UniProtKB - P19156 (ATP4A_PIG)
Potassium-transporting ATPase alpha chain 1
ATP4A
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 PublicationsCatalytic activityi
Activity regulationi
Kineticsi
- KM=1.2 mM for ATP (ATPase activity)1 Publication
- Vmax=4.3 µmol/h/mg enzyme toward ATP (ATPase activity)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 339 | Potassium; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 340 | Potassium; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 342 | Potassium; via carbonyl oxygenCombined sources1 Publication | 1 | |
Metal bindingi | 344 | PotassiumCombined sources1 Publication | 1 | |
Active sitei | 386 | 4-aspartylphosphate intermediate1 Publication | 1 | |
Metal bindingi | 386 | MagnesiumCombined sources2 Publications | 1 | |
Metal bindingi | 388 | MagnesiumCombined sources2 Publications | 1 | |
Metal bindingi | 727 | MagnesiumCombined sources2 Publications | 1 | |
Metal bindingi | 731 | MagnesiumBy similarity | 1 | |
Metal bindingi | 796 | PotassiumCombined sources1 Publication | 1 | |
Metal bindingi | 821 | PotassiumCombined sources1 Publication | 1 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- magnesium ion binding Source: UniProtKB
- potassium ion binding Source: UniProtKB
- P-type potassium:proton transporter activity Source: UniProtKB-EC
Keywordsi
Molecular function | Translocase |
Biological process | Hydrogen ion transport, Ion transport, Potassium transport, Transport |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Potassium |
Enzyme and pathway databases
BRENDAi | 7.2.2.19, 6170 |
Names & Taxonomyi
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 |
Gene namesi | Name:ATP4A |
Organismi | Sus scrofa (Pig) |
Taxonomic identifieri | 9823 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Suina › Suidae › Sus |
Proteomesi |
|
Subcellular locationi
Plasma membrane
- Apical cell membrane By similarity; Multi-pass membrane protein Sequence analysis
- Cell membrane 1 Publication; Multi-pass membrane protein
Note: Localized in the apical canalicular membrane of parietal cells.By similarity
Plasma Membrane
- apical plasma membrane Source: UniProtKB-SubCell
Other locations
- integral component of membrane Source: UniProtKB-KW
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 2 – 97 | CytoplasmicSequence analysisAdd BLAST | 96 | |
Transmembranei | 98 – 118 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 119 – 141 | LumenalSequence analysisAdd BLAST | 23 | |
Transmembranei | 142 – 162 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 163 – 298 | CytoplasmicSequence analysisAdd BLAST | 136 | |
Transmembranei | 299 – 318 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 319 – 330 | LumenalSequence analysisAdd BLAST | 12 | |
Transmembranei | 331 – 348 | HelicalSequence analysisAdd BLAST | 18 | |
Topological domaini | 349 – 782 | CytoplasmicSequence analysisAdd BLAST | 434 | |
Transmembranei | 783 – 802 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 803 – 812 | LumenalSequence analysis | 10 | |
Transmembranei | 813 – 833 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 834 – 853 | CytoplasmicSequence analysisAdd BLAST | 20 | |
Transmembranei | 854 – 876 | HelicalSequence analysisAdd BLAST | 23 | |
Topological domaini | 877 – 928 | LumenalSequence analysisAdd BLAST | 52 | |
Transmembranei | 929 – 948 | HelicalSequence analysisAdd BLAST | 20 | |
Topological domaini | 949 – 962 | CytoplasmicSequence analysisAdd BLAST | 14 | |
Transmembranei | 963 – 981 | HelicalSequence analysisAdd BLAST | 19 | |
Topological domaini | 982 – 996 | LumenalSequence analysisAdd BLAST | 15 | |
Transmembranei | 997 – 1017 | HelicalSequence analysisAdd BLAST | 21 | |
Topological domaini | 1018 – 1034 | CytoplasmicSequence analysisAdd BLAST | 17 |
Keywords - Cellular componenti
Cell membrane, MembranePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 120 | I → A: Has potassium-independent constitutive ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 120 | I → M: Has normal potassium-dependent ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 335 | M → A: Has potassium-independent constitutive ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 335 | M → I: Has normal potassium-dependent ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 344 | E → D: Loss of ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 344 | E → Q: Reduces potassium-dependent ATPase activity. 2 Publications | 1 | |
Mutagenesisi | 796 | E → D: Reduces potassium-dependent ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 796 | E → Q: Has normal potassium-dependent ATPase activity. 2 Publications | 1 | |
Mutagenesisi | 800 | Y → 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 Publication | 1 | |
Mutagenesisi | 804 | I → S: Has potassium-dependent ATPase activity; when associated with W-800. 1 Publication | 1 | |
Mutagenesisi | 812 | L → G: Inactive due to impaired folding. Has weak potassium-dependent ATPase activity; when associated with W-800. 1 Publication | 1 | |
Mutagenesisi | 821 | E → D: Has normal potassium-dependent ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 821 | E → Q: Has potassium-independent constitutive ATPase activity. 2 Publications | 1 | |
Mutagenesisi | 825 | D → E: Reduces potassium-dependent ATPase activity. 1 Publication | 1 | |
Mutagenesisi | 825 | D → N: Reduces potassium-dependent ATPase activity. 1 Publication | 1 |
Chemistry databases
ChEMBLi | CHEMBL3919 |
DrugCentrali | P19156 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000046255 | 2 – 1034 | Potassium-transporting ATPase alpha chain 1Add BLAST | 1033 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 7 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 10 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 27 | Phosphoserine; by PKA and PKC1 Publication | 1 | |
Modified residuei | 462 | PhosphoserineBy similarity | 1 | |
Modified residuei | 600 | PhosphoserineBy similarity | 1 | |
Modified residuei | 839 | PhosphoserineBy similarity | 1 | |
Modified residuei | 953 | Phosphoserine; by PKABy similarity | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P19156 |
PeptideAtlasi | P19156 |
PTM databases
iPTMneti | P19156 |
Interactioni
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 PublicationsBinary interactionsi
P19156
With | #Exp. | IntAct |
---|---|---|
ATP4B [P18434] | 2 | EBI-8803609,EBI-9009115 |
Protein-protein interaction databases
ComplexPortali | CPX-2195, Hydrogen:potassium-exchanging ATPase complex |
IntActi | P19156, 2 interactors |
MINTi | P19156 |
STRINGi | 9823.ENSSSCP00000003126 |
Chemistry databases
BindingDBi | P19156 |
Structurei
Secondary structure
3D structure databases
SMRi | P19156 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P19156 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 13 – 40 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 222 – 244 | DisorderedSequence analysisAdd BLAST | 23 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 222 – 242 | Polar residuesSequence analysisAdd BLAST | 21 |
Sequence similaritiesi
Keywords - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG0203, Eukaryota |
InParanoidi | P19156 |
OrthoDBi | 388324at2759 |
Family and domain databases
CDDi | cd02608, P-type_ATPase_Na-K_like, 1 hit |
Gene3Di | 3.40.1110.10, 1 hit 3.40.50.1000, 1 hit |
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 |
Pfami | View protein in Pfam PF00689, Cation_ATPase_C, 1 hit PF00690, Cation_ATPase_N, 1 hit PF09040, H-K_ATPase_N, 1 hit |
SFLDi | SFLDF00027, p-type_atpase, 1 hit |
SMARTi | View protein in SMART SM00831, Cation_ATPase_N, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit SSF81653, SSF81653, 1 hit SSF81660, SSF81660, 1 hit SSF81665, SSF81665, 1 hit |
TIGRFAMsi | TIGR01106, ATPase-IIC_X-K, 1 hit TIGR01494, ATPase_P-type, 2 hits |
PROSITEi | View protein in PROSITE PS00154, ATPASE_E1_E2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 2 | G → Y AA sequence (PubMed:3017315).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22724 mRNA Translation: AAA31003.1 |
PIRi | A31671 |
RefSeqi | NP_999456.1, NM_214291.1 |
Genome annotation databases
GeneIDi | 397552 |
KEGGi | ssc:397552 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22724 mRNA Translation: AAA31003.1 |
PIRi | A31671 |
RefSeqi | NP_999456.1, NM_214291.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1IWC | NMR | - | A | 1-34 | [»] | |
1IWF | NMR | - | A | 1-34 | [»] | |
2XZB | electron microscopy | 7.00 | A | 1-1034 | [»] | |
2YN9 | electron microscopy | 8.00 | A | 1-1034 | [»] | |
3IXZ | electron microscopy | 6.50 | A | 1-1034 | [»] | |
4UX1 | electron microscopy | 8.00 | A | 1-1034 | [»] | |
4UX2 | electron microscopy | 7.00 | A | 1-1034 | [»] | |
5Y0B | electron microscopy | 6.70 | A | 1-1034 | [»] | |
5YLU | X-ray | 2.80 | A | 1-1034 | [»] | |
5YLV | X-ray | 2.80 | A | 1-1034 | [»] | |
6JXH | X-ray | 2.50 | A | 49-1034 | [»] | |
6JXI | X-ray | 2.60 | A | 49-1034 | [»] | |
6JXJ | X-ray | 2.50 | A | 49-1034 | [»] | |
6JXK | X-ray | 4.30 | A/E | 49-1034 | [»] | |
SMRi | P19156 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
ComplexPortali | CPX-2195, Hydrogen:potassium-exchanging ATPase complex |
IntActi | P19156, 2 interactors |
MINTi | P19156 |
STRINGi | 9823.ENSSSCP00000003126 |
Chemistry databases
BindingDBi | P19156 |
ChEMBLi | CHEMBL3919 |
DrugCentrali | P19156 |
PTM databases
iPTMneti | P19156 |
Proteomic databases
PaxDbi | P19156 |
PeptideAtlasi | P19156 |
Genome annotation databases
GeneIDi | 397552 |
KEGGi | ssc:397552 |
Organism-specific databases
CTDi | 495 |
Phylogenomic databases
eggNOGi | KOG0203, Eukaryota |
InParanoidi | P19156 |
OrthoDBi | 388324at2759 |
Enzyme and pathway databases
BRENDAi | 7.2.2.19, 6170 |
Miscellaneous databases
EvolutionaryTracei | P19156 |
PROi | PR:P19156 |
Family and domain databases
CDDi | cd02608, P-type_ATPase_Na-K_like, 1 hit |
Gene3Di | 3.40.1110.10, 1 hit 3.40.50.1000, 1 hit |
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 |
Pfami | View protein in Pfam PF00689, Cation_ATPase_C, 1 hit PF00690, Cation_ATPase_N, 1 hit PF09040, H-K_ATPase_N, 1 hit |
SFLDi | SFLDF00027, p-type_atpase, 1 hit |
SMARTi | View protein in SMART SM00831, Cation_ATPase_N, 1 hit |
SUPFAMi | SSF56784, SSF56784, 1 hit SSF81653, SSF81653, 1 hit SSF81660, SSF81660, 1 hit SSF81665, SSF81665, 1 hit |
TIGRFAMsi | TIGR01106, ATPase-IIC_X-K, 1 hit TIGR01494, ATPase_P-type, 2 hits |
PROSITEi | View protein in PROSITE PS00154, ATPASE_E1_E2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATP4A_PIG | |
Accessioni | P19156Primary (citable) accession number: P19156 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families