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Protein

ATPase 2, plasma membrane-type

Gene

AHA2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

The plasma membrane H+ ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H+-symport (PubMed:10748244, PubMed:12920605, PubMed:27013734). The resulting external acidification and/or internal alkinization may mediate growth responses (PubMed:10748244, PubMed:12920605). Involved in maintaining the membrane potential and delta-pH, together forming the plasma membrane protonmotive force (PMF) required for root and hypocotyl elongation and root tropism (PubMed:22214817, PubMed:24492258). Important for root growth and development during different nitrogen regimes (PubMed:25382626). Forms a functional cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes (PubMed:26071421).1 Publication6 Publications

Miscellaneous

The catalytic mechanism involves at least four different enzyme conformational states named E1, E1P, E2P, and E2, with the E1P-E2P transition accompanying the transfer of ion across the membrane. E1P and E2P are phosphorylated intermediates.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by an auto-inhibitory C-terminal domain that can be displaced by phosphorylation of Thr-947 and the subsequent binding of 14-3-3 proteins (PubMed:10353834). Negatively regulated by PKS5 (PubMed:17483306). PKS5 phosphorylates Ser-931, inhibiting interaction with the activating 14-3-3 protein (PubMed:17483306). Positively regulated by PSY1R (PubMed:25267325). PSY1R phosphorylates Thr-881, situated in the auto-inhibitory region I of the C-terminal domain, causing pump activation (PubMed:25267325). Negatively regulated by the secreted peptide RALF (PubMed:24458638). After specific binding to FERONIA, RALF causes phosphorylation at Ser-899, mediating the inhibition of proton transport (PubMed:24458638). Activated by lysophospholipids, without the involvement of phosphorylation of Thr-947 (PubMed:25971968). This activation is critically dependent on the single autoinhibitory residue Leu-919 (PubMed:25971968).6 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=1.2 mM for ATP1 Publication
  1. Vmax=0.87 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei3294-aspartylphosphate intermediateBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi588MagnesiumBy similarity1
Metal bindingi592MagnesiumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTranslocase
Biological processHydrogen ion transport, Ion transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
ARA:AT4G30190-MONOMER
MetaCyc:AT4G30190-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.6.3.6 399

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P19456

Protein family/group databases

Transport Classification Database

More...
TCDBi
3.A.3.3.9 the p-type atpase (p-atpase) superfamily

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
ATPase 2, plasma membrane-type1 Publication (EC:7.1.2.1Curated)
Alternative name(s):
Proton pump 2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:AHA21 Publication
Ordered Locus Names:At4g30190Imported
ORF Names:F9N11.40Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiArabidopsis thaliana (Mouse-ear cress)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3702 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006548 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Arabidopsis Information Portal

More...
Araporti
AT4G30190

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 61CytoplasmicSequence analysisAdd BLAST60
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei62 – 81Helical; Name=1Sequence analysisAdd BLAST20
Topological domaini82 – 93ExtracellularSequence analysisAdd BLAST12
Transmembranei94 – 114Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini115 – 243CytoplasmicSequence analysisAdd BLAST129
Transmembranei244 – 264Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini265 – 273ExtracellularSequence analysis9
Transmembranei274 – 291Helical; Name=4Sequence analysisAdd BLAST18
Topological domaini292 – 643CytoplasmicSequence analysisAdd BLAST352
Transmembranei644 – 665Helical; Name=5Sequence analysisAdd BLAST22
Topological domaini666 – 670ExtracellularSequence analysis5
Transmembranei671 – 693Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini694 – 709CytoplasmicSequence analysisAdd BLAST16
Transmembranei710 – 730Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini731 – 751ExtracellularSequence analysisAdd BLAST21
Transmembranei752 – 772Helical; Name=8Sequence analysisAdd BLAST21
Topological domaini773 – 784CytoplasmicSequence analysisAdd BLAST12
Transmembranei785 – 805Helical; Name=9Sequence analysisAdd BLAST21
Topological domaini806 – 813ExtracellularSequence analysis8
Transmembranei814 – 834Helical; Name=10Sequence analysisAdd BLAST21
Topological domaini835 – 948CytoplasmicSequence analysisAdd BLAST114

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

No visible phenotype under normal growth conditions, due to the redudancy with AHA1. Aha1 and aha2 double mutants are embryo lethal.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi106N → A, D, K, Q or T: Reduced proton transport. 1 Publication1
Mutagenesisi655R → A or D: No effect on ATP affinity, but reduced proton transport. 1 Publication1
Mutagenesisi655R → K: No effect on ATP affinity and proton transport. 1 Publication1
Mutagenesisi684D → A, V or R: No effect on ATP affinity, but loss of proton transport. 1 Publication1
Mutagenesisi684D → E: No effect on ATP affinity, but reduced proton transport. 1 Publication1
Mutagenesisi684D → N: Insensitive to the inhibitor vanadate and locked in the E1 conformation. No effect on ATP hydrolysis, but loss of proton transport. 2 Publications1
Mutagenesisi881T → A: Decreased phosphorylation by PSY1R. 1 Publication1
Mutagenesisi881T → D: No effect on 14-3-3 protein binding, but increased activity. 1 Publication1
Mutagenesisi904S → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi919L → A: Loss of activation by lysophospholipids. 1 Publication1
Mutagenesisi922L → A: Increased activation by lysophospholipids. 1 Publication1
Mutagenesisi924T → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi931S → A: Loss of phosphorylation and increased 14-3-3 protein binding. 1 Publication1
Mutagenesisi931S → D: Loss of interaction with 14-3-3 protein. 1 Publication1
Mutagenesisi942T → A: No effect on phosphorylation. 1 Publication1
Mutagenesisi947T → A: No effect on phosphorylation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000462752 – 948ATPase 2, plasma membrane-typeAdd BLAST947

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
Modified residuei881Phosphothreonine1 Publication1
Modified residuei899Phosphoserine1 Publication1
Modified residuei931Phosphoserine; by CIPK111 Publication1
Modified residuei947Phosphothreonine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Thr-881 by PSY1R (PubMed:17651370, PubMed:25267325). This phosphorylation activates proton pumping (PubMed:25267325). Decreased phosphorylation in response to flg22 elicitation (PubMed:17651370).2 Publications
Phosphorylation at Ser-899 is specifically induced by RALF1, thus leading to the inhibition of proton transport (PubMed:24458638). Increased phosphorylation in response to flg22 elicitation (PubMed:17651370).2 Publications
Phosphorylation of Thr-947 induces the binding to 14-3-3 proteins, but phosphorylation of Ser-931 interfers with this binding no matter whether Thr-947 is phosphorylated or not (PubMed:10593986, PubMed:17483306). Decreased phosphorylation in response to flg22 elicitation (PubMed:17651370).3 Publications
Abscisic acid induces dephosphorylation of AHA2 in etiolated seedlings, suppressing ATP hydrolysis and hypocotyl elongation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P19456

PRoteomics IDEntifications database

More...
PRIDEi
P19456

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P19456

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Higher levels in roots than in shoots (PubMed:2143186). Expressed in epidermal and root cortex cells, in phloem, xylem and root hairs (PubMed:17483306). Detected in cotyledons, hypocotyls, roots and root hairs (PubMed:25267325).3 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed on the surface of developing seeds and up to the early globular stage of embryo development.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated by low nitrate conditions.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P19456 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P19456 AT

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Binds to 14-3-3 proteins (PubMed:10593986). The binding is induced by phosphorylation of Thr-947 and it activates the H+-ATPase (PubMed:10593986). Interacts (via the R-domain) with PSY1R (via C-terminus) (PubMed:25267325). Part of a functional complex containing PSKR1, BAK1, CNGC17, and AHA (PubMed:26071421). Interacts with CNGC17 and PSKR1 (PubMed:26071421).3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
CIPK11O229323EBI-2293350,EBI-537638

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
14429, 43 interactors

Protein interaction database and analysis system

More...
IntActi
P19456, 30 interactors

STRING: functional protein association networks

More...
STRINGi
3702.AT4G30190.2

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1948
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P19456

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P19456

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P19456

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni946 – 948Interaction with 14-3-3 proteins3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminus contains a R-domain composed of 2 autoinhibitory regions (863-885 and 904-919).1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0205 Eukaryota
COG0474 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000160005

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P19456

KEGG Orthology (KO)

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KOi
K01535

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P19456

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02076 P-type_ATPase_H, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1110.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR006534 P-type_ATPase_IIIA
IPR001757 P_typ_ATPase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00690 Cation_ATPase_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00120 HATPASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00831 Cation_ATPase_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01647 ATPase-IIIA_H, 1 hit
TIGR01494 ATPase_P-type, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoform i produced by alternative splicing. AlignAdd to basket
Note: A number of isoforms are produced. According to EST sequences.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P19456-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
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MSSLEDIKNE TVDLEKIPIE EVFQQLKCSR EGLTTQEGED RIQIFGPNKL
60 70 80 90 100
EEKKESKLLK FLGFMWNPLS WVMEMAAIMA IALANGDGRP PDWQDFVGII
110 120 130 140 150
CLLVINSTIS FIEENNAGNA AAALMAGLAP KTKVLRDGKW SEQEAAILVP
160 170 180 190 200
GDIVSIKLGD IIPADARLLE GDPLKVDQSA LTGESLPVTK HPGQEVFSGS
210 220 230 240 250
TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQKVL TAIGNFCICS
260 270 280 290 300
IAIGMVIEII VMYPIQRRKY RDGIDNLLVL LIGGIPIAMP TVLSVTMAIG
310 320 330 340 350
SHRLSQQGAI TKRMTAIEEM AGMDVLCSDK TGTLTLNKLS VDKNLVEVFC
360 370 380 390 400
KGVEKDQVLL FAAMASRVEN QDAIDAAMVG MLADPKEARA GIREVHFLPF
410 420 430 440 450
NPVDKRTALT YIDGSGNWHR VSKGAPEQIL ELAKASNDLS KKVLSIIDKY
460 470 480 490 500
AERGLRSLAV ARQVVPEKTK ESPGAPWEFV GLLPLFDPPR HDSAETIRRA
510 520 530 540 550
LNLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGT HKDANLASIP
560 570 580 590 600
VEELIEKADG FAGVFPEHKY EIVKKLQERK HIVGMTGDGV NDAPALKKAD
610 620 630 640 650
IGIAVADATD AARGASDIVL TEPGLSVIIS AVLTSRAIFQ RMKNYTIYAV
660 670 680 690 700
SITIRIVFGF MLIALIWEFD FSAFMVLIIA ILNDGTIMTI SKDRVKPSPT
710 720 730 740 750
PDSWKLKEIF ATGVVLGGYQ AIMTVIFFWA AHKTDFFSDT FGVRSIRDNN
760 770 780 790 800
HELMGAVYLQ VSIISQALIF VTRSRSWSFV ERPGALLMIA FLIAQLIATL
810 820 830 840 850
IAVYANWEFA KIRGIGWGWA GVIWLYSIVT YFPLDVFKFA IRYILSGKAW
860 870 880 890 900
LNLFENKTAF TMKKDYGKEE REAQWALAQR TLHGLQPKEA VNIFPEKGSY
910 920 930 940
RELSEIAEQA KRRAEIARLR ELHTLKGHVE SVVKLKGLDI ETPSHYTV
Length:948
Mass (Da):104,401
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i431F4021E99A3CEC
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F4JPJ7F4JPJ7_ARATH
Plasma membrane ATPase
HA2 AHA2, H(+)-ATPase 2, P-TYPE H(+)-ATPASE ISOFORM 2, PMA2, At4g30190
981Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J05570 Genomic DNA Translation: AAA32751.1
AL109796 Genomic DNA Translation: CAB52463.1
AL161576 Genomic DNA Translation: CAB81012.1
CP002687 Genomic DNA Translation: AEE85731.1
AY035075 mRNA Translation: AAK59580.1
BT000781 mRNA Translation: AAN31920.1
BT001969 mRNA Translation: AAN71968.1

Protein sequence database of the Protein Information Resource

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PIRi
A37116 PXMUP2

NCBI Reference Sequences

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RefSeqi
NP_194748.1, NM_119165.4 [P19456-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
At.23014

Genome annotation databases

Ensembl plant genome annotation project

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EnsemblPlantsi
AT4G30190.1; AT4G30190.1; AT4G30190 [P19456-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
829142

Gramene; a comparative resource for plants

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Gramenei
AT4G30190.1; AT4G30190.1; AT4G30190 [P19456-1]

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
ath:AT4G30190

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05570 Genomic DNA Translation: AAA32751.1
AL109796 Genomic DNA Translation: CAB52463.1
AL161576 Genomic DNA Translation: CAB81012.1
CP002687 Genomic DNA Translation: AEE85731.1
AY035075 mRNA Translation: AAK59580.1
BT000781 mRNA Translation: AAN31920.1
BT001969 mRNA Translation: AAN71968.1
PIRiA37116 PXMUP2
RefSeqiNP_194748.1, NM_119165.4 [P19456-1]
UniGeneiAt.23014

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KSDX-ray3.50A/B12-844[»]
ProteinModelPortaliP19456
SMRiP19456
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14429, 43 interactors
IntActiP19456, 30 interactors
STRINGi3702.AT4G30190.2

Protein family/group databases

TCDBi3.A.3.3.9 the p-type atpase (p-atpase) superfamily

PTM databases

iPTMnetiP19456

Proteomic databases

PaxDbiP19456
PRIDEiP19456

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G30190.1; AT4G30190.1; AT4G30190 [P19456-1]
GeneIDi829142
GrameneiAT4G30190.1; AT4G30190.1; AT4G30190 [P19456-1]
KEGGiath:AT4G30190

Organism-specific databases

AraportiAT4G30190

Phylogenomic databases

eggNOGiKOG0205 Eukaryota
COG0474 LUCA
HOGENOMiHOG000160005
InParanoidiP19456
KOiK01535
PhylomeDBiP19456

Enzyme and pathway databases

BioCyciARA:AT4G30190-MONOMER
MetaCyc:AT4G30190-MONOMER
BRENDAi3.6.3.6 399
SABIO-RKiP19456

Miscellaneous databases

EvolutionaryTraceiP19456

Protein Ontology

More...
PROi
PR:P19456

Gene expression databases

ExpressionAtlasiP19456 baseline and differential
GenevisibleiP19456 AT

Family and domain databases

CDDicd02076 P-type_ATPase_H, 1 hit
Gene3Di3.40.1110.10, 1 hit
InterProiView protein in InterPro
IPR004014 ATPase_P-typ_cation-transptr_N
IPR023299 ATPase_P-typ_cyto_dom_N
IPR018303 ATPase_P-typ_P_site
IPR023298 ATPase_P-typ_TM_dom_sf
IPR008250 ATPase_P-typ_transduc_dom_A_sf
IPR036412 HAD-like_sf
IPR006534 P-type_ATPase_IIIA
IPR001757 P_typ_ATPase
PfamiView protein in Pfam
PF00690 Cation_ATPase_N, 1 hit
PRINTSiPR00120 HATPASE
SMARTiView protein in SMART
SM00831 Cation_ATPase_N, 1 hit
SUPFAMiSSF56784 SSF56784, 1 hit
SSF81653 SSF81653, 1 hit
SSF81665 SSF81665, 1 hit
TIGRFAMsiTIGR01647 ATPase-IIIA_H, 1 hit
TIGR01494 ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154 ATPASE_E1_E2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPMA2_ARATH
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19456
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: December 5, 2018
This is version 181 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
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