PMA1_NICPL
ID PMA1_NICPL Reviewed; 957 AA.
AC Q08435;
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 1;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 1;
GN Name=PMA1;
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].
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
CC stem.
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; M80489; AAA34094.1; -; Genomic_DNA.
DR PIR; A41779; A41779.
DR AlphaFoldDB; Q08435; -.
DR SMR; Q08435; -.
DR PRIDE; Q08435; -.
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..957
FT /note="Plasma membrane ATPase 1"
FT /id="PRO_0000046291"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..86
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 87..98
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..301
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 649..670
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..675
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 676..698
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 699..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..760
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 761..781
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 782..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 794..814
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 815..823
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 824..844
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 845..957
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 334
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 593
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 597
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 957 AA; 105155 MW; 1A2B0F8A5420BEB1 CRC64;
MGEEKPEVLD AVLKEAVDLE NIPIEEVFEN LRCTKEGLTA TAAQERLAIF GYNKLEEKKD
SKLLKFLGFM WNPLSWVMEA AAIMAIALAN GGGKPPDWQD FVGIITLLII NSTISFIEEN
NAGNAAAALM ARLAPKAKVL RDGRWKEEDA AVLVPGDIIS IKLGDIIPAD ARLLEGDPLK
IDQSALTGES LPVTKGPGDG VYSGSTCKQG EIEAIVIATG VHTFFGKAAH LVDSTNQVGH
FQKVLTAIGN FCICSIAVGM IIEIIVMYPI QHRAYRPGID NLLVLLIGGI PIAMPTVLSV
TMAIGSHRLA QQGAITKRMT AIEEMAGMDV LCSDKTGTLT LNKLTVDKNL IEVFAKGVDA
DMVVLMAARA SRTENQDAID AAIVGMLADP KEARAGIREI HFLPFNPTDK RTALTYLDGE
GKMHRVSKGA PEQILNLAHN KSDIERRVHA VIDKFAERGL RSLGVAYQEV PEGRKESAGG
PWQFIGLLPL FDPPRHDSAE TIRRALNLGV NVKMVTGDQL AIGKETGRRL GMGTNMYPSS
ALLGQTKDES ISALPIDELI EKADGFAGVF PEHKYEIVKR LQARKHICGM TGDGVNDAPA
LKKADIGIAV DDATDAARSA SDIVLTEPGL SVIISAVLTS RAIFQRMKNY TIYAVSITIR
IVLGFMLLAL IWKFDFPPFM VLIIAILNDG TIMTISKDRV KPSPLPDSWK LAEIFTTGIV
LGGYLAMMTV IFFWAAYKTN FFPHVFGVST LEKTATDDFR KLASAIYLQV SIISQALIFV
TRSRSWSFVE RPGFLLVIAF VIAQLVATLI AVYANWSFAA IEGIGWGWAG VIWIYNLVFY
IPLDIIKFFI RYALSGRAWD LVFERRIAFT RKKDFGKEQR ELQWAHAQRT LHGLQVPDTK
LFSEATNFNE LNQLAEEAKR RAEIARLREL HTLKGHVESV VKLKGLDIET IQQAYTV
