ID   VPP1_NEUCR              Reviewed;         856 AA.
AC   Q01290; Q7RV48;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=V-type proton ATPase subunit a;
DE            Short=V-ATPase a subunit;
DE   AltName: Full=Vacuolar ATPase 98 kDa subunit;
DE   AltName: Full=Vacuolar proton pump a subunit;
DE   AltName: Full=Vacuolar proton translocating ATPase subunit a;
GN   Name=vph-1; Synonyms=vph1; ORFNames=B8J24.100, NCU03463;
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].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA   Bowman E.J.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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).
CC   -!- FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments (By similarity).
CC       {ECO:0000250|UniProtKB:P32563}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC       catalytic V1 complex (components A to H) attached to an integral
CC       membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC       VOA1). {ECO:0000250|UniProtKB:P32563}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P32563};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC       {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; U36396; AAA93078.1; -; Genomic_DNA.
DR   EMBL; AL669990; CAD21112.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA26818.1; -; Genomic_DNA.
DR   RefSeq; XP_956054.1; XM_950961.2.
DR   AlphaFoldDB; Q01290; -.
DR   SMR; Q01290; -.
DR   STRING; 5141.EFNCRP00000002737; -.
DR   PRIDE; Q01290; -.
DR   EnsemblFungi; EAA26818; EAA26818; NCU03463.
DR   GeneID; 3872192; -.
DR   KEGG; ncr:NCU03463; -.
DR   VEuPathDB; FungiDB:NCU03463; -.
DR   HOGENOM; CLU_005230_0_0_1; -.
DR   InParanoid; Q01290; -.
DR   OMA; FSYDRAR; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   InterPro; IPR002490; V-ATPase_116kDa_su.
DR   InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR   PANTHER; PTHR11629; PTHR11629; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
DR   PIRSF; PIRSF001293; ATP6V0A1; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..856
FT                   /note="V-type proton ATPase subunit a"
FT                   /id="PRO_0000119222"
FT   TOPO_DOM        1..409
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..430
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        448..460
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        461..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..544
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        545..564
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        565..582
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        583..603
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        604..648
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        649..668
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        669..738
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        739..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        764..784
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        785..823
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        824..856
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          689..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   856 AA;  97992 MW;  F75E3737A7DA3DE8 CRC64;
     MAPKQDTPFR SADMSMVQLY ISNEIGREVC NALGELGLVH FRDLNSELSA FQRAFTQDIR
     RLDNVERQLR YFHSQMEKAG IPLRKFDPDV DILTPPTTTE IDELAERAQT LEQRVSSLNE
     SYETLKKREV ELTEWRWVLR EAGGFFDRAH GNVEEIRAST DNDDAPLLQD VEQHNTAADV
     ERSFSGMNIG FVAGVIGRDR VDAFERILWR TLRGNLYMNQ AEIPEPLIDP TINEPVLKNV
     FVIFAHGKEI LAKIRRISES MGAEVYNVDE HSDLRRDQVH EVNARLEDVQ NVLRNTQQTL
     EAELAQISQS LSAWMITISK EKAVYNTLNL FSYDRARRTL IAEGWCPTND LPLIRSTLQD
     VNNRAGLSVP SIINEIRTNK TPPTYLKTNK FTEAFQTIVN AYGTATYQEV NPAIPVIVTF
     PFLFAVMFGD FGHALIMLCA ALAMIYWEKP LKKVTFELFA MVFYGRYIVL VMAVFSVYTG
     LIYNDVFSKS MTLFDSQWKW VVPENFKEGM TVKAVLREPN GYRYPFGLDW RWHGTENELL
     FINSYKMKMA IILGWAHMTY SLCFSYINAR HFKRPIDIWG NFVPGMIFFQ SIFGYLVLCI
     IYKWSVDWFG TGRQPPGLLN MLIYMFLQPG TLDGGVELYP GQATVQVILL LLAVIQVPIL
     LFLKPFYLRW ENNRARAKGY RGIGERSRVS ALDEDDEEDP SNGDDYEGAA MLTHDEHGDG
     EHEEFEFGEV MIHQVIHTIE FCLNSVSHTA SYLRLWALSL AHQQLSAVLW SMTMAKALES
     KGLGGAIFLV VAFAMFFVLS VIILIIMEGV SAMLHSLRLA WVESFSKFAE FGGWPFTPFS
     FKQQLEESEE LKEYIG