PMA1_DUNAC
ID PMA1_DUNAC Reviewed; 1103 AA.
AC P54210;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN Name=DHA1;
OS Dunaliella acidophila (Green alga) (Spermatozopsis acidophila).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX NCBI_TaxID=38272;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SAG 19.85;
RX PubMed=8972605; DOI=10.1104/pp.112.4.1693;
RA Weiss M., Pick U.;
RT "Primary structure and effect of pH on the expression of the plasma
RT membrane H(+)-ATPase from Dunaliella acidophila and Dunaliella salina.";
RL Plant Physiol. 112:1693-1702(1996).
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 -!- 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; U54690; AAB49042.1; -; mRNA.
DR AlphaFoldDB; P54210; -.
DR SMR; P54210; -.
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 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..1103
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000046287"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 266..286
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 690..710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 944..964
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1074..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 358
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 616
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 620
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1103 AA; 119791 MW; 6F8BC2370D03DDC8 CRC64;
MSGKERTEEN GAVKQDTKEQ VKKSADNGDK GVDEVDFAKI GLEDAFKYLN CSEHGLSGAE
AEARLKQHGP NKLPDNSRNP VLVYFGYMWN PLAWAMEAAA IIAIALVDGA DFALIVGLLI
INATISFVEE SNADKAIKAL SAALAPKAMA LRNGAMVTID AVDLVPGDVI LIRIGNVVPA
DVKLLPEHGA DDYETPVQID QAALTGESLP AKKFTGNVAF SGSTVKQGER HAVVYATGVN
TFFGRAAALI SGTHNVANIQ RVMNRIGGLC LITIGVWVVI EVPVQFAHYK HSCVAGKEGC
PTLLNMLVIL VGAIPIAMPT VLSVTLALGA YKLAREGAIV TRMSAVEEMA GLDVLCSDKT
GTLTLNKLSI DPSNVFPVGT MDIPEVMKFG ALSANIITEE PIDMVLWESY PEREKLKSEY
KHTKYFPFNP NDKITIATVL EIATGRVFRV LKGSPQVVLA KAWNAQALDG PVNEKIKEYA
GRGFRSLGIA MAEGDGKDGT KWEMLAVLPM FDPPRHDTKE TIERCMKQGI AVKMVTGDHL
LIGKETAKML GMGTEMYPSE VLIKARNGDV EAPHGYKNYV AMVEACNGFA QVFPEHKFEI
VEILQEAHHR VGMTGDGVND APALKKAHVG VAVADATDAA RGAADIVLTE PGLSTIVTAV
IGARKIFKRM TTYAKYTISV TFRIAFTFGL LTVIYDWYFP TILIVILAVF NDGAMIALSK
DRVVASVLPS TWNLATIFVP GFVYAMWLTL SSWALYQVAT HSTFFERMTP LPSLNTQHAT
LISWCEDEIS SKLGVNPQDS LCTYPSYADQ LNECKGSVSL SSQVPGVPTI LDQCVTEQRY
IRDALTRALI YTHLSVSGQA VVFVVRTSGF SLKEVAGVST YVAFALAQFG ATMFGIFGLG
GYNKPRQNFD NCQFCDYSTH NRVLFFNSEV EPRAGTESVY TASVIGCGGY VIVAWIWAAL
FYTALDPLKW GLMWIMNDDG FRDRHAWRKS NHEAMERRSR EQLDNKEFAG PSGMVPANFS
NPLGRASMSK PVSALLDRKS ASLVAINRSS MTVSHDPNHA LNIGRRSMIG RPSGPLGRNS
NTGQSNPLNS SSVEIKPDAP NKV
