PMA1_AJECA
ID PMA1_AJECA Reviewed; 916 AA.
AC Q07421;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN Name=PMA1;
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7916725; DOI=10.1016/0378-1119(93)90483-j;
RA Schafer M.P., Dean G.E.;
RT "Cloning and sequence analysis of an H(+)-ATPase-encoding gene from the
RT human dimorphic pathogen Histoplasma capsulatum.";
RL Gene 136:295-300(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 -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIIA subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L07305; AAB53772.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07421; -.
DR SMR; Q07421; -.
DR PRIDE; Q07421; -.
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 3: Inferred from homology;
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..916
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000046265"
FT TOPO_DOM 1..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..134
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..155
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..305
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..350
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..734
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..754
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..776
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 818..843
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 844..847
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 848..874
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 875..916
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..63
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 374
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 630
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 634
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 916 AA; 98885 MW; 1B750ACE83F330AD CRC64;
MAHSAASGAA SAAHFEKKTP EVAHEEKKPP LPEEEDEDED MDALIEELES QDGHIDIEDD
EDGEPGGARP VPDELLTTDT RHGLTDAEVV ARRKKYGLNQ MKEEKENLVL KFLSYFVGPI
QFVMEAAAIL AAGLEDWVDF GVICALLLLN ACVGFVQEFQ AGSIVDELKK TLALKAVVLR
NGRLTEVEAP EVVPGDILQV EEGTIIPADG RIVTEEAFLQ VDQSAITGES LAVDKHKGDT
CYASSAVKRG EAFMVITATG DNTFVGRGPA LVNAASAGTG HFTEVLNGIG TVLLILVILT
LLVVWVSSFY RSNSIVTILE FTLAITIIGV PVGLPAVVTT TMAVGAAYLA KKKAIVQKLS
AIESLAGVEI LCSDKTGTLT KNKLSLAEPY CVSGVDPEDL MLTACLAASR KKKGIDAIDK
AFLKSLRYYP RAKSVLTQYK VLEFHPFDPV SKKVSAVVLS PQGERITCVK GAPLSVLKTV
EEDHPIPDEV DSAYKNKVAE FATRGFRSLG VARKRGEGSW EILGIMPCSD PPRHDTAKTI
NEAKTLGLSI KMLTGDAVGI ARETSRQLGL GTNVYNAERL GLGGGGTMPG SEVYDFVEAA
DGFAEVFPQH KYNVVEILQQ RGYLVAMTGD GVNDAPSLKK ADTGIAVEGA SDAARSAADI
VFLAPGLSAI IDALKTSRQI FHRMYAYVVY RIALSLHLEI FLGLWIAILN TSLNLQLVVF
IAIFADIATL AIAYDNAPFS KTPVKWNLPK LWGMSVLLGI VLAVGTWITL TTMLVGSENG
GIVQNFGRTH PVLFLEISLT ENWLIFITRA NGPFWSSIPS WQLSGAILLV DIIATLFTIF
GWFVGGQTSI VAVVRIWVFS FGCFCVLGGL YYLLQGSAGF DNMMHGKSPK KNQKQRSLED
FVVSLQRVST QHEKSS
