ATPase 3, plasma membrane-type - Arabidopsis thaliana (Mouse-ear cress)

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P20431 (PMA3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 114. History...

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

Documents (2) |

Third-party data

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

Names and origin

Protein names

Recommended name:
ATPase 3, plasma membrane-type
EC=3.6.3.6

Alternative name(s):
Proton pump 3

Gene names

Name:	AHA3
Ordered Locus Names:	At5g57350
ORF Names:	MJB24.16

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. Ref.7
Subcellular location	Cell membrane; Multi-pass membrane protein Probable Ref.8.
Tissue specificity	Found predominantly in phloem cells of leaves, stems, roots and flowers.
Post-translational modification	Phosphorylation level varies significantly during early response to bacterial elicitor (e.g. fusicoccin FC).
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
Cellular component	integral to membrane Inferred from direct assay. Source: UniProtKB plasma membrane Inferred from direct assay. Source: TAIR plasmodesma 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
Complete GO annotation...

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 3, plasma membrane-type

PRO_0000046276

Regions

Topological domain

2 – 62

Cytoplasmic Potential

Transmembrane

63 – 82

Helical; Name=1; Potential

Topological domain

83 – 94

Extracellular Potential

Transmembrane

95 – 115

Helical; Name=2; Potential

Topological domain

116 – 244

129

Cytoplasmic Potential

Transmembrane

245 – 265

Helical; Name=3; Potential

Topological domain

266 – 274

Extracellular Potential

Transmembrane

275 – 292

Helical; Name=4; Potential

Topological domain

293 – 644

352

Cytoplasmic Potential

Transmembrane

645 – 666

Helical; Name=5; Potential

Topological domain

667 – 671

Extracellular Potential

Transmembrane

672 – 694

Helical; Name=6; Potential

Topological domain

695 – 710

Cytoplasmic Potential

Transmembrane

711 – 731

Helical; Name=7; Potential

Topological domain

732 – 752

Extracellular Potential

Transmembrane

753 – 773

Helical; Name=8; Potential

Topological domain

774 – 785

Cytoplasmic Potential

Transmembrane

786 – 806

Helical; Name=9; Potential

Topological domain

807 – 814

Extracellular Potential

Transmembrane

815 – 835

Helical; Name=10; Potential

Topological domain

836 – 949

114

Cytoplasmic Potential

Region

947 – 949

Interaction with 14-3-3 proteins

Sites

Active site

330

4-aspartylphosphate intermediate By similarity

Metal binding

589

Magnesium By similarity

Metal binding

593

Magnesium By similarity

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

882

Phosphothreonine Ref.9 Ref.10 Ref.11

Modified residue

948

Phosphothreonine Ref.7 Ref.8

Experimental info

Mutagenesis

947

Y → A: Impaired fusicoccin- (FC) dependent activation by 14-3-3 protein. Ref.7

Mutagenesis

948

T → A: Impaired fusicoccin- (FC) dependent activation by 14-3-3 protein. Ref.7

Mutagenesis

949

V → A: Impaired fusicoccin- (FC) dependent activation by 14-3-3 protein. Ref.7

Sequences

Sequence

Length

Mass (Da)

Tools

P20431 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 3F88C87D849A4001
Show »

FASTA

949

104,450

        10         20         30         40         50         60 
MASGLEDIVN ENVDLEKIPI EEVFQQLKCS REGLSGAEGE NRLQIFGPNK LEEKKESKLL 

        70         80         90        100        110        120 
KFLGFMWNPL SWVMEAAAIM AIALANGGGK PPDWQDFVGI VCLLVINSTI SFVEENNAGN 

       130        140        150        160        170        180 
AAAALMAGLA PKTKVLRDGK WSEQEASILV PGDIVSIKLG DIIPADARLL EGDPLKVDQS 

       190        200        210        220        230        240 
ALTGESLPAT KGPGEEVFSG STCKQGEIEA VVIATGVHTF FGKAAHLVDS TNQVGHFQKV 

       250        260        270        280        290        300 
LTAIGNFCIC SIAVGIAIEI VVMYPIQRRH YRDGIDNLLV LLIGGIPIAM PTVLSVTMAI 

       310        320        330        340        350        360 
GSHKLSQQGA ITKRMTAIEE MAGMDVLCSD KTGTLTLNKL SVDKNLIEVY CKGVEKDEVL 

       370        380        390        400        410        420 
LFAARASRVE NQDAIDAAMV GMLADPKEAR AGIREIHFLP FNPVDKRTAL TFIDSNGNWH 

       430        440        450        460        470        480 
RVSKGAPEQI LDLCNARADL RKRVHSTIDK YAERGLRSLA VSRQTVPEKT KESSGSPWEF 

       490        500        510        520        530        540 
VGVLPLFDPP RHDSAETIRR ALDLGVNVKM ITGDQLAIAK ETGRRLGMGS NMYPSSSLLG 

       550        560        570        580        590        600 
KHKDEAMAHI PVEDLIEKAD GFAGVFPEHK YEIVKKLQER KHICGMTGDG VNDAPALKKA 

       610        620        630        640        650        660 
DIGIAVADAT DAARGASDIV LTEPGLSVII SAVLTSRAIF QRMKNYTIYA VSITIRIVFG 

       670        680        690        700        710        720 
FMLIALIWKF DFSPFMVLII AILNDGTIMT ISKDRVKPSP TPDSWKLKEI FATGVVLGGY 

       730        740        750        760        770        780 
MAIMTVVFFW AAYKTDFFPR TFHVRDLRGS EHEMMSALYL QVSIVSQALI FVTRSRSWSF 

       790        800        810        820        830        840 
TERPGYFLLI AFWVAQLIAT AIAVYGNWEF ARIKGIGWGW AGVIWLYSIV FYFPLDIMKF 

       850        860        870        880        890        900 
AIRYILAGTA WKNIIDNRTA FTTKQNYGIE EREAQWAHAQ RTLHGLQNTE TANVVPERGG 

       910        920        930        940 
YRELSEIANQ AKRRAEIARL RELHTLKGHV ESVVKLKGLD IETAGHYTV

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of a plasma membrane H+-ATPase gene from the plant Arabidopsis thaliana." Pardo J.M., Serrano R. J. Biol. Chem. 264:8557-8562(1989) [PubMed: 2524481] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S. DNA Res. 7:31-63(2000) [PubMed: 10718197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones." Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S. DNA Res. 5:379-391(1998) [PubMed: 10048488] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"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.
[6]	"Evidence for a plasma membrane proton pump in phloem cells of higher plants." Dewitt N.D., Harper J.F., Sussman M.R. Plant J. 1:121-128(1991) [PubMed: 1844877] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8. Strain: cv. Columbia.
[7]	"Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947)." Fuglsang A.T., Visconti S., Drumm K., Jahn T., Stensballe A., Mattei B., Jensen O.N., Aducci P., Palmgren M.G. J. Biol. Chem. 274:36774-36780(1999) [PubMed: 10593986] [Abstract] Cited for: PHOSPHORYLATION AT THR-948, INTERACTION WITH 14-3-3 PROTEINS, MUTAGENESIS OF TYR-947; THR-948 AND VAL-949.
[8]	"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 THR-948, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[9]	"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-882, MASS SPECTROMETRY.
[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-882, 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-882, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J04737 Genomic DNA. Translation: AAA32750.1. AB019233, AB016891 Genomic DNA. Translation: BAB09963.1. CP002688 Genomic DNA. Translation: AED96889.1. CP002688 Genomic DNA. Translation: AED96890.1. AY072153 mRNA. Translation: AAL59975.1. X60115 Genomic DNA. Translation: CAA42714.1.
IPI	IPI00532025.
PIR	PXMUP3. A33698.
RefSeq	NP_001190559.1. NM_001203630.1. NP_200545.1. NM_125118.2.
UniGene	At.290.
3D structure databases
ProteinModelPortal	P20431.
SMR	P20431. Positions 13-845, 901-943.
ModBase	Search...
Protein-protein interaction databases
STRING	P20431.
Proteomic databases
PRIDE	P20431.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT5G57350.1; AT5G57350.1; AT5G57350. AT5G57350.2; AT5G57350.2; AT5G57350.
GeneID	835841.
GenomeReviews	Gene locus AT5G57350 in contig BA000015_GR.
KEGG	ath:AT5G57350.
NMPDR	fig\|3702.1.peg.27687.
Organism-specific databases
TAIR	At5g57350.
Phylogenomic databases
eggNOG	KOG0205.
HOGENOM	HBG706356.
InParanoid	P20431.
OMA	NIAKEMA.
PhylomeDB	P20431.
Gene expression databases
ArrayExpress	P20431.
Genevestigator	P20431.
GermOnline	AT5G57350. 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

PMA3_ARATH

Accession

Primary (citable) accession number: P20431

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 114 of the entry and version 2 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

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

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