PMA3_NICPL
ID PMA3_NICPL Reviewed; 956 AA.
AC Q08436;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Plasma membrane ATPase 3;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 3;
GN Name=PMA3;
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 [GENOMIC DNA / MRNA].
RC TISSUE=Root;
RX PubMed=1530935; DOI=10.1016/s0021-9258(18)48415-3;
RA Perez C., Michelet B., Ferrant V., Bogaerts P., Boutry M.;
RT "Differential expression within a three-gene subfamily encoding a plasma
RT membrane H(+)-ATPase in Nicotiana plumbaginifolia.";
RL J. Biol. Chem. 267:1204-1211(1992).
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 in roots, stems, leaves from both
CC vegetative and flowering plants, and flowers at early and late stages
CC of development with highest expression levels found in flowers and root
CC tissue.
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; M80490; AAA34098.1; -; mRNA.
DR EMBL; M80491; AAA34099.1; -; Genomic_DNA.
DR PDB; 2O98; X-ray; 2.70 A; P/Q=905-956.
DR PDBsum; 2O98; -.
DR SMR; Q08436; -.
DR PRIDE; Q08436; -.
DR EvolutionaryTrace; Q08436; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Hydrogen ion transport;
KW Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..956
FT /note="Plasma membrane ATPase 3"
FT /id="PRO_0000046292"
FT TOPO_DOM 1..65
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..85
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86..97
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..278
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..300
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 648..669
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..674
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 675..697
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 714..734
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..759
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 760..780
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 781..792
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 793..813
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 814..822
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 823..843
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..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"
FT VARIANT 63
FT /note="S -> L"
FT HELIX 907..930
FT /evidence="ECO:0007829|PDB:2O98"
FT HELIX 932..943
FT /evidence="ECO:0007829|PDB:2O98"
SQ SEQUENCE 956 AA; 105116 MW; 94916371CB434BA4 CRC64;
MGEKPEVLDA VLKETVDLEN IPIEEVFENL RCTKEGLTAT AAQERLSIFG YNKLEEKKES
KFSKFLGFMW NPLSWVMEAA AIMAIALANG GGKPPDWQDF VGIITLLIIN STISFIEENN
AGNAAAALMA RLAPKAKVLR DGKWKEEDAA VLVPGDIISI KLGDIIPADA RLLEGDPLKI
DQSALTGESL PVTKGPGDGV YSGSTCKQGE IEAVVIATGV HTFFGKAAHL VDSTNQVGHF
QKVLTAIGNF CICSIAVGMI IEIIVMYPIQ HRKYRPGIDN LLVLLIGGIP IAMPTVLSVT
MAIGSHRLAQ QGAITKRMTA IEEMAGMDVL CSDKTGTLTL NKLTVDKYLI EVFARGVDAD
TVVLMAARAS RTENQDAIDA AIVGMLADPK EARAGIREIH FLPFNPTDKR TALTYLDGEG
KMHRVSKGAP EQILHLAHNK SDIERRVHAV IDKFAERGLR SLAVAYQEVP EGRKESAGGP
WQFIALLPLF DPPRHDSAET IRRALNLGVN VKMITGDQLA IGKETGRRLG MGTNMYPSSA
LLGQTKDESI SALPVDELIE KADGFAGVFP EHKYEIVKRL QARKHICGMT GDGVNDAPAL
KKADIGIAVD DATDAARSAS DIVLTEPGLS VIISAVLTSR AIFQRMKNYT IYAVSITIRI
VLGFMLLALI WQFDFPPFMV LIIAILNDGT IMTISKDRVK PSPLPDSWKL AEIFTTGVVL
GGYLAMMTVI FFWAAYKTNF FPRVFGVSTL EKTATDDFRK LASAIYLQVS TISQALIFVT
RSRSWSFMER PGLLLVVAFF IAQLVATLIA VYANWSFAAI EGIGWGWAGV IWLYNIVFYI
PLDLXXFLIR YALSGKAWDL VIEQRIAFTR KKDFGKEQRE LQWAHAQRTL HGLQVPDPKI
FSETTNFNEL NQLAEEAKRR AEIARLRELH TLKGHVESVV KLKGLDIETI QQAYTV
