PMA2_SOLLC
ID PMA2_SOLLC Reviewed; 704 AA.
AC P23980;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Plasma membrane ATPase 2;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 2;
DE Flags: Fragment;
GN Name=LHA2;
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.
RC 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 LHA1 gene
CC product which is 96% identical to the LHA2 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 AlphaFoldDB; P23980; -.
DR SMR; P23980; -.
DR InParanoid; P23980; -.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P23980; 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 Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
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; 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 PRINTS; PR00120; HATPASE.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 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 Reference proteome; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN <1..704
FT /note="Plasma membrane ATPase 2"
FT /id="PRO_0000046290"
FT TRANSMEM <1..16
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 17..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..48
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..417
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..422
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..445
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..704
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 81
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT NON_TER 1
SQ SEQUENCE 704 AA; 78040 MW; 1AA38026D7BE92C7 CRC64;
CSIAVGMIIE IIVMYPIQHR KYRPGIDNLL VLLIGGIPIA MPTVLSVTMA IGSHRLAQQG
AITKRMTAIE EMAGMDVLCS DKTGTLTLNK LTVDKNLVEV FAKGVDADTV VLMAARASRT
ENQDAIDTAI VGMLADPKEA RAGIREIHFL PFNPTDKRTA LTYLDGEGKM HRVSKGAPEQ
ILNLAHNKSD IERRVHTVID KFAERGLRSL GVAYQEVPEG RKESSGGPWQ FIGLLPLFDP
PRHDSAETIR RALNLGVNVK MITGDQLAIG KETGRRLGMG TNMYPSSALL GQTKDESIAS
LPIDELIEKA DGFAGVFPEH KYEIVKRLQA RKHICGMTGD GVNDAPALKK ADIGIAVDDA
TDAARSASDI VLTEPGLSVI ISAVLTSRAI FQRMKNYTIY AVSITIRIVL GFMLLALIWK
FDFPPFMVLI IAILNDGTIM TISKDRVKPS PLPDSWKLAE IFTTGVVLGG YLAMMTVIFF
WAAYETQFFP RVFGVSTLQR TATDDFRKLA SAIYLQVSTI SQALIFVTRS RSWSFVERPG
LLLVVALIVA QLVATLIAVY ASWSFAAIEG IGWGWAGVIW LYNLVFYFPL DIIKFLIRYA
LSGRAWDLVL EQRIAFTRKK DFGKEQRELQ WAHAQRTLHG LQVPDIKLFS EATNFNELNQ
LAEEAKRRAE IARQRELHTL KGHVESVVKL KGLDIETIQQ SYTV
