PMA1_NEUCR
ID PMA1_NEUCR Reviewed; 920 AA.
AC P07038; Q7RV59;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Plasma membrane ATPase;
DE EC=7.1.2.1;
DE AltName: Full=Proton pump;
GN Name=pma-1; ORFNames=B1D1.210, NCU01680;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2876429; DOI=10.1073/pnas.83.20.7693;
RA Hager K.M., Mandala S.M., Davenport J.W., Speicher D.W., Benz E.J. Jr.,
RA Slayman C.W.;
RT "Amino acid sequence of the plasma membrane ATPase of Neurospora crassa:
RT deduction from genomic and cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7693-7697(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2876992; DOI=10.1016/s0021-9258(18)66801-2;
RA Addison R.;
RT "Primary structure of the Neurospora plasma membrane H+-ATPase deduced from
RT the gene sequence. Homology to Na+/K+-, Ca2+-, and K+-ATPase.";
RL J. Biol. Chem. 261:14896-14901(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [5]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2524486; DOI=10.1016/s0021-9258(18)60541-1;
RA Pardo J.P., Slayman C.W.;
RT "Cysteine 532 and cysteine 545 are the N-ethylmaleimide-reactive residues
RT of the Neurospora plasma membrane H+-ATPase.";
RL J. Biol. Chem. 264:9373-9379(1989).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, AND TOPOLOGY.
RX PubMed=2144525; DOI=10.1016/s0021-9258(17)46200-4;
RA Scarborough G.A., Hennessey J.P. Jr.;
RT "Identification of the major cytoplasmic regions of the Neurospora crassa
RT plasma membrane H(+)-ATPase using protein chemical techniques.";
RL J. Biol. Chem. 265:16145-16149(1990).
RN [7]
RP TOPOLOGY.
RX PubMed=1830591; DOI=10.1016/s0021-9258(18)98749-1;
RA Rao U.S., Hennessey J.P. Jr., Scarborough G.A.;
RT "Identification of the membrane-embedded regions of the Neurospora crassa
RT plasma membrane H(+)-ATPase.";
RL J. Biol. Chem. 266:14740-14746(1991).
RN [8]
RP TOPOLOGY.
RX PubMed=1386255; DOI=10.1016/0005-2736(92)90020-m;
RA Rao U.S., Bauzon D.D., Scarborough G.A.;
RT "Cytoplasmic location of amino acids 359-440 of the Neurospora crassa
RT plasma membrane H(+)-ATPase.";
RL Biochim. Biophys. Acta 1108:153-158(1992).
RN [9]
RP TOPOLOGY.
RX PubMed=8106434; DOI=10.1016/s0021-9258(17)41943-0;
RA Lin A., Addison R.;
RT "Topology of the Neurospora plasma membrane H(+)-ATPase. Localization of a
RT transmembrane segment.";
RL J. Biol. Chem. 269:3887-3890(1994).
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; M14085; AAA33561.1; -; Genomic_DNA.
DR EMBL; J02602; AAA33563.1; -; Genomic_DNA.
DR EMBL; AL355927; CAB91270.1; -; Genomic_DNA.
DR EMBL; CM002237; EAA27650.1; -; Genomic_DNA.
DR PIR; A26497; PXNCP.
DR RefSeq; XP_956886.1; XM_951793.3.
DR PDB; 1MHS; EM; 8.00 A; A/B=1-920.
DR PDBsum; 1MHS; -.
DR AlphaFoldDB; P07038; -.
DR SMR; P07038; -.
DR STRING; 5141.EFNCRP00000001834; -.
DR TCDB; 3.A.3.3.1; the p-type atpase (p-atpase) superfamily.
DR PRIDE; P07038; -.
DR EnsemblFungi; EAA27650; EAA27650; NCU01680.
DR GeneID; 3873048; -.
DR KEGG; ncr:NCU01680; -.
DR VEuPathDB; FungiDB:NCU01680; -.
DR HOGENOM; CLU_002360_6_0_1; -.
DR InParanoid; P07038; -.
DR EvolutionaryTrace; P07038; -.
DR Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0015662; F:P-type ion transporter activity; IBA:GO_Central.
DR GO; GO:0008553; F:P-type proton-exporting transporter activity; IBA:GO_Central.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:InterPro.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
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 3D-structure; ATP-binding; Cell membrane; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..920
FT /note="Plasma membrane ATPase"
FT /id="PRO_0000046268"
FT TOPO_DOM 1..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 116..138
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 139..140
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 141..160
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TOPO_DOM 161..291
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 292..314
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 315..321
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 322..354
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 355..687
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 688..713
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 714..720
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 721..738
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 739..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 755..779
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 780..806
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 807..826
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TRANSMEM 827..847
FT /note="Helical; Name=9"
FT /evidence="ECO:0000305"
FT TOPO_DOM 848..853
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 854..878
FT /note="Helical; Name=10"
FT /evidence="ECO:0000305"
FT TOPO_DOM 879..920
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 378
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 634
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 638
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="G -> A (in Ref. 2; AAA33563)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="I -> M (in Ref. 2; AAA33563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 920 AA; 99887 MW; 2A8F035F26337CF7 CRC64;
MADHSASGAP ALSTNIESGK FDEKAAEAAA YQPKPKVEDD EDEDIDALIE DLESHDGHDA
EEEEEEATPG GGRVVPEDML QTDTRVGLTS EEVVQRRRKY GLNQMKEEKE NHFLKFLGFF
VGPIQFVMEG AAVLAAGLED WVDFGVICGL LLLNAVVGFV QEFQAGSIVD ELKKTLALKA
VVLRDGTLKE IEAPEVVPGD ILQVEEGTII PADGRIVTDD AFLQVDQSAL TGESLAVDKH
KGDQVFASSA VKRGEAFVVI TATGDNTFVG RAAALVNAAS GGSGHFTEVL NGIGTILLIL
VIFTLLIVWV SSFYRSNPIV QILEFTLAIT IIGVPVGLPA VVTTTMAVGA AYLAKKKAIV
QKLSAIESLA GVEILCSDKT GTLTKNKLSL HDPYTVAGVD PEDLMLTACL AASRKKKGID
AIDKAFLKSL KYYPRAKSVL SKYKVLQFHP FDPVSKKVVA VVESPQGERI TCVKGAPLFV
LKTVEEDHPI PEEVDQAYKN KVAEFATRGF RSLGVARKRG EGSWEILGIM PCMDPPRHDT
YKTVCEAKTL GLSIKMLTGD AVGIARETSR QLGLGTNIYN AERLGLGGGG DMPGSEVYDF
VEAADGFAEV FPQHKYNVVE ILQQRGYLVA MTGDGVNDAP SLKKADTGIA VEGSSDAARS
AADIVFLAPG LGAIIDALKT SRQIFHRMYA YVVYRIALSI HLEIFLGLWI AILNRSLNIE
LVVFIAIFAD VATLAIAYDN APYSQTPVKW NLPKLWGMSV LLGVVLAVGT WITVTTMYAQ
GENGGIVQNF GNMDEVLFLQ ISLTENWLIF ITRANGPFWS SIPSWQLSGA IFLVDILATC
FTIWGWFEHS DTSIVAVVRI WIFSFGIFCI MGGVYYILQD SVGFDNLMHG KSPKGNQKQR
SLEDFVVSLQ RVSTQHEKSQ
