ID ATP4A_PIG Reviewed; 1034 AA.
AC P19156;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 24-JAN-2024, entry version 191.
DE RecName: Full=Potassium-transporting ATPase alpha chain 1;
DE EC=7.2.2.19 {ECO:0000250|UniProtKB:P09626};
DE AltName: Full=Gastric H(+)/K(+) ATPase subunit alpha {ECO:0000303|PubMed:3017315};
DE AltName: Full=Proton pump {ECO:0000303|PubMed:29618813};
GN Name=ATP4A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2848518; DOI=10.1016/s0006-291x(88)80033-0;
RA Maeda M., Ishizaki J., Futai M.;
RT "cDNA cloning and sequence determination of pig gastric (H+ + K+)-ATPase.";
RL Biochem. Biophys. Res. Commun. 157:203-209(1988).
RN [2]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=3017315; DOI=10.1016/0006-291x(86)90264-0;
RA Lane L.K., Kirley T.L., Ball W.J. Jr.;
RT "Structural studies on H+,K+-ATPase: determination of the NH2-terminal
RT amino acid sequence and immunological cross-reactivity with Na+,K+-
RT ATPase.";
RL Biochem. Biophys. Res. Commun. 138:185-192(1986).
RN [3]
RP ACTIVE SITE ASP-386.
RX PubMed=1720615; DOI=10.1042/bj2800243;
RA Van Uem T.J., Swarts H.G., De Pont J.J.;
RT "Determination of the epitope for the inhibitory monoclonal antibody 5-B6
RT on the catalytic subunit of gastric Mg(2+)-dependent H(+)-transporting and
RT K(+)-stimulated ATPase.";
RL Biochem. J. 280:243-248(1991).
RN [4]
RP PHOSPHORYLATION AT TYR-7 AND TYR-10.
RX PubMed=7797539; DOI=10.1074/jbc.270.26.15475;
RA Togawa K., Ishiguro T., Kaya S., Shimada A., Imagawa T., Taniguchi K.;
RT "Reversible phosphorylation of both Tyr7 and Tyr10 in the alpha-chain of
RT pig stomach H+,K(+)-ATPase by a membrane-bound kinase and a phosphatase.";
RL J. Biol. Chem. 270:15475-15478(1995).
RN [5]
RP PROTEIN SEQUENCE OF 2-11, AND PHOSPHORYLATION AT SER-27.
RX PubMed=8886014; DOI=10.1006/bbrc.1996.1589;
RA Togawa K., Kaya S., Shimada A., Imagawa T., Maardh S., Corbin J.,
RA Kikkawa U., Taniguchi K.;
RT "Ser-27, Tyr-10 and Tyr-7 in the alpha-chain of pig stomach H+,K(+)-ATPase
RT as Ca(2+)-dependent phosphorylatable sites by intrinsic and extrinsic
RT protein kinases.";
RL Biochem. Biophys. Res. Commun. 227:810-815(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLU-344; GLU-796 AND
RP GLU-821.
RX PubMed=30143663; DOI=10.1038/s41598-018-30885-w;
RA Dubey V., Han M., Kopec W., Solov'yov I.A., Abe K., Khandelia H.;
RT "K+ binding and proton redistribution in the E2P state of the H+, K+-
RT ATPase.";
RL Sci. Rep. 8:12732-12732(2018).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.50 ANGSTROMS), FUNCTION, CATALYTIC
RP ACTIVITY, AND INTERACTION WITH ATP4B.
RX PubMed=19387495; DOI=10.1038/emboj.2009.102;
RA Abe K., Tani K., Nishizawa T., Fujiyoshi Y.;
RT "Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse
RT reaction of the transport cycle.";
RL EMBO J. 28:1637-1643(2009).
RN [8]
RP STRUCTURE BY ELECTRON MICROSCOPY (7.0 ANGSTROMS) IN COMPLEX WITH ATP4B AND
RP INHIBITOR, AND SUBCELLULAR LOCATION.
RX PubMed=21224846; DOI=10.1038/ncomms1154;
RA Abe K., Tani K., Fujiyoshi Y.;
RT "Conformational rearrangement of gastric H(+),K(+)-ATPase induced by an
RT acid suppressant.";
RL Nat. Commun. 2:155-155(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ATP4B; MAGNESIUM AND
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND MUTAGENESIS OF ILE-120; MET-335; GLU-344; GLU-796;
RP GLU-821 AND ASP-825.
RX PubMed=29618813; DOI=10.1038/s41586-018-0003-8;
RA Abe K., Irie K., Nakanishi H., Suzuki H., Fujiyoshi Y.;
RT "Crystal structures of the gastric proton pump.";
RL Nature 556:214-218(2018).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 49-1034 IN COMPLEX WITH POTASSIUM
RP AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP TYR-800; ILE-804 AND LEU-812.
RX PubMed=31436534; DOI=10.7554/elife.47701;
RA Yamamoto K., Dubey V., Irie K., Nakanishi H., Khandelia H., Fujiyoshi Y.,
RA Abe K.;
RT "A single K(+)-binding site in the crystal structure of the gastric proton
RT pump.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: The catalytic subunit of the gastric H(+)/K(+) ATPase pump
CC which transports H(+) ions in exchange for K(+) ions across the apical
CC membrane of parietal cells. Uses ATP as an energy source to pump H(+)
CC ions to the gastric lumen while transporting K(+) ion from the lumen
CC into the cell (By similarity). Remarkably generates a million-fold
CC proton gradient across the gastric parietal cell membrane, acidifying
CC the gastric juice down to pH 1 (By similarity). Within a transport
CC cycle, the transfer of a H(+) ion across the membrane is coupled to ATP
CC hydrolysis and is associated with a transient phosphorylation that
CC shifts the pump conformation from inward-facing (E1) to outward-facing
CC state (E2). The release of the H(+) ion in the stomach lumen is
CC followed by binding of K(+) ion converting the pump conformation back
CC to the E1 state (PubMed:29618813, PubMed:31436534, PubMed:30143663,
CC PubMed:19387495). {ECO:0000250|UniProtKB:P09626,
CC ECO:0000250|UniProtKB:Q64436, ECO:0000269|PubMed:19387495,
CC ECO:0000269|PubMed:29618813, ECO:0000269|PubMed:30143663,
CC ECO:0000269|PubMed:31436534}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) +
CC K(+)(in) + phosphate; Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19;
CC Evidence={ECO:0000250|UniProtKB:P09626, ECO:0000305|PubMed:19387495,
CC ECO:0000305|PubMed:29618813, ECO:0000305|PubMed:30143663,
CC ECO:0000305|PubMed:31436534};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
CC Evidence={ECO:0000250|UniProtKB:P09626};
CC -!- ACTIVITY REGULATION: Down-regulated by K(+)-competitive acid blockers
CC (P-CABs) such as vonoprazan. {ECO:0000269|PubMed:29618813}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for ATP (ATPase activity) {ECO:0000269|PubMed:29618813};
CC Vmax=4.3 umol/h/mg enzyme toward ATP (ATPase activity)
CC {ECO:0000269|PubMed:29618813};
CC -!- SUBUNIT: The gastric H(+)/K(+) ATPase pump is composed of the catalytic
CC alpha subunit ATP4A and the regulatory beta subunit ATP4B
CC (PubMed:29618813, PubMed:19387495, PubMed:21224846). Interacts (via the
CC P-domain) with ATP4B (via N-terminus); this interaction stabilizes the
CC lumenal-open E2 conformation state and prevents the reverse reaction of
CC the transport cycle (PubMed:19387495). {ECO:0000269|PubMed:19387495,
CC ECO:0000269|PubMed:21224846, ECO:0000269|PubMed:29618813}.
CC -!- INTERACTION:
CC P19156; P18434: ATP4B; NbExp=2; IntAct=EBI-8803609, EBI-9009115;
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P20648}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21224846}; Multi-pass
CC membrane protein. Note=Localized in the apical canalicular membrane of
CC parietal cells. {ECO:0000250|UniProtKB:P20648}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; M22724; AAA31003.1; -; mRNA.
DR PIR; A31671; A31671.
DR RefSeq; NP_999456.1; NM_214291.1.
DR PDB; 1IWC; NMR; -; A=1-34.
DR PDB; 1IWF; NMR; -; A=1-34.
DR PDB; 2XZB; EM; 7.00 A; A=1-1034.
DR PDB; 2YN9; EM; 8.00 A; A=1-1034.
DR PDB; 3IXZ; EM; 6.50 A; A=1-1034.
DR PDB; 4UX1; EM; 8.00 A; A=1-1034.
DR PDB; 4UX2; EM; 7.00 A; A=1-1034.
DR PDB; 5Y0B; EM; 6.70 A; A=1-1034.
DR PDB; 5YLU; X-ray; 2.80 A; A=1-1034.
DR PDB; 5YLV; X-ray; 2.80 A; A=1-1034.
DR PDB; 6JXH; X-ray; 2.50 A; A=49-1034.
DR PDB; 6JXI; X-ray; 2.60 A; A=49-1034.
DR PDB; 6JXJ; X-ray; 2.50 A; A=49-1034.
DR PDB; 6JXK; X-ray; 4.30 A; A/E=49-1034.
DR PDB; 7EFL; X-ray; 3.40 A; A=49-1034.
DR PDB; 7EFM; X-ray; 3.20 A; A=49-1034.
DR PDB; 7EFN; X-ray; 3.20 A; A=50-1034.
DR PDB; 7ET1; EM; 2.60 A; A=49-1034.
DR PDB; 7W47; X-ray; 3.00 A; A=1-1034.
DR PDB; 7W48; X-ray; 3.50 A; A=1-1034.
DR PDB; 7W49; X-ray; 3.10 A; A=1-1034.
DR PDB; 7W4A; EM; 2.76 A; A=1-1034.
DR PDBsum; 1IWC; -.
DR PDBsum; 1IWF; -.
DR PDBsum; 2XZB; -.
DR PDBsum; 2YN9; -.
DR PDBsum; 3IXZ; -.
DR PDBsum; 4UX1; -.
DR PDBsum; 4UX2; -.
DR PDBsum; 5Y0B; -.
DR PDBsum; 5YLU; -.
DR PDBsum; 5YLV; -.
DR PDBsum; 6JXH; -.
DR PDBsum; 6JXI; -.
DR PDBsum; 6JXJ; -.
DR PDBsum; 6JXK; -.
DR PDBsum; 7EFL; -.
DR PDBsum; 7EFM; -.
DR PDBsum; 7EFN; -.
DR PDBsum; 7ET1; -.
DR PDBsum; 7W47; -.
DR PDBsum; 7W48; -.
DR PDBsum; 7W49; -.
DR PDBsum; 7W4A; -.
DR AlphaFoldDB; P19156; -.
DR EMDB; EMD-1831; -.
DR EMDB; EMD-2759; -.
DR EMDB; EMD-2760; -.
DR EMDB; EMD-31294; -.
DR EMDB; EMD-32299; -.
DR EMDB; EMD-6799; -.
DR SMR; P19156; -.
DR ComplexPortal; CPX-2195; Hydrogen:potassium-exchanging ATPase complex.
DR IntAct; P19156; 2.
DR MINT; P19156; -.
DR STRING; 9823.ENSSSCP00000069966; -.
DR BindingDB; P19156; -.
DR ChEMBL; CHEMBL3919; -.
DR DrugCentral; P19156; -.
DR iPTMnet; P19156; -.
DR PaxDb; 9823-ENSSSCP00000003126; -.
DR PeptideAtlas; P19156; -.
DR GeneID; 397552; -.
DR KEGG; ssc:397552; -.
DR CTD; 495; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; P19156; -.
DR OrthoDB; 203629at2759; -.
DR BRENDA; 7.2.2.19; 6170.
DR EvolutionaryTrace; P19156; -.
DR PRO; PR:P19156; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Proteomes; UP000694570; Unplaced.
DR Proteomes; UP000694571; Unplaced.
DR Proteomes; UP000694720; Unplaced.
DR Proteomes; UP000694722; Unplaced.
DR Proteomes; UP000694723; Unplaced.
DR Proteomes; UP000694724; Unplaced.
DR Proteomes; UP000694725; Unplaced.
DR Proteomes; UP000694726; Unplaced.
DR Proteomes; UP000694727; Unplaced.
DR Proteomes; UP000694728; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005889; C:potassium:proton exchanging ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; IBA:GO_Central.
DR GO; GO:0005391; F:P-type sodium:potassium-exchanging transporter activity; IBA:GO_Central.
DR GO; GO:0030955; F:potassium ion binding; IDA:UniProtKB.
DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR015127; ATPase_P-typ_H/K-transp_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF10; POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 1; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF09040; H-K_ATPase_N; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3017315,
FT ECO:0000269|PubMed:8886014"
FT CHAIN 2..1034
FT /note="Potassium-transporting ATPase alpha chain 1"
FT /id="PRO_0000046255"
FT TOPO_DOM 2..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..141
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..330
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 783..802
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 803..812
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..853
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 854..876
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..928
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 929..948
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 949..962
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..981
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 982..996
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 997..1017
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1018..1034
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 13..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000269|PubMed:1720615"
FT BINDING 339
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:6JXH"
FT BINDING 340
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:6JXH"
FT BINDING 342
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:6JXH"
FT BINDING 344
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:6JXH"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU,
FT ECO:0007744|PDB:6JXH"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU,
FT ECO:0007744|PDB:6JXH"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:31436534, ECO:0007744|PDB:5YLU,
FT ECO:0007744|PDB:6JXH"
FT BINDING 731
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 796
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:6JXH"
FT BINDING 821
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:31436534,
FT ECO:0007744|PDB:6JXH"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:7797539"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:7797539"
FT MOD_RES 27
FT /note="Phosphoserine; by PKA and PKC"
FT /evidence="ECO:0000269|PubMed:8886014"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PIE5"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50993"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09626"
FT MOD_RES 953
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
FT MUTAGEN 120
FT /note="I->A: Has potassium-independent constitutive ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 120
FT /note="I->M: Has normal potassium-dependent ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 335
FT /note="M->A: Has potassium-independent constitutive ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 335
FT /note="M->I: Has normal potassium-dependent ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 344
FT /note="E->D: Loss of ATPase activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 344
FT /note="E->Q: Reduces potassium-dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:30143663"
FT MUTAGEN 796
FT /note="E->D: Reduces potassium-dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 796
FT /note="E->Q: Has normal potassium-dependent ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:30143663"
FT MUTAGEN 800
FT /note="Y->W: Has constitutive ATPase activity that
FT decreases in the presence of potassium ions. Has potassium-
FT dependent ATPase activity; when associated with S-804. Has
FT weak potassium-dependent ATPase activity; when associated
FT with G-812."
FT /evidence="ECO:0000269|PubMed:31436534"
FT MUTAGEN 804
FT /note="I->S: Has potassium-dependent ATPase activity; when
FT associated with W-800."
FT /evidence="ECO:0000269|PubMed:31436534"
FT MUTAGEN 812
FT /note="L->G: Inactive due to impaired folding. Has weak
FT potassium-dependent ATPase activity; when associated with
FT W-800."
FT /evidence="ECO:0000269|PubMed:31436534"
FT MUTAGEN 821
FT /note="E->D: Has normal potassium-dependent ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 821
FT /note="E->Q: Has potassium-independent constitutive ATPase
FT activity."
FT /evidence="ECO:0000269|PubMed:29618813,
FT ECO:0000269|PubMed:30143663"
FT MUTAGEN 825
FT /note="D->E: Reduces potassium-dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT MUTAGEN 825
FT /note="D->N: Reduces potassium-dependent ATPase activity."
FT /evidence="ECO:0000269|PubMed:29618813"
FT CONFLICT 2
FT /note="G -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:1IWC"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1IWC"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:1IWC"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 75..85
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 128..132
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7EFL"
FT HELIX 138..158
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:7ET1"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 200..204
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 211..224
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:7ET1"
FT STRAND 258..270
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 293..322
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 327..341
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 346..363
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 373..376
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 387..391
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:7W49"
FT HELIX 426..437
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 447..449
FT /evidence="ECO:0007829|PDB:6JXJ"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 461..473
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 477..482
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 513..519
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 521..525
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 561..570
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 577..579
FT /evidence="ECO:0007829|PDB:7W4A"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 591..602
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 609..618
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 622..626
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 631..640
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:7ET1"
FT HELIX 651..657
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 671..676
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 677..682
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 685..694
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 696..702
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 705..717
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 722..726
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 729..731
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 732..737
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 738..744
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 745..747
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 750..755
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 767..791
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 793..806
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 814..822
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 823..825
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 826..831
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 832..834
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 841..843
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 849..851
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 857..865
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 867..884
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 885..887
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 890..893
FT /evidence="ECO:0007829|PDB:6JXH"
FT TURN 894..896
FT /evidence="ECO:0007829|PDB:7EFL"
FT HELIX 897..900
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 906..909
FT /evidence="ECO:0007829|PDB:5YLV"
FT HELIX 918..946
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 950..952
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 954..957
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 959..961
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 963..981
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 985..988
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 997..1000
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 1003..1022
FT /evidence="ECO:0007829|PDB:6JXH"
FT STRAND 1024..1026
FT /evidence="ECO:0007829|PDB:6JXH"
FT HELIX 1027..1032
FT /evidence="ECO:0007829|PDB:6JXH"
SQ SEQUENCE 1034 AA; 114287 MW; 97077AC0ADEA8DDE CRC64;
MGKAENYELY QVELGPGPSG DMAAKMSKKK AGRGGGKRKE KLENMKKEME INDHQLSVAE
LEQKYQTSAT KGLSASLAAE LLLRDGPNAL RPPRGTPEYV KFARQLAGGL QCLMWVAAAI
CLIAFAIQAS EGDLTTDDNL YLALALIAVV VVTGCFGYYQ EFKSTNIIAS FKNLVPQQAT
VIRDGDKFQI NADQLVVGDL VEMKGGDRVP ADIRILQAQG RKVDNSSLTG ESEPQTRSPE
CTHESPLETR NIAFFSTMCL EGTAQGLVVN TGDRTIIGRI ASLASGVENE KTPIAIEIEH
FVDIIAGLAI LFGATFFIVA MCIGYTFLRA MVFFMAIVVA YVPEGLLATV TVCLSLTAKR
LASKNCVVKN LEAVETLGST SVICSDKTGT LTQNRMTVSH LWFDNHIHSA DTTEDQSGQT
FDQSSETWRA LCRVLTLCNR AAFKSGQDAV PVPKRIVIGD ASETALLKFS ELTLGNAMGY
RERFPKVCEI PFNSTNKFQL SIHTLEDPRD PRHVLVMKGA PERVLERCSS ILIKGQELPL
DEQWREAFQT AYLSLGGLGE RVLGFCQLYL SEKDYPPGYA FDVEAMNFPT SGLSFAGLVS
MIDPPRATVP DAVLKCRTAG IRVIMVTGDH PITAKAIAAS VGIISEGSET VEDIAARLRV
PVDQVNRKDA RACVINGMQL KDMDPSELVE ALRTHPEMVF ARTSPQQKLV IVESCQRLGA
IVAVTGDGVN DSPALKKADI GVAMGIAGSD AAKNAADMIL LDDNFASIVT GVEQGRLIFD
NLKKSIAYTL TKNIPELTPY LIYITVSVPL PLGCITILFI ELCTDIFPSV SLAYEKAESD
IMHLRPRNPK RDRLVNEPLA AYSYFQIGAI QSFAGFTDYF TAMAQEGWFP LLCVGLRPQW
ENHHLQDLQD SYGQEWTFGQ RLYQQYTCYT VFFISIEMCQ IADVLIRKTR RLSAFQQGFF
RNRILVIAIV FQVCIGCFLC YCPGMPNIFN FMPIRFQWWL VPMPFGLLIF VYDEIRKLGV
RCCPGSWWDQ ELYY
//
