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Protein

Plasma membrane ATPase 1

Gene

PMA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei3784-aspartylphosphate intermediateBy similarity1
Metal bindingi634MagnesiumBy similarity1
Metal bindingi638MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

  • ATP biosynthetic process Source: InterPro
  • proteasome storage granule assembly Source: SGD
  • proton transport Source: SGD
  • regulation of intracellular pH Source: GO_Central
  • regulation of pH Source: SGD
  • 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.
BRENDAi3.6.3.6. 984.

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
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL008C.
SGDiS000002976. PMA1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 115CytoplasmicSequence analysisAdd BLAST115
Transmembranei116 – 136Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini137 – 140ExtracellularSequence analysis4
Transmembranei141 – 160Helical; Name=2Sequence analysisAdd BLAST20
Topological domaini161 – 291CytoplasmicSequence analysisAdd BLAST131
Transmembranei292 – 313Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini314 – 325ExtracellularSequence analysisAdd BLAST12
Transmembranei326 – 347Helical; Name=4Sequence analysisAdd BLAST22
Topological domaini348 – 719CytoplasmicSequence analysisAdd BLAST372
Transmembranei720 – 738Helical; Name=5Sequence analysisAdd BLAST19
Topological domaini739 – 754ExtracellularSequence analysisAdd BLAST16
Transmembranei755 – 774Helical; Name=6Sequence analysisAdd BLAST20
Topological domaini775 – 824CytoplasmicSequence analysisAdd BLAST50
Transmembranei825 – 845Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini846 – 857ExtracellularSequence analysisAdd BLAST12
Transmembranei858 – 874Helical; Name=8Sequence analysisAdd BLAST17
Topological domaini875 – 918CytoplasmicSequence analysisAdd BLAST44

GO - Cellular componenti

  • integral component of plasma membrane Source: GO_Central
  • membrane raft Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Amyloid, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi129E → L or Q: Normal activity. 1 Publication1
Mutagenesisi200D → N: Activity reduced to 23%. 1 Publication1
Mutagenesisi233E → Q: Activity reduced to 33%. 1 Publication1
Mutagenesisi271R → T: Normal activity. 1 Publication1
Mutagenesisi335P → A: Activity reduced to 53%. 1 Publication1
Mutagenesisi378D → E: Activity reduced to 67%. 1 Publication1
Mutagenesisi378D → N: Activity reduced to 73%. 1 Publication1
Mutagenesisi378D → T: Activity reduced to 49%. 1 Publication1
Mutagenesisi474K → Q: Activity reduced to 19%. 1 Publication1
Mutagenesisi534D → N: Activity reduced to 37%. 1 Publication1
Mutagenesisi560D → N: Activity reduced to 24%. 1 Publication1
Mutagenesisi638D → N: Activity reduced to 24%. 1 Publication1
Mutagenesisi848N → D: Normal activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000462711 – 918Plasma membrane ATPase 1Add BLAST918

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei61PhosphoserineCombined sources1
Modified residuei175PhosphothreonineCombined sources1
Cross-linki252Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki555Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei911PhosphoserineCombined sources1
Modified residuei912PhosphothreonineCombined sources1
Modified residuei918PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated on multiple Ser and Thr residues.

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP05030.
PRIDEiP05030.

PTM databases

iPTMnetiP05030.

Interactioni

Protein-protein interaction databases

BioGridi33238. 265 interactors.
DIPiDIP-2537N.
IntActiP05030. 9 interactors.
MINTiMINT-685556.

Structurei

3D structure databases

ProteinModelPortaliP05030.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi5 – 17Poly-SerAdd BLAST13
Compositional biasi31 – 78Asp/Glu-rich (acidic)Add BLAST48
Compositional biasi39 – 44Poly-Asp6
Compositional biasi585 – 590Poly-Gly6

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00840000130975.
HOGENOMiHOG000160005.
InParanoidiP05030.
KOiK01535.
OMAiFMQGSTG.
OrthoDBiEOG092C0HLD.

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.
IPR023214. HAD-like_dom.
IPR006534. P-type_ATPase_IIIA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. 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

        10         20         30         40         50
MTDTSSSSSS SSASSVSAHQ PTQEKPAKTY DDAASESSDD DDIDALIEEL
60 70 80 90 100
QSNHGVDDED SDNDGPVAAG EARPVPEEYL QTDPSYGLTS DEVLKRRKKY
110 120 130 140 150
GLNQMADEKE SLVVKFVMFF VGPIQFVMEA AAILAAGLSD WVDFGVICGL
160 170 180 190 200
LMLNAGVGFV QEFQAGSIVD ELKKTLANTA VVIRDGQLVE IPANEVVPGD
210 220 230 240 250
ILQLEDGTVI PTDGRIVTED CFLQIDQSAI TGESLAVDKH YGDQTFSSST
260 270 280 290 300
VKRGEGFMVV TATGDNTFVG RAAALVNKAA GGQGHFTEVL NGIGIILLVL
310 320 330 340 350
VIATLLLVWT ACFYRTNGIV RILRYTLGIT IIGVPVGLPA VVTTTMAVGA
360 370 380 390 400
AYLAKKQAIV QKLSAIESLA GVEILCSDKT GTLTKNKLSL HEPYTVEGVS
410 420 430 440 450
PDDLMLTACL AASRKKKGLD AIDKAFLKSL KQYPKAKDAL TKYKVLEFHP
460 470 480 490 500
FDPVSKKVTA VVESPEGERI VCVKGAPLFV LKTVEEDHPI PEDVHENYEN
510 520 530 540 550
KVAELASRGF RALGVARKRG EGHWEILGVM PCMDPPRDDT AQTVSEARHL
560 570 580 590 600
GLRVKMLTGD AVGIAKETCR QLGLGTNIYN AERLGLGGGG DMPGSELADF
610 620 630 640 650
VENADGFAEV FPQHKYRVVE ILQNRGYLVA MTGDGVNDAP SLKKADTGIA
660 670 680 690 700
VEGATDAARS AADIVFLAPG LSAIIDALKT SRQIFHRMYS YVVYRIALSL
710 720 730 740 750
HLEIFLGLWI AILDNSLDID LIVFIAIFAD VATLAIAYDN APYSPKPVKW
760 770 780 790 800
NLPRLWGMSI ILGIVLAIGS WITLTTMFLP KGGIIQNFGA MNGIMFLQIS
810 820 830 840 850
LTENWLIFIT RAAGPFWSSI PSWQLAGAVF AVDIIATMFT LFGWWSENWT
860 870 880 890 900
DIVTVVRVWI WSIGIFCVLG GFYYEMSTSE AFDRLMNGKP MKEKKSTRSV
910
EDFMAAMQRV STQHEKET
Length:918
Mass (Da):99,619
Last modified:November 1, 1995 - v2
Checksum:iAA1E93966B37E8E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP05030.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33238. 265 interactors.
DIPiDIP-2537N.
IntActiP05030. 9 interactors.
MINTiMINT-685556.

Protein family/group databases

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

PTM databases

iPTMnetiP05030.

Proteomic databases

MaxQBiP05030.
PRIDEiP05030.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGL008C.
SGDiS000002976. PMA1.

Phylogenomic databases

GeneTreeiENSGT00840000130975.
HOGENOMiHOG000160005.
InParanoidiP05030.
KOiK01535.
OMAiFMQGSTG.
OrthoDBiEOG092C0HLD.

Enzyme and pathway databases

BioCyciYEAST:G3O-30531-MONOMER.
BRENDAi3.6.3.6. 984.

Miscellaneous databases

PROiP05030.

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.
IPR023214. HAD-like_dom.
IPR006534. P-type_ATPase_IIIA.
IPR001757. P_typ_ATPase.
[Graphical view]
PfamiPF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
[Graphical view]
PRINTSiPR00120. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 183 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.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.