ATPase 1, plasma membrane-type - Arabidopsis thaliana (Mouse-ear cress)

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P20649 (PMA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
ATPase 1, plasma membrane-type
EC=3.6.3.6

Alternative name(s):
Proton pump 1

Gene names

Name:	AHA1
Ordered Locus Names:	At2g18960
ORF Names:	F19F24.16

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	949 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The plasma membrane H⁺ ATPase of plants and fungi generates a proton gradient that 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).
Subunit structure	Binds to 14-3-3 proteins. The binding is induced by phosphorylation of Thr-948. Binding to 14-3-3 proteins activates the H⁺-ATPase By similarity.
Subcellular location	Cell membrane; Multi-pass membrane protein Probable Ref.5.
Post-translational modification	Phosphorylation level varies significantly during early response to general elicitors.
Sequence similarities	Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIIA subfamily. [View classification]

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from electronic annotation. Source: InterPro ATP hydrolysis coupled proton transport Inferred from direct assay. Source: UniProtKB regulation of stomatal movement Inferred from mutant phenotype. Source: TAIR response to abscisic acid stimulus Inferred from mutant phenotype. Source: TAIR response to water deprivation Inferred from mutant phenotype. Source: TAIR
Cellular component	integral to membrane Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay Ref.9. Source: TAIR plasma membrane Inferred from direct assay Ref.7. Source: TAIR plasmodesma Inferred from direct assay. Source: TAIR vacuole Inferred from direct assay. Source: TAIR
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from direct assay. Source: UniProtKB magnesium ion binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ppi	O23144	7	EBI-2354448,EBI-2354477

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 949

948

ATPase 1, plasma membrane-type

PRO_0000046274

Regions

Topological domain

2 – 61

Cytoplasmic Potential

Transmembrane

62 – 81

Helical; Name=1; Potential

Topological domain

82 – 93

Extracellular Potential

Transmembrane

94 – 114

Helical; Name=2; Potential

Topological domain

115 – 243

129

Cytoplasmic Potential

Transmembrane

244 – 264

Helical; Name=3; Potential

Topological domain

265 – 273

Extracellular Potential

Transmembrane

274 – 291

Helical; Name=4; Potential

Topological domain

292 – 643

352

Cytoplasmic Potential

Transmembrane

644 – 665

Helical; Name=5; Potential

Topological domain

666 – 670

Extracellular Potential

Transmembrane

671 – 693

Helical; Name=6; Potential

Topological domain

694 – 709

Cytoplasmic Potential

Transmembrane

710 – 730

Helical; Name=7; Potential

Topological domain

731 – 751

Extracellular Potential

Transmembrane

752 – 772

Helical; Name=8; Potential

Topological domain

773 – 784

Cytoplasmic Potential

Transmembrane

785 – 805

Helical; Name=9; Potential

Topological domain

806 – 813

Extracellular Potential

Transmembrane

814 – 834

Helical; Name=10; Potential

Topological domain

835 – 949

115

Cytoplasmic Potential

Region

947 – 949

Interaction with 14-3-3 proteins By similarity

Sites

Active site

329

4-aspartylphosphate intermediate By similarity

Metal binding

588

Magnesium By similarity

Metal binding

592

Magnesium By similarity

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

881

Phosphothreonine Ref.6 Ref.8 Ref.11

Modified residue

899

Phosphoserine Ref.5 Ref.8

Modified residue

948

Phosphothreonine Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Experimental info

Sequence conflict

771

V → L in AAA32813. Ref.1

Sequence conflict

778

S → Y in AAA32813. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P20649 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A613FF6070ECC9F3
Show »

FASTA

949

104,224

        10         20         30         40         50         60 
MSGLEDIKNE TVDLEKIPIE EVFQQLKCTR EGLTTQEGED RIVIFGPNKL EEKKESKILK 

        70         80         90        100        110        120 
FLGFMWNPLS WVMEAAALMA IALANGDNRP PDWQDFVGII CLLVINSTIS FIEENNAGNA 

       130        140        150        160        170        180 
AAALMAGLAP KTKVLRDGKW SEQEAAILVP GDIVSIKLGD IIPADARLLE GDPLKVDQSA 

       190        200        210        220        230        240 
LTGESLPVTK HPGQEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL 

       250        260        270        280        290        300 
TSIGNFCICS IAIGIAIEIV VMYPIQHRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG 

       310        320        330        340        350        360 
SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC KGVEKDQVLL 

       370        380        390        400        410        420 
FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF NPVDKRTALT YIDSDGNWHR 

       430        440        450        460        470        480 
VSKGAPEQIL DLANARPDLR KKVLSCIDKY AERGLRSLAV ARQVVPEKTK ESPGGPWEFV 

       490        500        510        520        530        540 
GLLPLFDPPR HDSAETIRRA LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSAALLGT 

       550        560        570        580        590        600 
DKDSNIASIP VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD 

       610        620        630        640        650        660 
IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV SITIRIVFGF 

       670        680        690        700        710        720 
MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT PDSWKLKEIF ATGIVLGGYQ 

       730        740        750        760        770        780 
AIMSVIFFWA AHKTDFFSDK FGVRSIRDNN DELMGAVYLQ VSIISQALIF VTRSRSWSFV 

       790        800        810        820        830        840 
ERPGALLMIA FVIAQLVATL IAVYADWTFA KVKGIGWGWA GVIWIYSIVT YFPQDILKFA 

       850        860        870        880        890        900 
IRYILSGKAW ASLFDNRTAF TTKKDYGIGE REAQWAQAQR TLHGLQPKED VNIFPEKGSY 

       910        920        930        940 
RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVAKLKGLDI DTAGHHYTV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and sequence of cDNA encoding the plasma membrane proton pump (H+-ATPase) of Arabidopsis thaliana." Harper J.F., Surowy T.K., Sussman M.R. Proc. Natl. Acad. Sci. U.S.A. 86:1234-1238(1989) [PubMed: 2521951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[4]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database." Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C. Plant Cell 16:2394-2405(2004) [PubMed: 15308754] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899 AND THR-948, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[6]	"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis." Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X. Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed: 17586839] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881 AND THR-948, MASS SPECTROMETRY. Tissue: Seedling.
[7]	"Quantitative phosphoproteomics of early elicitor signaling in Arabidopsis." Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M., Menke F.L.H. Mol. Cell. Proteomics 6:1198-1214(2007) [PubMed: 17317660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, MASS SPECTROMETRY. Strain: cv. Columbia.
[8]	"Quantitative phosphoproteomic analysis of plasma membrane proteins reveals regulatory mechanisms of plant innate immune responses." Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C. Plant J. 51:931-940(2007) [PubMed: 17651370] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881; SER-899 AND THR-948, MASS SPECTROMETRY.
[9]	"Site-specific phosphorylation profiling of Arabidopsis proteins by mass spectrometry and peptide chip analysis." de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E., Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H. J. Proteome Res. 7:2458-2470(2008) [PubMed: 18433157] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, MASS SPECTROMETRY. Tissue: Root.
[10]	"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana." Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C. J. Proteomics 72:439-451(2009) [PubMed: 19245862] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, MASS SPECTROMETRY. Strain: cv. Columbia.
[11]	"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks." Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S. Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881 AND THR-948, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M24107 mRNA. Translation: AAA32813.1. AC003673 Genomic DNA. Translation: AAC09030.1. CP002685 Genomic DNA. Translation: AEC06832.1. BT008692 mRNA. Translation: AAP40498.1.
IPI	IPI00526113.
PIR	PXMUP1. T01624.
RefSeq	NP_179486.1. NM_127453.3.
UniGene	At.24695.
3D structure databases
ProteinModelPortal	P20649.
SMR	P20649. Positions 12-844, 900-949.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20649. 4 interactions.
MINT	MINT-6822995.
STRING	P20649.
Protein family/group databases
TCDB	3.A.3.3.7. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PRIDE	P20649.
ProMEX	P20649.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G18960.1; AT2G18960.1; AT2G18960.
GeneID	816413.
GenomeReviews	Gene locus AT2G18960 in contig CT485783_GR.
KEGG	ath:AT2G18960.
NMPDR	fig\|3702.1.peg.8893.
Organism-specific databases
TAIR	At2g18960.
Phylogenomic databases
eggNOG	KOG0205.
HOGENOM	HBG706356.
InParanoid	P20649.
OMA	DNNDELM.
PhylomeDB	P20649.
ProtClustDB	CLSN2683068.
Gene expression databases
ArrayExpress	P20649.
Genevestigator	P20649.
GermOnline	AT2G18960. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR008250. ATPase_P-typ_ATPase-assoc-dom. IPR004014. ATPase_P-typ_cation-transptr_N. IPR023300. ATPase_P-typ_cyto_domA. IPR023299. ATPase_P-typ_cyto_domN. IPR000695. ATPase_P-typ_H-transp. IPR001757. ATPase_P-typ_ion-transptr. IPR018303. ATPase_P-typ_P_site. IPR006534. ATPase_P-typ_PM_proton-efflux. IPR023298. ATPase_P-typ_TM_dom. IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. [Graphical view]
Gene3D	G3DSA:2.70.150.10. ATPase_P-typ_cyto_domA. 2 hits. G3DSA:3.40.1110.10. ATPase_P-typ_cyto_domN. 1 hit. G3DSA:1.20.1110.10. ATPase_P-typ_TM_dom. 3 hits.
KO	K01535.
PANTHER	PTHR24093:SF61. PTHR24093:SF61. 1 hit.
Pfam	PF00690. Cation_ATPase_N. 1 hit. PF00122. E1-E2_ATPase. 1 hit. PF00702. Hydrolase. 1 hit. [Graphical view]
PRINTS	PR00119. CATATPASE. PR00120. HATPASE.
SMART	SM00831. Cation_ATPase_N. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01647. ATPase-IIIA_H. 1 hit. TIGR01494. ATPase_P-type. 2 hits.
PROSITE	PS00154. ATPASE_E1_E2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PMA1_ARATH

Accession

Primary (citable) accession number: P20649
Secondary accession number(s): O64626

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents