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Database: UniProt
Entry: P07038
LinkDB: P07038
Original site: P07038 
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   29-SEP-2021, entry version 183.
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;
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;
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;
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;
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;
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   SMR; P07038; -.
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   Proteomes; UP000001805; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008553; F:P-type proton-exporting transporter activity; 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   METAL           634
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250"
FT   METAL           638
FT                   /note="Magnesium"
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
//
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