ID   ATP4A_XENLA             Reviewed;        1031 AA.
AC   Q92126;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Potassium-transporting ATPase alpha chain 1;
DE            EC=7.2.2.19;
DE   AltName: Full=Gastric H(+)/K(+) ATPase subunit alpha;
DE   AltName: Full=Proton pump;
GN   Name=atp4a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Gastric mucosa;
RX   PubMed=7762614; DOI=10.1152/ajpcell.1995.268.5.c1207;
RA   Mathews P.M., Claeys D., Jaisser F., Geering K., Horisberger J.-D.,
RA   Kraehenbuhl J.-P., Rossier B.C.;
RT   "Primary structure and functional expression of the mouse and frog alpha-
RT   subunit of the gastric H(+)-K(+)-ATPase.";
RL   Am. J. Physiol. 268:C1207-C1214(1995).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the exchange of
CC       H(+) and K(+) ions across the plasma membrane. Responsible for acid
CC       production in the stomach.
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   -!- SUBUNIT: Composed of two subunits: alpha (catalytic) and beta.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in stomach mucosa.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIC subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U17249; AAA76601.1; -; mRNA.
DR   PIR; I51674; I51674.
DR   RefSeq; NP_001084343.1; NM_001090874.1.
DR   AlphaFoldDB; Q92126; -.
DR   SMR; Q92126; -.
DR   GeneID; 399450; -.
DR   CTD; 399450; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008900; F:P-type potassium:proton transporter activity; IEA:UniProtKB-EC.
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; 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   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; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW   Potassium transport; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..1031
FT                   /note="Potassium-transporting ATPase alpha chain 1"
FT                   /id="PRO_0000046258"
FT   TOPO_DOM        2..94
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        95..115
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        116..138
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..327
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        328..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        346..779
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        780..799
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        800..809
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        810..830
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        831..850
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        851..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        874..925
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        926..945
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        946..959
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        960..978
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        979..993
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        994..1014
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1015..1031
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          221..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..239
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        383
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         724
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         728
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         950
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1031 AA;  115037 MW;  9366AC1C6ED4D5FC CRC64;
     MGKKEQYDMY SVEMEREGDG AMDVKVMKKN KASKKKEKLE SMKKEMDIND HEITVEELEQ
     KYTTSVSKGL KSAFAAEVIL RDGPNELKPP KGTPEYIKFA RQLAGGLQCL MWVAAVICLI
     AFGIEESQGD LTSADNLYLA ITLIAVVVVT GCFGYYQEFK STNIIASFKN LVPQQATVVR
     DGDKFQINAN QLVVGDLVEI KGGDRVPADI RIITSQGCKV DNSSLTGESE PQTRSPEYTH
     ESPLETRNIA FFSTMCLEGT ATGIIINTGD RTIIGRIATL ASGVGNEKTP IAIEIEHFVD
     IIAGLAIFFG ATFFVVAMVI GYTFLRAMVF FMAIVVAYVP EGLLATVTVC LSLTAKRLAR
     KNCVVKNLEA VETLGSTSVI CSDKTGTLTQ NRMTVSHLWF DNHIHSADTT EDQSGQSFDQ
     TSDTWRALSK VVSLCNRAFF KSGQDGIPVP KRIVIGDASE TALVKFSEIT VGNVMEYRER
     FKKVTEVPFN STNKFQLSIH ELQDPLDLRY LMVMKGAPER ILERCSTIMI KGQELPLDEQ
     WKEAFQTAYM DLGGLGERVL GFCHLYLNEK EYSRGFNFDT EEMNFPTSGL CFAGLISMID
     PPRATVPDAV MKCRTAGIRV IMVTGDHPIT AKAIAASVGI ISEGSETVED IAARLRIPVE
     QVNKRDARAC VINGGQLKEM SSEELVEALK LHPEMVFART SPQQKLIIVE SCQKLGAIVA
     VTGDGVNDSP ALKKADIGVA MGIAGSDAAK NAADMILLDD NFASIVTGVE QGRLIFDNLK
     KSIAYTLTKN IPELAPYLIY ITASVPLPLG CITILFIELC TDIFPSVSLA YERAESDIMH
     LKPRNPRRDR LVNEALAVYS YFQIGIIQSF AGFVDYFTVM AQEGWFPAYV LGLRSHWENQ
     HLQDLQDSYG QEWTFSQRLY QQYTCYTVFF ISYEICQISD VLIRKTRRLS VFQQGFFRNK
     VLVIAIVFQL CLGNFLCYCP GMPNVFNFMP IRFQWWLVPL PFGILIFVYD EIRKLGVRRH
     PGSWFDKEMY Y