PMA1_DUNBI
ID PMA1_DUNBI Reviewed; 1131 AA.
AC P54211;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN Name=PMA1;
OS Dunaliella bioculata (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX NCBI_TaxID=13790;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SAG 19-4;
RX PubMed=7647298; DOI=10.1007/bf00021191;
RA Wolf A.H., Slayman C.W., Gradmann D.;
RT "Primary structure of the plasma membrane H(+)-ATPase from the halotolerant
RT alga Dunaliella bioculata.";
RL Plant Mol. Biol. 28:657-666(1995).
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; X73901; CAA52107.1; -; mRNA.
DR PIR; S57807; S34213.
DR AlphaFoldDB; P54211; -.
DR SMR; P54211; -.
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..1131
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000046288"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 946..966
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 994..1023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1067..1131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 357
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 619
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1131 AA; 123451 MW; E493726BD5CD732D CRC64;
MADIKEGVEE GSVKVDMIKE PLTQGDTGVD EVDFAKITLD DAFKYLNCNK HGLSSAEAAA
RLQQHGPNKL PDSSRNPVLV FLGYMWNPLA WAMEAAAIIS IALLDVADFV LIVGLLLINA
IISFYEESNA DKAIKALTAA LAPKAMVVRD GAIVTIDAVN LVPGDVILIR LGNIVPADVK
LLEEEGADEG EQEAPMQIDQ AALTGESLPA KKFTGDVAFS GSSIKQGERH AVVYATGVNT
FFGRAAALIS GTNNVSNLQT VMNKMSAICI VTILLWVVVE LAVQFGHYSH ECVGGREGCP
TLLNMLVVLV GGIPIAMPTV LSVTLALGAY KLAREGAIVT RMSAVEEMAG MDVLCSDKTG
TLTLNKLSID KSMVVPVGNM GVDEIMRMGA LSANTVTEEP IDMVLWESYP DRETIKRDYK
HTKYFPFNPN DKITIATCLE IATGRVFRVL KGSPQVVLAK AWNAAELDAT VNQKMVEFAN
RGFRALGLAM ADGDGKDGTK WEMLALLPLF DPPRHDTKET IEHCQNQGIQ VKMITGDHLL
IGKETAKMLG MGTEMFPSEV MIKARNGDAS QLHGYKNFVE MVETCNGFAQ VFPEHKFEIV
KILQDSNHVV GMTGDGVNDA PALKKADVGV AVADATDAAR GAADIVLTEP GLSTIVTAVI
GARKIFQRMT TYSKYTIAMT FRICFTFGLI TVIYDWYFPT ILIVIMAVFN DGAMIALSKD
RVVASKTPNS WNITNIFIMG MVYGLYLTLS TWALYQTATK TTFFEDKTPL HSLNDQYSVL
QPWCEDEVRA KLGQTIDPYA SLCESNSYAK QFDECEGYQK GSGVQVEDVP TLHAQCVTEQ
RYLRGAMTRS LIYTQVSISG QALVFVVRTA GYSLMERAGT STYLAFFFAQ VGATLFGIFG
LGGFEKPRHQ LEDCQFCDYS FHEPVDWFDS GIVPESGTES DFTASVIGCG GYVIVAWIWS
AIWYVLLDPI KWILFWILNE EGFRDTMSWR ESTKRSLDRR SKDDIGDKEF TGPSGMVPAN
YSNPLGRASM SKPVSAVLDR KSASLVAINR NSMTVSQDPN RALNIGRRSM IGRPSGPVGR
TSMPLGRISR TSNTLSTGSK DGQIGRGSKP LNSSSAEIKP DKYDFASTIR E
