P20649 (PMA1_ARATH) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › 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. Interacts with PPI1; this interaction promotes ATPase activity. Ref.5 Ref.7
Subcellular location	Cell membrane; Multi-pass membrane protein Probable.
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 PubMed 8300635. Source: UniProtKB regulation of stomatal movement Inferred from mutant phenotype PubMed 12047634. Source: TAIR response to abscisic acid stimulus Inferred from mutant phenotype PubMed 12047634. Source: TAIR response to water deprivation Inferred from mutant phenotype PubMed 12047634. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR integral to membrane Inferred from direct assay PubMed 8300635. Source: UniProtKB nucleus Inferred from direct assay Ref.11. Source: TAIR plasma membrane Inferred from direct assay PubMed 14506206PubMed 15060130PubMed 16618929Ref.9PubMed 17644812PubMed 22923678. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from direct assay PubMed 8300635. Source: UniProtKB magnesium ion binding Inferred from direct assay PubMed 8300635. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPI1	O23144	7	EBI-2354448,EBI-2354477

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 949	948	ATPase 1, plasma membrane-type		PRO_0000046274
Regions
	Topological domain	2 – 61	60	Cytoplasmic Potential
	Transmembrane	62 – 81	20	Helical; Name=1; Potential
	Topological domain	82 – 93	12	Extracellular Potential
	Transmembrane	94 – 114	21	Helical; Name=2; Potential
	Topological domain	115 – 243	129	Cytoplasmic Potential
	Transmembrane	244 – 264	21	Helical; Name=3; Potential
	Topological domain	265 – 273	9	Extracellular Potential
	Transmembrane	274 – 291	18	Helical; Name=4; Potential
	Topological domain	292 – 643	352	Cytoplasmic Potential
	Transmembrane	644 – 665	22	Helical; Name=5; Potential
	Topological domain	666 – 670	5	Extracellular Potential
	Transmembrane	671 – 693	23	Helical; Name=6; Potential
	Topological domain	694 – 709	16	Cytoplasmic Potential
	Transmembrane	710 – 730	21	Helical; Name=7; Potential
	Topological domain	731 – 751	21	Extracellular Potential
	Transmembrane	752 – 772	21	Helical; Name=8; Potential
	Topological domain	773 – 784	12	Cytoplasmic Potential
	Transmembrane	785 – 805	21	Helical; Name=9; Potential
	Topological domain	806 – 813	8	Extracellular Potential
	Transmembrane	814 – 834	21	Helical; Name=10; Potential
	Topological domain	835 – 949	115	Cytoplasmic Potential
	Region	947 – 949	3	Interaction with 14-3-3 proteins By similarity
Sites
	Active site	329	1	4-aspartylphosphate intermediate By similarity
	Metal binding	588	1	Magnesium By similarity
	Metal binding	592	1	Magnesium By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	881	1	Phosphothreonine Ref.8 Ref.10 Ref.13
	Modified residue	899	1	Phosphoserine Ref.6 Ref.10
	Modified residue	948	1	Phosphothreonine Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Experimental info
	Sequence conflict	771	1	V → L in AAA32813. Ref.1
	Sequence conflict	778	1	S → Y in AAA32813. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P20649 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A613FF6070ECC9F3	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

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] [Europe PMC] [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. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed] [Europe PMC] [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. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"A novel interaction partner for the C-terminus of Arabidopsis thaliana plasma membrane H+-ATPase (AHA1 isoform): site and mechanism of action on H+-ATPase activity differ from those of 14-3-3 proteins." Morandini P., Valera M., Albumi C., Bonza M.C., Giacometti S., Ravera G., Murgia I., Soave C., De Michelis M.I. Plant J. 31:487-497(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPI1. Strain: cv. Landsberg erecta. Tissue: Leaf and Root.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-899 AND THR-948, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[7]	"Characterization of the interaction between the plasma membrane H-ATPase of Arabidopsis thaliana and a novel interactor (PPI1)." Viotti C., Luoni L., Morandini P., De Michelis M.I. FEBS J. 272:5864-5871(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPI1.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881 AND THR-948, MASS SPECTROMETRY. Tissue: Seedling.
[9]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, MASS SPECTROMETRY. Strain: cv. Columbia.
[10]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-881; SER-899 AND THR-948, MASS SPECTROMETRY.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, MASS SPECTROMETRY. Tissue: Root.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, MASS SPECTROMETRY. Strain: cv. Columbia.
[13]	"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] [Europe PMC] [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. 3 interactions.
MINT	MINT-6822995.
Protein family/group databases
TCDB	3.A.3.3.7. P-type ATPase (P-ATPase) superfamily.
Proteomic databases
PaxDb	P20649.
PRIDE	P20649.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G18960.1; AT2G18960.1; AT2G18960.
GeneID	816413.
KEGG	ath:AT2G18960.
Organism-specific databases
TAIR	At2g18960.
Phylogenomic databases
eggNOG	COG0474.
HOGENOM	HOG000160005.
InParanoid	P20649.
KO	K01535.
OMA	DNNDELM.
PhylomeDB	P20649.
ProtClustDB	CLSN2683068.
Gene expression databases
ArrayExpress	P20649.
Genevestigator	P20649.
GermOnline	AT2G18960. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.20.1110.10. 3 hits. 2.70.150.10. 2 hits. 3.40.1110.10. 1 hit.
InterPro	IPR004014. 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]
PANTHER	PTHR24093. PTHR24093. 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:	May 1, 2013
This is version 133 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program