PMA1_SOLLC
ID PMA1_SOLLC Reviewed; 956 AA.
AC P22180;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Plasma membrane ATPase 1;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 1;
GN Name=LHA1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Castlemart; TISSUE=Root;
RX PubMed=16667929; DOI=10.1104/pp.94.4.1874;
RA Ewing N.N., Wimmers L.E., Meyer D.J., Chetelat R.T., Bennett A.B.;
RT "Molecular cloning of tomato plasma membrane H+-ATPase.";
RL Plant Physiol. 94:1874-1881(1990).
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 -!- SUBUNIT: Possibly exists as a homodimer or a homotrimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: As many as 6 to 8 closely related genes may encode other
CC isoforms of plasma membrane ATPase in tomato, like the LHA2 gene
CC product which is 96% identical to the LHA1 gene product.
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; M60166; AAA34173.1; -; mRNA.
DR PIR; A45506; A45506.
DR RefSeq; NP_001234775.1; NM_001247846.1.
DR AlphaFoldDB; P22180; -.
DR SMR; P22180; -.
DR STRING; 4081.Solyc03g113400.2.1; -.
DR iPTMnet; P22180; -.
DR PaxDb; P22180; -.
DR PRIDE; P22180; -.
DR GeneID; 543982; -.
DR KEGG; sly:543982; -.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR InParanoid; P22180; -.
DR OrthoDB; 188115at2759; -.
DR PhylomeDB; P22180; -.
DR BRENDA; 7.1.2.1; 3101.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P22180; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
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; 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 Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..956
FT /note="Plasma membrane ATPase 1"
FT /id="PRO_0000046289"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..666
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 667..674
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..697
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..792
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..821
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..956
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 333
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 596
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 956 AA; 105103 MW; CD23AA8B10E7B6E5 CRC64;
MAEKPEVLDA VLKETVDLEN IPIEEVFENL RCTREGLTAT AAQERLSIFG YNKLEEKKES
KFLKFLGFMW NPLSWVMEAA AIMAIALANG GGKPPDWQDF VGIITLLIIN STISFIEENN
AGNAAAALMA RLAPKAKVLR DGKWDEEDAS VLVPGDIISI KLGDIIPADA RLLEGDPLKI
DQSALTGESL PVTKGPGDGV YSGSTCKQGE IEAVVIATGV HTFFGKAAHL VDSTNQVGHF
QKVLTAIGNF CICSIAVGMI IEIIVMYPIQ HRKYRPGIDN LLVLLIGGIP IAMPTVLSVT
MAIGSHRLAQ QGAITKRMTA IEEMAGMDVL CSDKTGTLTL NKLTVDKALI EVFAKGIDAD
TVVLMAARAS RIENQDAIDT AIVGMLADPK EARAGIREIH FLPFNPTDKR TALTYLDGEG
KMHRVSKGAP EQILNLAHNK SDIERRVHTV IDKFAERGLR SLGVAYQEVP EGRKESAGGP
WQFIALLPLF DPPRHDSAET IRRALNLGVN VKMITGDQLA IGKETGRRLG MGTNMYPSSA
LLGQTKDESI AALPIDELIE KADGFAGVFP EHKYEIVKRL QARKHICGMT GDGVNDAPAL
KKADIGIAVD DATDAARSAS DIVLTEPGLS VIISAVLTSR AIFQRMKNYT IYAVSITIRI
VLGFMLLALI WKFDFPPFMV LIIAILNDGT IMTISKDRVK PSPLPDSWKL AEIFTTGVVL
GGYLAMMTVI FFWAAYKTNF FPRIFGVSTL EKTATDDFRK LASAIYLQVS TISQALIFVT
RSRSWSFVER PGLLLVFAFF VAQLVATLIA VYANWSFAAI EGIGWGWAGV IWLYNIVTYI
PLDLIKFLIR YALSGKAWDL VLEQRIAFTR KKDFGKELRE LQWAHAQRTL HGLQVPDPKI
FSETTNFNEL NQLAEEAKRR AEIARLRELH TLKGHVESVV KLKGLDIETI QQSYTV
