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Protein

Plasma membrane ATPase 2

Gene

pma2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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 sitei464 – 46414-aspartylphosphate intermediateBy similarity
Metal bindingi720 – 7201MagnesiumBy similarity
Metal bindingi724 – 7241MagnesiumBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • hydrogen-exporting ATPase activity, phosphorylative mechanism Source: PomBase
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Plasma membrane ATPase 2 (EC:3.6.3.6)
Alternative name(s):
Proton pump 2
Gene namesi
Name:pma2
ORF Names:SPCC1020.01c, SPCC1393.01
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1020.01c.
PomBaseiSPCC1020.01c. pma2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 201201CytoplasmicSequence analysisAdd
BLAST
Transmembranei202 – 22221Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini223 – 2264ExtracellularSequence analysis
Transmembranei227 – 24620Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini247 – 377131CytoplasmicSequence analysisAdd
BLAST
Transmembranei378 – 39922Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini400 – 41011ExtracellularSequence analysisAdd
BLAST
Transmembranei411 – 43323Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini434 – 805372CytoplasmicSequence analysisAdd
BLAST
Transmembranei806 – 82419Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini825 – 84016ExtracellularSequence analysisAdd
BLAST
Transmembranei841 – 86020Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini861 – 91252CytoplasmicSequence analysisAdd
BLAST
Transmembranei913 – 93321Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini934 – 94613ExtracellularSequence analysisAdd
BLAST
Transmembranei947 – 96317Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini964 – 101047CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell division site Source: PomBase
  • cell tip Source: PomBase
  • integral component of plasma membrane Source: GO_Central
  • intracellular membrane-bounded organelle Source: GO_Central
  • plasma membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10101010Plasma membrane ATPase 2PRO_0000046270Add
BLAST

Post-translational modificationi

In addition to transient phosphorylation of the active site Asp residue, this protein, but not the product of the pma1 locus, is phosphorylated efficiently in isolated plasma membrane.

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

BioGridi275585. 1 interaction.
MINTiMINT-4688140.

Structurei

3D structure databases

ProteinModelPortaliP28876.
SMRiP28876. Positions 131-1003.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi121 – 15030Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000160005.
InParanoidiP28876.
KOiK01535.
OMAiTSITHET.
OrthoDBiEOG092C0HLD.
PhylomeDBiP28876.

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. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P28876-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQRNNGEGRP EGMHRISRFL HGNPFKNNAS PQDDSTTRTE VYEEGGVEDS
60 70 80 90 100
AVDYDNASGN AAPRLTAAPN THAQQANLQS GNTSITHETQ STSRGQEATT
110 120 130 140 150
SPSLSASHEK PARPQTGEGS DNEDEDEDID ALIEDLYSQD QEEEQVEEEE
160 170 180 190 200
SPGPAGAAKV VPEELLETDP KYGLTESEVE ERKKKYGLNQ MKEEKTNNIK
210 220 230 240 250
KFLSFFVGPI QFVMELAAAL AAGLRDWVDF GVICALLLLN ATVGFVQEYQ
260 270 280 290 300
AGSIVDELKK TMALKASVLR DGRVKEIEAS EIVPGDILHL DEGTICPADG
310 320 330 340 350
RLITKDCFLQ VDQSAITGES LAVDKHQNDT MYSSSTVKRG EAFMVVTATA
360 370 380 390 400
DSTFVGRAAS LVGAAGQSQG HFTEVLNGIG TILLVLVILT LLCIYTAAFY
410 420 430 440 450
RSVRLAALLE YTLAITIIGV PVGLPAVVTT TMAVGAAYLA KKKAIVQKLS
460 470 480 490 500
AIESLAGVEI LCSDKTGTLT KNRLSLGEPY CVEGVSPDDL MLTACLASSR
510 520 530 540 550
KKKGLDAIDK AFLKALRNYP KAKDQLSKYK VLDFHPFDPV SKKITAYVEA
560 570 580 590 600
PDGQRITCVK GAPLWVFKTV QDDHEVPEAI TDAYREQVND MASRGFRSLG
610 620 630 640 650
VARKADGKQW EILGIMPCSD PPRHDTARTI HEAIGLGLRI KMLTGDAVGI
660 670 680 690 700
AKETARQLGM GTNVYNAERL GLSGGGDMPG SEVNDFVEAA DGFAEVFPQH
710 720 730 740 750
KYAVVDILQQ RGYLVAMTGD GVNDAPSLKK ADAGIAVEGA SDAARSAADI
760 770 780 790 800
VFLAPGLSAI IDALKTSRQI FHRMYAYVVY RIALSLHLEI FLGLWLIIRN
810 820 830 840 850
QLLNLELIVF IAIFADVATL AIAYDNAPYA MKPVKWNLPR LWGLATIVGI
860 870 880 890 900
LLAIGTWIVN TTMIAQGQNR GIVQNFGVQD EVLFLQISLT ENWLIFITRC
910 920 930 940 950
SGPFWSSFPS WQLSGAVLVV DILATLFCIF GWFKGGHQTS IVAVIRIWMY
960 970 980 990 1000
SFGIFCLIAG VYYILSESSS FDRWMHGKHK ERGTTRKLED FVMQLQRTST
1010
HHEAEGKVTS
Length:1,010
Mass (Da):110,128
Last modified:December 1, 1992 - v1
Checksum:i2C629A45125B4DC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60471 Genomic DNA. Translation: AAA35325.1.
CU329672 Genomic DNA. Translation: CAA18989.1.
PIRiA40945. PXZP2P.
RefSeqiNP_587959.2. NM_001022950.2.

Genome annotation databases

EnsemblFungiiSPCC1020.01c.1; SPCC1020.01c.1:pep; SPCC1020.01c.
GeneIDi2539012.
KEGGispo:SPCC1020.01c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60471 Genomic DNA. Translation: AAA35325.1.
CU329672 Genomic DNA. Translation: CAA18989.1.
PIRiA40945. PXZP2P.
RefSeqiNP_587959.2. NM_001022950.2.

3D structure databases

ProteinModelPortaliP28876.
SMRiP28876. Positions 131-1003.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275585. 1 interaction.
MINTiMINT-4688140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1020.01c.1; SPCC1020.01c.1:pep; SPCC1020.01c.
GeneIDi2539012.
KEGGispo:SPCC1020.01c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1020.01c.
PomBaseiSPCC1020.01c. pma2.

Phylogenomic databases

HOGENOMiHOG000160005.
InParanoidiP28876.
KOiK01535.
OMAiTSITHET.
OrthoDBiEOG092C0HLD.
PhylomeDBiP28876.

Miscellaneous databases

PROiP28876.

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. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPMA2_SCHPO
AccessioniPrimary (citable) accession number: P28876
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: September 7, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

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.