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 04-NOV-2026, entry version 142. DE RecName: Full=Plasma membrane ATPase; DE EC=7.1.2.1; DE AltName: Full=Proton pump; OS Zygosaccharomyces rouxii (Yeast) (Saccharomyces rouxii). 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 + H2O + H(+)(in) = ADP + phosphate + 2 H(+)(out); 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}. 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; D10764; BAA01594.1; -; Genomic_DNA. DR PIR; JX0181; PXKZP. DR AlphaFoldDB; P24545; -. DR SMR; P24545; -. DR eggNOG; KOG0205; Eukaryota. DR OMA; AAKMPQW; -. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. 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 FunFam; 2.70.150.10:FF:000011; Plasma membrane ATPase; 1. DR FunFam; 3.40.1110.10:FF:000005; Plasma membrane ATPase; 1. DR FunFam; 3.40.50.1000:FF:000008; Plasma membrane ATPase; 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; 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; IPR059000; ATPase_P-type_domA. 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 NCBIfam; TIGR01647; ATPase-IIIA_H; 1. DR NCBIfam; TIGR01494; ATPase_P-type; 3. DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR Pfam; PF00702; Hydrolase; 1. DR PRINTS; PR00119; CATATPASE. DR PRINTS; PR00120; HATPASE. DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1. 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 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..11 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 17..50 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 //