PMA1_CANAX
ID PMA1_CANAX Reviewed; 895 AA.
AC P28877;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Plasma membrane ATPase 1;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump 1;
GN Name=PMA1;
OS Candida albicans (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5476;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1834633; DOI=10.1128/jb.173.21.6826-6836.1991;
RA Monk B.C., Kurtz M.B., Marrinan J.A., Perlin D.S.;
RT "Cloning and characterization of the plasma membrane H(+)-ATPase from
RT Candida albicans.";
RL J. Bacteriol. 173:6826-6836(1991).
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; M74075; AAA34319.1; -; Genomic_DNA.
DR PIR; A41336; PXCKP.
DR AlphaFoldDB; P28877; -.
DR SMR; P28877; -.
DR VEuPathDB; FungiDB:C3_00720W_A; -.
DR VEuPathDB; FungiDB:CAWG_02408; -.
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:EnsemblFungi.
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:1901691; F:proton binding; IEA:EnsemblFungi.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0051453; P:regulation of intracellular pH; IEA:EnsemblFungi.
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 ATP-binding; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..895
FT /note="Plasma membrane ATPase 1"
FT /id="PRO_0000046266"
FT TOPO_DOM 1..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 114..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..137
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..290
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..301
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..324
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..715
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 716..731
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..751
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 752..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..834
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..851
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 852..895
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 355
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 611
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 615
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 895 AA; 97460 MW; 2CF2451DD3CB25B1 CRC64;
MSATEPTNEK VDKIVSDDED EDIDQLVADL QSNPGAGDEE EEEENDSSFK AVPEELLQTD
PRVGLTDDEV TKRRKRYGLN QMAEEQENLV LKFVMFFVGP IQFVMEAAAV LAAGLEDWVD
FGVICALLLL NAFVGFIQEY QAGSIVDELK KTLANSALVV RNGQLVEIPA NEVVPGDILQ
LEDGTVIPTD GRIVSEDCLL QVDQSAITGE SLAVDKRSGD SCYSSSTVKT GEAFMIVTAT
GDSTFVGRAA ALVNKASAGT GHFTEVLNGI GTTLLVFVIV TLLVVWVACF YRTVRIVPIL
RYTLAITIIG VPVGLPAVVT TTMAVGAAYL AKKQAIVQKL SAIESLAGVE ILCSDKTGTL
TKNKLSLHEP YTVEGVEPDD LMLTACLAAS RKKKGLDAID KAFLKSLINY PRAKAALPKY
KVIEFQPFDP VSKKVTAIVE SPEGERIICV KGAPLFVLKT VEDDHPIPED VHENYQNTVA
EFASRGFRSL GVARKRGEGH WEILGIMPCM DPPRDDTAAT VNEARRLGLR VKMLTGDAVG
IAKETCRQLG LGTNIYDADR LGLSGGGDMA GSEIADFVEN ADGFAEGFPT NKYNAVEILQ
SRGYLVAMTG DGVNDAPSLK KADTGIAVEG ATDAARSAAD IVFLAPGLSA IIDALKTSRQ
IFHRMYSYVV YRIALSLHLE LFLGLWIAIL NRSLDINLIV FIAIFADVAT LAIAYDNAPY
DPKPVKWNLP RLWGMSIVLG IILAIGTWIT LTTMLLPKGG IIQNFGGLDG ILFLQISLTE
NWLIFVTRAQ GPFWSSIPSW QLSGAVLIVD IIATCFTLFG WWSQNWTDIV TVVRTWIWSF
GVFCVMGGAY YLMSTSEAFD NFCNGRKPQQ HTDKRSLEDF LVSMQRVSTQ HEKST
