PMA4_NICPL
ID PMA4_NICPL Reviewed; 952 AA.
AC Q03194;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Plasma membrane ATPase 4;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 4;
GN Name=PMA4;
OS Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4092;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf;
RX PubMed=8490141; DOI=10.1007/bf00023594;
RA Moriau L., Bogaerts P., Jonniaux J.-L., Boutry M.;
RT "Identification and characterization of a second plasma membrane H(+)-
RT ATPase gene subfamily in Nicotiana plumbaginifolia.";
RL Plant Mol. Biol. 21:955-963(1993).
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 -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in root, stem, leaf and
CC flower.
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; X66737; CAA47275.1; -; mRNA.
DR PIR; S33548; S33548.
DR AlphaFoldDB; Q03194; -.
DR SMR; Q03194; -.
DR PRIDE; Q03194; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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 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 Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..952
FT /note="Plasma membrane ATPase 4"
FT /id="PRO_0000046293"
FT TOPO_DOM 1..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..84
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 85..96
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..299
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 647..668
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..673
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..696
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 788..808
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 809..817
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..838
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 839..952
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 332
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 591
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 595
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 952 AA; 105189 MW; FD66F994796B3C6F CRC64;
MAKAISLEEI KNETVDLEKI PIEEVFEQLK CTREGLSADE GASRLQIFGP NKLEEKNESK
ILKFLGFMWN PLSWVMEAAA VMAIALANGD GKPPDWQDFI GIICLLVINS TISFIEENNA
GNAAAALMAG LAPKTKVLRD GRWSEQEAAI LVPGDIISVK LGDIIPADAR LLEGDPLKID
QSALTGESLP VTKNPGDEVF SGSTCKQGEL EAVVIATGVH TFFGKAAHLV DSTNNVGHFQ
KVLTAIGNFC ICSIAIGMLV EIIVMYPIQH RKYRDGIDNL LVLLIGGIPI AMPTVLSVTM
AIGSHRLSQQ GAITKRMTAI EEMAGMDVLC SDKTGTLTLN KLSVDRNLVE VFAKGVDKEY
VLLLAARASR VENQDAIDAC MVGMLADPKE ARAGIREVHF LPFNPVDKRT ALTYIDNNNN
WHRASKGAPE QILDLCNAKE DVRRKVHSMM DKYAERGLRS LAVARRTVPE KSKESPGGRW
EFVGLLPLFD PPRHDSAETI RRALNLGVNV KMITGDQLAI AKETGRRLGM GTNMYPSASL
LGQDKDSAIA SLPIEELIEK ADGFAGVFPE HKYEIVKKLQ ERKHIVGMTG DGVNDAPALK
KADIGIAVAD ATDAARGASD IVLTEPGLSV IISAVLTSRA IFQRMKNYTI YAVSITIRIV
FGFMFIALIW KYDFSAFMVL IIAILNDGTI MTISKDRVKP SPMPDSWKLK EIFATGVVLG
GYQALMTVVF FWAMHDTDFF SDKFGVKSLR NSDEEMMSAL YLQVSIISQA LIFVTRSRSW
SFLERPGMLL VIAFMIAQLV ATLIAVYANW AFARVKGCGW GWAGVIWLYS IIFYLPLDIM
KFAIRYILSG KAWNNLLDNK TAFTTKKDYG KEEREAQWAL AQRTLHGLQP PEATNLFNEK
NSYRELSEIA EQAKRRAEMA RLRELHTLKG HVESVVKLKG LDIETIQQHY TV
