ATP4A_CANLF
ID ATP4A_CANLF Reviewed; 1034 AA.
AC P50996;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
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;
DE AltName: Full=Proton pump;
GN Name=ATP4A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Stomach;
RX PubMed=8250881; DOI=10.1006/bbrc.1993.2385;
RA Song I., Mortell M.P., Gantz I., Brown D.R., Yamada T.;
RT "Molecular cloning and structural analysis of canine gastric H+,K(+)-
RT ATPase.";
RL Biochem. Biophys. Res. Commun. 196:1240-1247(1993).
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 (By similarity). {ECO:0000250|UniProtKB:P09626,
CC ECO:0000250|UniProtKB:P19156, ECO:0000250|UniProtKB:Q64436}.
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22045;
CC Evidence={ECO:0000250|UniProtKB:P09626};
CC -!- SUBUNIT: The gastric H(+)/K(+) ATPase pump is composed of the catalytic
CC alpha subunit ATP4A and the regulatory beta subunit ATP4B. Interacts
CC (via the P-domain) with ATP4B (via N-terminus); this interaction
CC stabilizes the lumenal-open E2 conformation state and prevents the
CC reverse reaction of the transport cycle.
CC {ECO:0000250|UniProtKB:P19156}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:P20648}; Multi-pass membrane protein
CC {ECO:0000255}. 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; L11568; AAA30848.1; -; mRNA.
DR PIR; JN0903; JN0903.
DR RefSeq; NP_001003342.1; NM_001003342.1.
DR AlphaFoldDB; P50996; -.
DR SMR; P50996; -.
DR STRING; 9612.ENSCAFP00000040362; -.
DR PaxDb; P50996; -.
DR GeneID; 431686; -.
DR KEGG; cfa:431686; -.
DR CTD; 495; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; P50996; -.
DR OrthoDB; 388324at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
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; -; 1.
DR Gene3D; 3.40.50.1000; -; 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 Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF09040; H-K_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Potassium; Potassium transport; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1034
FT /note="Potassium-transporting ATPase alpha chain 1"
FT /id="PRO_0000046252"
FT TOPO_DOM 1..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 14..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 339
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 340
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 342
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 344
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 386
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 388
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT BINDING 727
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P19156"
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:0000250|UniProtKB:P19156"
FT BINDING 821
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 7
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 10
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P19156"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19156"
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"
SQ SEQUENCE 1034 AA; 114106 MW; 452AE1185C0D62E8 CRC64;
MGKAENYEMY SVELGPGPGG DMAAKMSKKK AGKGGGKKKE KLENMKKEME INDHQLSVAE
LEQKYQTSAT KGLSASLAAD LLLRDGPNAL RPPRGTPEYV KFARQLAGGL QCLMWVAAAI
CLIAFAIQAS EGDLTTDDNL YLALALIAVV VVTGCFGYYQ EFKSTNIIAS FKNLVPQQAT
VIRDGDKFQI NADQLVVGDL VEMKGGDRVP ADIRILQAQG CKVDNSSLTG ESEPQTRSPE
CTHESPLETR NIALFSTMCL EGTAQGLVVN TGDRTIIGRI ASLASGVENE KTPIAIEIEH
FVDIIAGLAI LFGATFFVVA MCIGYTFLRA MVFFMAIVVA YVPEGLLATV TVCLSLTAKR
LASKNCVVKN LEAVETLGSK SVICSDKTGT LTQNSMTVSN LWFDNHIHTA DTTEDQSGQK
FDQSSETWRA LCRVLTLCNR AAFKSGQDAV PVPKRIVIGD ASETALLKFS ELTLGNAMGY
RERFPKVCEI PFNSTNKFQL SIHTLEDPRD PRHVLVMKGA PERVLERCSS ILIKGQELPL
DEQWREAFQT AYLSLGGLGE RVLGFCQLYL SEKDYPPGYA FDVEAMNFPT SGLCFAGLVS
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 LLCVGLRPYW
ENHHLQDLQD SYGQEWTFGQ RLYQQYTCYT VFFISIEMCQ IADVLIRKTR RLSAFQQGFF
RNRILVIAIV FQVCIGCFLC YCPGMPNIFN FMPIRYQWWL VPMPFGLLIF VYDEIRKLGV
RCCPGSWWDQ ELYY
