PMA1_WHEAT
ID PMA1_WHEAT Reviewed; 951 AA.
AC P83970;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN Name=ha1 {ECO:0000312|EMBL:AAS55889.1};
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565 {ECO:0000312|EMBL:AAS55889.1};
RN [1] {ECO:0000312|EMBL:AAS55889.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Yuma/8*Cc {ECO:0000312|EMBL:AAS55889.1};
RA Gu X., Ma Z.;
RT "Cloning of a plasma membrane H+-ATPase in wheat (T. aestivum L.).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000305};
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; AY543630; AAS55889.1; -; mRNA.
DR AlphaFoldDB; P83970; -.
DR SMR; P83970; -.
DR STRING; 4565.Traes_2AL_2C50DEE4C.1; -.
DR PRIDE; P83970; -.
DR EnsemblPlants; TraesCAD_scaffold_085250_01G000100.1; TraesCAD_scaffold_085250_01G000100.1; TraesCAD_scaffold_085250_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_089452_01G000100.1; TraesCLE_scaffold_089452_01G000100.1; TraesCLE_scaffold_089452_01G000100.
DR EnsemblPlants; TraesCS2A02G502400.1; TraesCS2A02G502400.1; TraesCS2A02G502400.
DR EnsemblPlants; TraesPAR_scaffold_081221_01G000100.1; TraesPAR_scaffold_081221_01G000100.1; TraesPAR_scaffold_081221_01G000100.
DR EnsemblPlants; TraesROB_scaffold_076640_01G000100.1; TraesROB_scaffold_076640_01G000100.1; TraesROB_scaffold_076640_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_081304_01G000100.1; TraesWEE_scaffold_081304_01G000100.1; TraesWEE_scaffold_081304_01G000100.
DR Gramene; TraesCAD_scaffold_085250_01G000100.1; TraesCAD_scaffold_085250_01G000100.1; TraesCAD_scaffold_085250_01G000100.
DR Gramene; TraesCLE_scaffold_089452_01G000100.1; TraesCLE_scaffold_089452_01G000100.1; TraesCLE_scaffold_089452_01G000100.
DR Gramene; TraesCS2A02G502400.1; TraesCS2A02G502400.1; TraesCS2A02G502400.
DR Gramene; TraesPAR_scaffold_081221_01G000100.1; TraesPAR_scaffold_081221_01G000100.1; TraesPAR_scaffold_081221_01G000100.
DR Gramene; TraesROB_scaffold_076640_01G000100.1; TraesROB_scaffold_076640_01G000100.1; TraesROB_scaffold_076640_01G000100.
DR Gramene; TraesWEE_scaffold_081304_01G000100.1; TraesWEE_scaffold_081304_01G000100.1; TraesWEE_scaffold_081304_01G000100.
DR eggNOG; KOG0205; Eukaryota.
DR HOGENOM; CLU_002360_6_4_1; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P83970; baseline.
DR Genevisible; P83970; TA.
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..951
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000046294"
FT TOPO_DOM 1..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..92
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..613
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..661
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 662..682
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..771
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 772..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 806..813
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..951
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 329
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q03194"
FT BINDING 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q03194"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q03194"
SQ SEQUENCE 951 AA; 104684 MW; 14079CD5F77B2854 CRC64;
MGGLEEIRNE AVDLENIPIE EVFEQLKCTR QGLTSDEGAQ RVEIFGLNKL EEKKESKVLK
FLGFMWNPLS WVMEMAAIMA IALANGGGKP PDWQDFVGII VLLVINSTIS FIEENNAGNA
AAALMANLAP KTKVLRDGRW GEQEASILVP GDIVSIKLGD IVPADARLLE GDPLKIDQSG
LTGESLPVTK NPGDEVFSGS TCKQGEIEAV VIATGVHTFF GKAAHLVDST NQVGHFQQVL
TAIGNFCIVS IAVGIVIEII VMFPIQRRKY RAGIENLLVL LIGGIPIAMP TVLSVTMAIG
SHKLSQQGAI TKRMTAIEEL AGMDVLCSDK TGTLTLNKLS VDKNLVEVFA KGVDKEHVLL
LAARASRVEN QDAIDACMVG MLADPKEARA GIREVHFLPF NPTDKRTALT YIDAEGNWHR
ASKGAPEQII TLCNCKEDVK RKVHSVIEKY AERGLRSLAV ARQEVPEKSK DSPGGPWQFI
GLLPLFDPPR HDSAETIRKA LVLGVNVKMI TGDQLAIGKE TGRRLGMGTN MYPSSALLGQ
SKDGSLESLP VDELIEKADG FAGVFPEHKY EIVKRLQEKK HIVGMTGDGV NDAPALKKAD
IGIAVDDATD AARSASDIVL TEPGLSVIIS AVLTSRCIFQ RMKNYTIYAV SITIRIVLGF
MLIALIWKFD FAPFMVLIIA ILNDGTIMTI SKDRVKPSPL PDSWKLNEIF ATGVVLGTYL
ALVTVVFFWL IHKTDFFTNK FGVESIRNTE FKEMSALYLQ VSIVSQALIF VTRSRSWSFV
ERPGFLLVTA FLLAQLVATL IAVYANWDFA RIKGIGWGWA GVIWLFSIVF YFPLDIFKFF
IRFVLSGRAW DNLLQNKTAF TTKENYGKGE REAQWATAQR TLHGLQAPEP ASHTLFNDKS
SYRELSEIAE QAKRRAEIAR LRELNTLKGH VESVVKLKGL DIDTINQNYT V
