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UniProtKB - P19156 (ATP4A_PIG)

Entry version 182 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Potassium-transporting ATPase alpha chain 1

Gene

ATP4A

Organism
Sus scrofa (Pig)
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 catalytic subunit of the gastric H+/K+ ATPase pump which transports H+ ions in exchange for K+ ions across the apical membrane of parietal cells. Uses ATP as an energy source to pump H+ ions to the gastric lumen while transporting K+ ion from the lumen into the cell (By similarity).

Remarkably generates a million-fold proton gradient across the gastric parietal cell membrane, acidifying the gastric juice down to pH 1 (By similarity).

Within a transport cycle, the transfer of a H+ ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing (E1) to outward-facing state (E2). The release of the H+ ion in the stomach lumen is followed by binding of K+ ion converting the pump conformation back to the E1 state (PubMed:29618813, PubMed:31436534, PubMed:30143663, PubMed:19387495).

By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Down-regulated by K+-competitive acid blockers (P-CABs) such as vonoprazan.1 Publication

<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 ATP (ATPase activity)1 Publication
  1. Vmax=4.3 µmol/h/mg enzyme toward ATP (ATPase activity)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi339Potassium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi340Potassium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi342Potassium; via carbonyl oxygenCombined sources1 Publication1
Metal bindingi344PotassiumCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei3864-aspartylphosphate intermediate1 Publication1
Metal bindingi386MagnesiumCombined sources2 Publications1
Metal bindingi388MagnesiumCombined sources2 Publications1
Metal bindingi727MagnesiumCombined sources2 Publications1
Metal bindingi731MagnesiumBy similarity1
Metal bindingi796PotassiumCombined sources1 Publication1
Metal bindingi821PotassiumCombined sources1 Publication1

<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

Complete GO annotation on QuickGO ...

<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, Potassium transport, Transport
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		7.2.2.19, 6170

<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%5Fand%5Ftaxonomy%5Fsection">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:
Potassium-transporting ATPase alpha chain 1 (EC:7.2.2.19By similarity)
Alternative name(s):
Gastric H(+)/K(+) ATPase subunit alpha1 Publication
Proton pump1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ATP4A
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000314985 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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: Unplaced
  • UP000008227 Componenti: Unplaced

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 97CytoplasmicSequence analysisAdd BLAST96
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei98 – 118HelicalSequence analysisAdd BLAST21
Topological domaini119 – 141LumenalSequence analysisAdd BLAST23
Transmembranei142 – 162HelicalSequence analysisAdd BLAST21
Topological domaini163 – 298CytoplasmicSequence analysisAdd BLAST136
Transmembranei299 – 318HelicalSequence analysisAdd BLAST20
Topological domaini319 – 330LumenalSequence analysisAdd BLAST12
Transmembranei331 – 348HelicalSequence analysisAdd BLAST18
Topological domaini349 – 782CytoplasmicSequence analysisAdd BLAST434
Transmembranei783 – 802HelicalSequence analysisAdd BLAST20
Topological domaini803 – 812LumenalSequence analysis10
Transmembranei813 – 833HelicalSequence analysisAdd BLAST21
Topological domaini834 – 853CytoplasmicSequence analysisAdd BLAST20
Transmembranei854 – 876HelicalSequence analysisAdd BLAST23
Topological domaini877 – 928LumenalSequence analysisAdd BLAST52
Transmembranei929 – 948HelicalSequence analysisAdd BLAST20
Topological domaini949 – 962CytoplasmicSequence analysisAdd BLAST14
Transmembranei963 – 981HelicalSequence analysisAdd BLAST19
Topological domaini982 – 996LumenalSequence analysisAdd BLAST15
Transmembranei997 – 1017HelicalSequence analysisAdd BLAST21
Topological domaini1018 – 1034CytoplasmicSequence analysisAdd BLAST17

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi120I → A: Has potassium-independent constitutive ATPase activity. 1 Publication1
Mutagenesisi120I → M: Has normal potassium-dependent ATPase activity. 1 Publication1
Mutagenesisi335M → A: Has potassium-independent constitutive ATPase activity. 1 Publication1
Mutagenesisi335M → I: Has normal potassium-dependent ATPase activity. 1 Publication1
Mutagenesisi344E → D: Loss of ATPase activity. 1 Publication1
Mutagenesisi344E → Q: Reduces potassium-dependent ATPase activity. 2 Publications1
Mutagenesisi796E → D: Reduces potassium-dependent ATPase activity. 1 Publication1
Mutagenesisi796E → Q: Has normal potassium-dependent ATPase activity. 2 Publications1
Mutagenesisi800Y → W: Has constitutive ATPase activity that decreases in the presence of potassium ions. Has potassium-dependent ATPase activity; when associated with S-804. Has weak potassium-dependent ATPase activity; when associated with G-812. 1 Publication1
Mutagenesisi804I → S: Has potassium-dependent ATPase activity; when associated with W-800. 1 Publication1
Mutagenesisi812L → G: Inactive due to impaired folding. Has weak potassium-dependent ATPase activity; when associated with W-800. 1 Publication1
Mutagenesisi821E → D: Has normal potassium-dependent ATPase activity. 1 Publication1
Mutagenesisi821E → Q: Has potassium-independent constitutive ATPase activity. 2 Publications1
Mutagenesisi825D → E: Reduces potassium-dependent ATPase activity. 1 Publication1
Mutagenesisi825D → N: Reduces potassium-dependent ATPase activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3919

DrugCentral

More...DrugCentrali		P19156

<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%5Fprocessing%5Fsection">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 methionineiRemoved2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000462552 – 1034Potassium-transporting ATPase alpha chain 1Add BLAST1033

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 residuei7Phosphotyrosine1 Publication1
Modified residuei10Phosphotyrosine1 Publication1
Modified residuei27Phosphoserine; by PKA and PKC1 Publication1
Modified residuei462PhosphoserineBy similarity1
Modified residuei600PhosphoserineBy similarity1
Modified residuei839PhosphoserineBy similarity1
Modified residuei953Phosphoserine; by PKABy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...PaxDbi		P19156

PeptideAtlas

More...PeptideAtlasi		P19156

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P19156

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The gastric H+/K+ ATPase pump is composed of the catalytic alpha subunit ATP4A and the regulatory beta subunit ATP4B (PubMed:29618813, PubMed:19387495, PubMed:21224846).

Interacts (via the P-domain) with ATP4B (via N-terminus); this interaction stabilizes the lumenal-open E2 conformation state and prevents the reverse reaction of the transport cycle (PubMed:19387495).

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-2195, Hydrogen:potassium-exchanging ATPase complex

Protein interaction database and analysis system

More...IntActi		P19156, 2 interactors

Molecular INTeraction database

More...MINTi		P19156

STRING: functional protein association networks

More...STRINGi		9823.ENSSSCP00000003126

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P19156

<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

11034
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P19156

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P19156

<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>Regioni13 – 40DisorderedSequence analysisAdd BLAST28
Regioni222 – 244DisorderedSequence analysisAdd BLAST23

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi222 – 242Polar residuesSequence analysisAdd BLAST21

<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

Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IIC subfamily. [View classification]Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0203, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P19156

Database of Orthologous Groups

More...OrthoDBi		388324at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd02608, P-type_ATPase_Na-K_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.1110.10, 1 hit
3.40.50.1000, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006068, ATPase_P-typ_cation-transptr_C
IPR004014, ATPase_P-typ_cation-transptr_N
IPR023299, ATPase_P-typ_cyto_dom_N
IPR015127, ATPase_P-typ_H/K-transp_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
IPR023214, HAD_sf
IPR005775, P-type_ATPase_IIC
IPR001757, P_typ_ATPase
IPR044492, P_typ_ATPase_HD_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00689, Cation_ATPase_C, 1 hit
PF00690, Cation_ATPase_N, 1 hit
PF09040, H-K_ATPase_N, 1 hit

Structure-Function Linkage Database

More...SFLDi		SFLDF00027, p-type_atpase, 1 hit

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
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01106, ATPase-IIC_X-K, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P19156-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGKAENYELY QVELGPGPSG DMAAKMSKKK AGRGGGKRKE KLENMKKEME 
        60         70         80         90        100
INDHQLSVAE LEQKYQTSAT KGLSASLAAE LLLRDGPNAL RPPRGTPEYV 
       110        120        130        140        150
KFARQLAGGL QCLMWVAAAI CLIAFAIQAS EGDLTTDDNL YLALALIAVV 
       160        170        180        190        200
VVTGCFGYYQ EFKSTNIIAS FKNLVPQQAT VIRDGDKFQI NADQLVVGDL 
       210        220        230        240        250
VEMKGGDRVP ADIRILQAQG RKVDNSSLTG ESEPQTRSPE CTHESPLETR 
       260        270        280        290        300
NIAFFSTMCL EGTAQGLVVN TGDRTIIGRI ASLASGVENE KTPIAIEIEH 
       310        320        330        340        350
FVDIIAGLAI LFGATFFIVA MCIGYTFLRA MVFFMAIVVA YVPEGLLATV 
       360        370        380        390        400
TVCLSLTAKR LASKNCVVKN LEAVETLGST SVICSDKTGT LTQNRMTVSH 
       410        420        430        440        450
LWFDNHIHSA DTTEDQSGQT FDQSSETWRA LCRVLTLCNR AAFKSGQDAV 
       460        470        480        490        500
PVPKRIVIGD ASETALLKFS ELTLGNAMGY RERFPKVCEI PFNSTNKFQL 
       510        520        530        540        550
SIHTLEDPRD PRHVLVMKGA PERVLERCSS ILIKGQELPL DEQWREAFQT 
       560        570        580        590        600
AYLSLGGLGE RVLGFCQLYL SEKDYPPGYA FDVEAMNFPT SGLSFAGLVS 
       610        620        630        640        650
MIDPPRATVP DAVLKCRTAG IRVIMVTGDH PITAKAIAAS VGIISEGSET 
       660        670        680        690        700
VEDIAARLRV PVDQVNRKDA RACVINGMQL KDMDPSELVE ALRTHPEMVF 
       710        720        730        740        750
ARTSPQQKLV IVESCQRLGA IVAVTGDGVN DSPALKKADI GVAMGIAGSD 
       760        770        780        790        800
AAKNAADMIL LDDNFASIVT GVEQGRLIFD NLKKSIAYTL TKNIPELTPY 
       810        820        830        840        850
LIYITVSVPL PLGCITILFI ELCTDIFPSV SLAYEKAESD IMHLRPRNPK 
       860        870        880        890        900
RDRLVNEPLA AYSYFQIGAI QSFAGFTDYF TAMAQEGWFP LLCVGLRPQW 
       910        920        930        940        950
ENHHLQDLQD SYGQEWTFGQ RLYQQYTCYT VFFISIEMCQ IADVLIRKTR 
       960        970        980        990       1000
RLSAFQQGFF RNRILVIAIV FQVCIGCFLC YCPGMPNIFN FMPIRFQWWL 
      1010       1020       1030 
VPMPFGLLIF VYDEIRKLGV RCCPGSWWDQ ELYY
Length:1,034
Mass (Da):114,287
Last modified:January 23, 2007 - v3
<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:i97077AC0ADEA8DDE
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2G → Y AA sequence (PubMed:3017315).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M22724 mRNA Translation: AAA31003.1

Protein sequence database of the Protein Information Resource

More...PIRi		A31671

NCBI Reference Sequences

More...RefSeqi		NP_999456.1, NM_214291.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		397552

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ssc:397552

<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
M22724 mRNA Translation: AAA31003.1
PIRiA31671
RefSeqiNP_999456.1, NM_214291.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IWCNMR-A1-34[»]
1IWFNMR-A1-34[»]
2XZBelectron microscopy7.00A1-1034[»]
2YN9electron microscopy8.00A1-1034[»]
3IXZelectron microscopy6.50A1-1034[»]
4UX1electron microscopy8.00A1-1034[»]
4UX2electron microscopy7.00A1-1034[»]
5Y0Belectron microscopy6.70A1-1034[»]
5YLUX-ray2.80A1-1034[»]
5YLVX-ray2.80A1-1034[»]
6JXHX-ray2.50A49-1034[»]
6JXIX-ray2.60A49-1034[»]
6JXJX-ray2.50A49-1034[»]
6JXKX-ray4.30A/E49-1034[»]
SMRiP19156
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2195, Hydrogen:potassium-exchanging ATPase complex
IntActiP19156, 2 interactors
MINTiP19156
STRINGi9823.ENSSSCP00000003126

Chemistry databases

BindingDBiP19156
ChEMBLiCHEMBL3919
DrugCentraliP19156

PTM databases

iPTMnetiP19156

Proteomic databases

PaxDbiP19156
PeptideAtlasiP19156

Genome annotation databases

GeneIDi397552
KEGGissc:397552

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		495

Phylogenomic databases

eggNOGiKOG0203, Eukaryota
InParanoidiP19156
OrthoDBi388324at2759

Enzyme and pathway databases

BRENDAi7.2.2.19, 6170

Miscellaneous databases

EvolutionaryTraceiP19156

Protein Ontology

More...PROi		PR:P19156

Family and domain databases

CDDicd02608, P-type_ATPase_Na-K_like, 1 hit
Gene3Di3.40.1110.10, 1 hit
3.40.50.1000, 1 hit
InterProiView protein in InterPro
IPR006068, ATPase_P-typ_cation-transptr_C
IPR004014, ATPase_P-typ_cation-transptr_N
IPR023299, ATPase_P-typ_cyto_dom_N
IPR015127, ATPase_P-typ_H/K-transp_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
IPR023214, HAD_sf
IPR005775, P-type_ATPase_IIC
IPR001757, P_typ_ATPase
IPR044492, P_typ_ATPase_HD_dom
PfamiView protein in Pfam
PF00689, Cation_ATPase_C, 1 hit
PF00690, Cation_ATPase_N, 1 hit
PF09040, H-K_ATPase_N, 1 hit
SFLDiSFLDF00027, p-type_atpase, 1 hit
SMARTiView protein in SMART
SM00831, Cation_ATPase_N, 1 hit
SUPFAMiSSF56784, SSF56784, 1 hit
SSF81653, SSF81653, 1 hit
SSF81660, SSF81660, 1 hit
SSF81665, SSF81665, 1 hit
TIGRFAMsiTIGR01106, ATPase-IIC_X-K, 1 hit
TIGR01494, ATPase_P-type, 2 hits
PROSITEiView protein in PROSITE
PS00154, ATPASE_E1_E2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiATP4A_PIG
<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: P19156
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 182 of the entry and version 3 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 programChordata 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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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