ID   PMA_AVESA               Reviewed;         110 AA.
AC   Q7M290;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Plasma membrane ATPase;
DE            EC=7.1.2.1;
DE   AltName: Full=Proton pump;
DE   Flags: Fragments;
OS   Avena sativa (Oat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Poodae; Poeae; Aveninae; Avena.
OX   NCBI_TaxID=4498;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Root;
RX   PubMed=16665938; DOI=10.1104/pp.86.2.512;
RA   Schaller G.E., Sussman M.R.;
RT   "Isolation and sequence of tryptic peptides from the proton-pumping ATPase
RT   of the oat plasma membrane.";
RL   Plant Physiol. 86:512-516(1988).
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 (By
CC       similarity). {ECO:0000250}.
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 {ECO:0000269|PubMed:16665938};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:16665938}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:16665938}.
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   PIR; JA0154; JA0154.
DR   AlphaFoldDB; Q7M290; -.
DR   SMR; Q7M290; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; ISS:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; ISS:UniProtKB.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   SUPFAM; SSF81653; SSF81653; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Translocase; Transmembrane; Transport.
FT   CHAIN           <1..>110
FT                   /note="Plasma membrane ATPase"
FT                   /id="PRO_0000046286"
FT   REGION          88..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         72
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P83970"
FT   BINDING         76
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P83970"
FT   UNSURE          103
FT                   /note="S or A"
FT                   /evidence="ECO:0000269|PubMed:16665938"
FT   NON_CONS        28..29
FT                   /evidence="ECO:0000305"
FT   NON_CONS        56..57
FT                   /evidence="ECO:0000305"
FT   NON_CONS        64..65
FT                   /evidence="ECO:0000305"
FT   NON_CONS        81..82
FT                   /evidence="ECO:0000305"
FT   NON_CONS        100..101
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|PIR:JA0154"
FT   NON_TER         110
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   110 AA;  11341 MW;  3A71185590860113 CRC64;
     WGEQEASILV PGDIVSIKLG DIVPADARID QSGLTGESLP VTKNPGDEVF SGSTCKTGTL
     TLNKGIVGMT GDGVNDAPAL KTLHGLQAPE STSLNLPNDK ELSEIAEQAK