VVYRIALSLH LEIFLGLWIA ILNNSLDINL IVFIAIFADV ATLTIAYDNA PYAPEPVKWN 

       790        800        810        820        830        840 
LPRLWGMSII LGIVLAIGSW ITLTTMFLPN GGIIQNFGAM NGVMFLQISL TENWLIFVTR 

       850        860        870        880        890        900 
AAGPFWSSIP SWQLAGAVFA VDIIATMFTL FGWWSENWTD IVSVVRVWIW SIGIFCVLGG 

       910        920        930        940 
FYYIMSTSQA FDRLMNGKSL KEKKSTRSVE DFMAAMQRVS TQHEKSS

« Hide

References

« Hide 'large scale' references
[1]"A second transport ATPase gene in Saccharomyces cerevisiae."
Schlesser A., Ulaszewski S., Ghislain M., Goffeau A.
J. Biol. Chem. 263:19480-19487(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"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-941, MASS SPECTROMETRY.
Strain: 2124.
[5]"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.
[6]"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 SER-536; THR-926 AND THR-941, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04421 Genomic DNA. Translation: AAA83387.1.
U44030 Genomic DNA. Translation: AAB68184.1.
BK006949 Genomic DNA. Translation: DAA11394.1.
PIRPXBY2P. S62039.
RefSeqNP_015289.1. NM_001183850.1.

3D structure databases

ProteinModelPortalP19657.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4036N.
IntActP19657. 3 interactions.
MINTMINT-485284.
STRING4932.YPL036W.

Proteomic databases

PaxDbP19657.
PeptideAtlasP19657.
PRIDEP19657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL036W; YPL036W; YPL036W.
GeneID856071.
KEGGsce:YPL036W.

Organism-specific databases

CYGDYPL036w.
SGDS000005957. PMA2.

Phylogenomic databases

eggNOGCOG0474.
GeneTreeENSGT00550000075390.
HOGENOMHOG000160005.
KOK01535.
OMAFASELDY.
OrthoDBEOG47DDQ8.

Gene expression databases

GenevestigatorP19657.
GermOnlineYPL036W. Saccharomyces cerevisiae.

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]
PANTHERPTHR24093. PTHR24093. 1 hit.
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. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01647. ATPase-IIIA_H. 1 hit.
TIGR01494. ATPase_P-type. 3 hits.
PROSITEPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio981065.

Entry information

Entry namePMA2_YEAST
AccessionPrimary (citable) accession number: P19657
Secondary accession number(s): D6W3X8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: October 1, 1996
Last modified: May 1, 2013
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome XVI

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents