VATA_NEUCR
ID VATA_NEUCR Reviewed; 607 AA.
AC P11592; Q7RVE0;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=V-type proton ATPase catalytic subunit A;
DE Short=V-ATPase subunit A;
DE EC=7.1.2.2 {ECO:0000250|UniProtKB:P17255};
DE AltName: Full=V-ATPase 67 kDa subunit;
DE AltName: Full=Vacuolar proton pump subunit alpha;
GN Name=vma-1; ORFNames=18F11.090, NCU01207;
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=2971651; DOI=10.1016/s0021-9258(18)68175-x;
RA Bowman E.J., Tenney K., Bowman B.J.;
RT "Isolation of genes encoding the Neurospora vacuolar ATPase. Analysis of
RT vma-1 encoding the 67-kDa subunit reveals homology to other ATPases.";
RL J. Biol. Chem. 263:13994-14001(1988).
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: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (By similarity). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments (By
CC similarity). {ECO:0000250|UniProtKB:P17255}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:P17255};
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:P17255}.
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Vacuole membrane
CC {ECO:0000250|UniProtKB:P17255}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Membranes of
CC various intracellular acidic compartments.
CC {ECO:0000250|UniProtKB:P17255}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains 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; J03955; AAA33621.1; -; Genomic_DNA.
DR EMBL; AL670011; CAD21414.1; -; Genomic_DNA.
DR EMBL; CM002240; EAA32337.1; -; Genomic_DNA.
DR PIR; A30799; PXNCV7.
DR RefSeq; XP_961573.1; XM_956480.3.
DR AlphaFoldDB; P11592; -.
DR SMR; P11592; -.
DR STRING; 5141.EFNCRP00000004274; -.
DR PRIDE; P11592; -.
DR EnsemblFungi; EAA32337; EAA32337; NCU01207.
DR GeneID; 3877696; -.
DR KEGG; ncr:NCU01207; -.
DR VEuPathDB; FungiDB:NCU01207; -.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; P11592; -.
DR OMA; RIVKTFW; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0090465; P:arginine homeostasis; IEA:EnsemblFungi.
DR GO; GO:0090464; P:histidine homeostasis; IEA:EnsemblFungi.
DR GO; GO:0090463; P:lysine homeostasis; IEA:EnsemblFungi.
DR GO; GO:0019538; P:protein metabolic process; IEA:EnsemblFungi.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0007035; P:vacuolar acidification; IEA:EnsemblFungi.
DR Gene3D; 1.10.1140.10; -; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR InterPro; IPR031686; ATP-synth_a_Xtn.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR020003; ATPase_a/bsu_AS.
DR InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR InterPro; IPR005725; ATPase_V1-cplx_asu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022878; V-ATPase_asu.
DR PANTHER; PTHR43607; PTHR43607; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF02874; ATP-synt_ab_N; 1.
DR Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR SUPFAM; SSF50615; SSF50615; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Reference proteome; Translocase; Transport; Vacuole.
FT CHAIN 1..607
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000144589"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 607 AA; 67122 MW; 06B33A7B306112AA CRC64;
MAPQQNGAEV DGIHTGKIYS VSGPVVVAED MIGVAMYELV KVGHDQLVGE VIRINGDQAT
IQVYEETAGV MVGDPVLRTG KPLSVELGPG LLNNIYDGIQ RPLEKIAEAS NSIYIPRGIA
TPALDRKKKW EFTPTMKVGD HIAGGDVWGT VYENSFISVH KILLPPRARG TITRIAEKGE
YTVEEKILEV EFDGKKTEYP MMQTWPVRVP RPAAEKHSAN QPFLVGQRVL DALFPSVQGG
TVAIPGAFGC GKTVISQSVS KFSNSDVIVY VGCGERGNEM AEVLKDFPEL SIEVDGRKEP
IMKRTTLIAN TSNMPVAARE ASIYTGITVA EYFRDQGMNV AMMADSSSRW AEALREISGR
LGEMPADQGF PAYLGAKLAS FYERAGKVQA LGSPPREGSV SIVGAVSPPG GDFSDPVTSA
TLGIVQVFWG LDKKLAQRKH FPSINTSVSY SKYLTILDKW YEREYPDFPR LRDRIRQLLS
DSEELDQVVQ LVGKSALSDP DKITLDMATL IKEDFLQQNG YSDYDQFCPI WKTEWMMKLM
MGFHDEAQKA IAQGQNWNKV REATQDLQAQ LKSLKFEVPS EGQEKICKKY EAIQQQMLDK
FASVIDE
