VATA_SCHPO
ID VATA_SCHPO Reviewed; 619 AA.
AC P31406;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=V-type proton ATPase catalytic subunit A {ECO:0000303|PubMed:1441756};
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=vma1 {ECO:0000312|PomBase:SPAC343.05};
GN ORFNames=SPAC343.05 {ECO:0000312|PomBase:SPAC343.05};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=1441756; DOI=10.1002/yea.320080913;
RA Ghislain M., Bowman E.J.;
RT "Sequence of the genes encoding subunits A and B of the vacuolar H(+)-
RT ATPase of Schizosaccharomyces pombe.";
RL Yeast 8:791-799(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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}.
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DR EMBL; X68580; CAA48573.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB52268.1; -; Genomic_DNA.
DR PIR; S25334; S25334.
DR RefSeq; NP_593425.1; NM_001018858.2.
DR AlphaFoldDB; P31406; -.
DR SMR; P31406; -.
DR BioGRID; 278156; 4.
DR STRING; 4896.SPAC343.05.1; -.
DR iPTMnet; P31406; -.
DR MaxQB; P31406; -.
DR PaxDb; P31406; -.
DR PRIDE; P31406; -.
DR EnsemblFungi; SPAC343.05.1; SPAC343.05.1:pep; SPAC343.05.
DR GeneID; 2541660; -.
DR KEGG; spo:SPAC343.05; -.
DR PomBase; SPAC343.05; vma1.
DR VEuPathDB; FungiDB:SPAC343.05; -.
DR eggNOG; KOG1352; Eukaryota.
DR HOGENOM; CLU_008162_3_1_1; -.
DR InParanoid; P31406; -.
DR OMA; RIVKTFW; -.
DR PhylomeDB; P31406; -.
DR Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-SPO-77387; Insulin receptor recycling.
DR Reactome; R-SPO-917977; Transferrin endocytosis and recycling.
DR Reactome; R-SPO-9639288; Amino acids regulate mTORC1.
DR PRO; PR:P31406; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
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; IMP:PomBase.
DR GO; GO:0090464; P:histidine homeostasis; IMP:PomBase.
DR GO; GO:0090463; P:lysine homeostasis; IMP:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; ISM:PomBase.
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..619
FT /note="V-type proton ATPase catalytic subunit A"
FT /id="PRO_0000144590"
FT BINDING 258..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 619 AA; 68806 MW; 785A6F291609DF73 CRC64;
MAGGIELAKK AIRSLKNYDE HENRYGSIFS VSGPVVVAAN MLGCSMYELV RVGHEELVGE
VIRIHQDKCT IQVYEETSGL TVGDPVQRTG KPLSVELGPG LAETIYDGIQ RPLKQIFDKS
QSIYIPRGIN TESLNREHKW DFTPNKDLRI GDHVSGGDVF GSVFENSLFN DHKIMLPPRA
RGTVTYIAEA GSYHVDEKLL EVEFNGKKHS FSMLHTWPVR AARPVADNLT ANQPLLTGQR
VLDALYPCVQ GGTTAIPGAF GCGKTVISQS LSKYSNSDLI VYVGCGERGN EMAEVLMDFP
ELTIDINGKP EPIMKRTTLV ANTSNMPVAA REASIYTGIT LAEYYRDQGK NVSMMADSTS
RWAEALREIS GRLAEMPADS GYPAYLGAKL ASFYERAGRA RCLGSPDREG TVSIVGAVSP
PGGDFSDPVT SATLGIVQVF WGLDKKLAQR KHFPSINTSL SYSKYINALQ PWYEERVPGF
NTLRDQIKQI IQQEDSMLEI IQLVGKSALS ETDKVTLDIA GIIKNDFLQQ NGYSDYDRCC
PLYKTYHMMR NMIAYYTKAK SAVETGSVPW SKIKESTSDI FYELTSMKFE NPNEGEKEIV
EHYETLHKKI EDKFHTLTE
