ID   PMA1_ZYGRO              Reviewed;         920 AA.
AC   P24545;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Plasma membrane ATPase;
DE            EC=7.1.2.1;
DE   AltName: Full=Proton pump;
OS   Zygosaccharomyces rouxii (Candida mogii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX   NCBI_TaxID=4956;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 42981 / IAM 12879 / JCM 22060 / S-96;
RX   PubMed=1837019; DOI=10.1093/oxfordjournals.jbchem.a123563;
RA   Watanabe Y., Shiramizu M., Tamai Y.;
RT   "Molecular cloning and sequencing of plasma membrane H(+)-ATPase gene from
RT   the salt-tolerant yeast Zygosaccharomyces rouxii.";
RL   J. Biochem. 110:237-240(1991).
CC   -!- FUNCTION: The plasma membrane ATPase of plants and fungi is a hydrogen
CC       ion pump. The proton gradient it generates drives the active transport
CC       of nutrients by H(+)-symport. The resulting external acidification
CC       and/or internal alkinization may mediate growth responses.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H(+)(in) + H2O = ADP + 2 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:20852, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.1;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IIIA subfamily. {ECO:0000305}.
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DR   EMBL; D10764; BAA01594.1; -; Genomic_DNA.
DR   PIR; JX0181; PXKZP.
DR   AlphaFoldDB; P24545; -.
DR   SMR; P24545; -.
DR   STRING; 4956.XP_002498439.1; -.
DR   eggNOG; KOG0205; Eukaryota.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0008553; F:P-type proton-exporting transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR   CDD; cd02076; P-type_ATPase_H; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
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; IPR006534; P-type_ATPase_IIIA.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   PRINTS; PR00120; HATPASE.
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; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Hydrogen ion transport; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..920
FT                   /note="Plasma membrane ATPase"
FT                   /id="PRO_0000046273"
FT   TOPO_DOM        1..117
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        139..142
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..162
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..293
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..315
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..326
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..349
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        350..721
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        722..740
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        741..756
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        757..776
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        777..826
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        827..847
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        848..859
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        860..876
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        877..920
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..67
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        380
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         636
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         640
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   920 AA;  100062 MW;  2E2F93178C80F009 CRC64;
     MSDERITEKP PHQQPESEGE PVPEEEVEEE TEEEVPDEQS SEDDDIDGLI DELQSQEAHE
     EAEEDDGPAA AGEARKIPEE LLQTDPSVGL SSDEVVNRRK KYGLNQMREE SENLLVKFLM
     FFIGPIQFVM EAAAVLAAGL EDWVDFGVIC GLLFLNAGVG FIQEFQAGSI VEELKKTLAN
     TATVIRDGSV QEAPANEIVP GDILKLEDGT VIPADGRLVT EECFLQVDQS SITGESLAVD
     KHYGDEVFSS STVKRGEGFM IVTATGDNTF VGRAASLVNA AAGGQGHFTE VLNGIGVILL
     VLVVITLLLI WTACFYRTVR IVPILRYTLG ITIVGVPVGL PAVVTTTMAG GAAYLAKKQA
     IVQKLSAIES LAGVEILCSD KTGTLTKNKL SLHEPYTVEG VSSDDLMLTA CLAASRKKKG
     LDAIDKAFLK SLAQYPKAKG ALTKYKVLEF HPFDPVSKKV TAVVESPEGE RIICVKGAPL
     FVLKTVEEDH PIPEDVHENY ENKVAELASR GFRALGVARK RGEGHWEILG VMPCMDPPRD
     DTAATVNEAK RLGLSVKMLT GDAVGIAKET CRQLGLGTNI YDAERLGLGG GGSMPGSEMY
     DFVENADGFA EVFPQHKFAV VDILQQRGYL VAMTGDGVND APSLKKADTG IAVEGATDAA
     RSAADIVFLA PGLSAIIDAL KTSRQIFHRM YAYVVYRIAL SLHLEIFLGL WIAILNHSLD
     IDLIVFIAIF ADVATLAIAY DNAPFSPSPV KWNLPRLWGM SIMMGIILAA GTWITLTTMF
     LPKGGIIQNF GSIDGILFLE ISLTENWLIF ITRAVGPFWS SIPSWQLAGA VFVVDVVATM
     FTLFGWWSQN WTDIVTVVRI YIWSIGIFCC LGGAYYLMSE SETFDRLMNG KPLKENKSTR
     SVEDFLASMR RVSTQHEKGN