Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Plasma membrane ATPase

Gene

PMA1

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 4 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).

Enzyme regulationi

Activated by high pH or also by potassium ions when the medium pH is low.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei359 – 35914-aspartylphosphate intermediateBy similarity
Metal bindingi615 – 6151MagnesiumBy similarity
Metal bindingi619 – 6191MagnesiumBy similarity

GO - Molecular functioni

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 (EC:3.6.3.6)
Alternative name(s):
Proton pump
Gene namesi
Name:PMA1
Ordered Locus Names:KLLA0A09031g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
Proteomesi
  • UP000000598 Componenti: Chromosome A

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 9696CytoplasmicSequence analysisAdd
BLAST
Transmembranei97 – 11721Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini118 – 1214ExtracellularSequence analysis
Transmembranei122 – 14120Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini142 – 272131CytoplasmicSequence analysisAdd
BLAST
Transmembranei273 – 29422Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini295 – 30511ExtracellularSequence analysisAdd
BLAST
Transmembranei306 – 32823Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini329 – 700372CytoplasmicSequence analysisAdd
BLAST
Transmembranei701 – 71919Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini720 – 73516ExtracellularSequence analysisAdd
BLAST
Transmembranei736 – 75520Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini756 – 80550CytoplasmicSequence analysisAdd
BLAST
Transmembranei806 – 82621Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini827 – 83812ExtracellularSequence analysisAdd
BLAST
Transmembranei839 – 85517Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini856 – 89944CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi669 – 6691M → I in 3.3; low capacity to pump out protons. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 899899Plasma membrane ATPasePRO_0000046267Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP49380.

Interactioni

Protein-protein interaction databases

STRINGi284590.XP_451395.1.

Structurei

3D structure databases

ProteinModelPortaliP49380.
SMRiP49380. Positions 28-897.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi566 – 5716Poly-Gly

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0205. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000160005.
InParanoidiP49380.
KOiK01535.
OMAiFGWFENS.
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.
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.

P49380-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAATEPTKE KPVNNQDSDD EDEDIDQLIE DLQSHHGLDD ESEDDEHVAA
60 70 80 90 100
GSARPVPEEL LQTDPSYGLT SDEVTKRRKK YGLNQMSEET ENLFVKFLMF
110 120 130 140 150
FIGPIQFVME AAAILAAGLE DWVDFGVICG LLFLNAAVGF IQEYQAGSIV
160 170 180 190 200
DELKKTLANS AVVIRDGNLV EVPSNEVVPG DILQLEDGVV IPADGRLVTE
210 220 230 240 250
DCFIQIDQSA ITGESLAVDK RFGDSTFSSS TVKRGEAFMI VTATGDSTFV
260 270 280 290 300
GRAAALVNKA AAGSGHFTEV LNGIGTILLI LVIVTLLLVW VASFYRTNKI
310 320 330 340 350
VRILRYTLAI TIVGVPVGLP AVVTTTMAVG AAYLAKKQAI VQKLSAIESL
360 370 380 390 400
AGVEILCSDK TGTLTKNKLS LHEPYTVEGV DPDDLMLTAC LAASRKKKGL
410 420 430 440 450
DAIDKAFLKS LISYPRAKAA LTKYKLLEFH PFDPVSKKVT AIVESPEGER
460 470 480 490 500
IICVKGAPLF VLKTVEEEHP IPEDVRENYE NKVAELASRG FRALGVARKR
510 520 530 540 550
GEGHWEILGV MPCMDPPRDD TAQTVNEARH LGLRVKMLTG DAVGIAKETC
560 570 580 590 600
RQLGLGTNIY NAERLGLGGG GDMPGSELAD FVENADGFAE VFPQHKYNVV
610 620 630 640 650
EILQQRGYLV AMTGDGVNDA PSLKKADTGI AVEGATDAAR SAADIVFLAP
660 670 680 690 700
GLSAIIDALK TSRQIFHRMY SYVVYRIALS LHLEIFLGLW IAILNRSLNI
710 720 730 740 750
DLVVFIAIFA DVATLAIAYD NAPYSPKPVK WNLRRLWGMS VILGIILAIG
760 770 780 790 800
TWITLTTMFV PKGGIIQNFG SIDGVLFLQI SLTENWLIFI TRAAGPFWSS
810 820 830 840 850
IPSWQLSGAV LIVDIIATMF CLFGWWSQNW NDIVTVVRVW IFSFGVFCVM
860 870 880 890
GGAYYMMSES EAFDRFMNGK SRRDKPSGRS VEDFLMAMQR VSTQHEKEN
Length:899
Mass (Da):98,260
Last modified:February 1, 1996 - v1
Checksum:iF29DC853BDCF4396
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37875 Genomic DNA. Translation: AAA69688.1.
CR382121 Genomic DNA. Translation: CAH02983.1.
RefSeqiXP_451395.1. XM_451395.1.

Genome annotation databases

EnsemblFungiiCAH02983; CAH02983; KLLA0_A09031g.
GeneIDi2896449.
KEGGikla:KLLA0A09031g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37875 Genomic DNA. Translation: AAA69688.1.
CR382121 Genomic DNA. Translation: CAH02983.1.
RefSeqiXP_451395.1. XM_451395.1.

3D structure databases

ProteinModelPortaliP49380.
SMRiP49380. Positions 28-897.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi284590.XP_451395.1.

Proteomic databases

PRIDEiP49380.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAH02983; CAH02983; KLLA0_A09031g.
GeneIDi2896449.
KEGGikla:KLLA0A09031g.

Phylogenomic databases

eggNOGiKOG0205. Eukaryota.
COG0474. LUCA.
HOGENOMiHOG000160005.
InParanoidiP49380.
KOiK01535.
OMAiFGWFENS.
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.
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...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of the plasma membrane H(+)-ATPase from Kluyveromyces lactis: a single nucleotide substitution in the gene confers ethidium bromide resistance and deficiency in K+ uptake."
    Miranda M., Ramirez J., Pena A., Coria R.
    J. Bacteriol. 177:2360-2367(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF MET-669.
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
  2. "Genome evolution in yeasts."
    Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.
    , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
    Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.

Entry informationi

Entry nameiPMA1_KLULA
AccessioniPrimary (citable) accession number: P49380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 13, 2016
This is version 123 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. 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.