VATF_SCHPO
ID VATF_SCHPO Reviewed; 120 AA.
AC O43046;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=V-type proton ATPase subunit F;
DE Short=V-ATPase subunit F;
DE AltName: Full=Vacuolar proton pump subunit F;
GN Name=vma7 {ECO:0000312|PomBase:SPBC3B9.18c};
GN ORFNames=SPBC3B9.18c {ECO:0000312|PomBase:SPBC3B9.18c};
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 [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: Subunit of the V1 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:P39111}.
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:P39111}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P39111};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17798.1; -; Genomic_DNA.
DR PIR; T40357; T40357.
DR RefSeq; NP_596676.1; NM_001022598.2.
DR AlphaFoldDB; O43046; -.
DR SMR; O43046; -.
DR BioGRID; 277498; 1.
DR STRING; 4896.SPBC3B9.18c.1; -.
DR MaxQB; O43046; -.
DR PaxDb; O43046; -.
DR PRIDE; O43046; -.
DR EnsemblFungi; SPBC3B9.18c.1; SPBC3B9.18c.1:pep; SPBC3B9.18c.
DR GeneID; 2540982; -.
DR KEGG; spo:SPBC3B9.18c; -.
DR PomBase; SPBC3B9.18c; vma7.
DR VEuPathDB; FungiDB:SPBC3B9.18c; -.
DR eggNOG; KOG3432; Eukaryota.
DR HOGENOM; CLU_135754_0_0_1; -.
DR InParanoid; O43046; -.
DR OMA; YTNAFPA; -.
DR PhylomeDB; O43046; -.
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:O43046; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISO:PomBase.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; ISO:PomBase.
DR GO; GO:1902600; P:proton transmembrane transport; IC:PomBase.
DR Gene3D; 3.40.50.10580; -; 1.
DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su.
DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk.
DR InterPro; IPR036906; ATPase_V1_fsu_sf.
DR Pfam; PF01990; ATP-synt_F; 1.
DR PIRSF; PIRSF015945; ATPase_V1_F_euk; 1.
DR SUPFAM; SSF159468; SSF159468; 1.
DR TIGRFAMs; TIGR01101; V_ATP_synt_F; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..120
FT /note="V-type proton ATPase subunit F"
FT /id="PRO_0000144811"
SQ SEQUENCE 120 AA; 13618 MW; 2D04228168125438 CRC64;
MSSQSYRERT LVSVIGDDDT VTGMLLAGTG QVNENGDKNF FIITQKTTDE QIAEAFDDYT
TKRKDIAIVL INQFAAERIR DRIENHVQAF PAVLEIPSKD DPYDPEKDSI LRRVRKIIGE
