VATE_SCHPO
ID VATE_SCHPO Reviewed; 227 AA.
AC O13687;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 139.
DE RecName: Full=V-type proton ATPase subunit E;
DE Short=V-ATPase subunit E;
DE AltName: Full=Vacuolar proton pump subunit E;
GN Name=vma4 {ECO:0000312|PomBase:SPAC11E3.07};
GN ORFNames=SPAC11E3.07 {ECO:0000312|PomBase:SPAC11E3.07};
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:P22203}.
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, ECO:0000250|UniProtKB:P22203}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P22203};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P22203}; Cytoplasmic
CC side {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11186.1; -; Genomic_DNA.
DR PIR; T37535; T37535.
DR RefSeq; NP_594932.1; NM_001020363.2.
DR AlphaFoldDB; O13687; -.
DR SMR; O13687; -.
DR BioGRID; 279438; 1.
DR STRING; 4896.SPAC11E3.07.1; -.
DR iPTMnet; O13687; -.
DR MaxQB; O13687; -.
DR PaxDb; O13687; -.
DR PRIDE; O13687; -.
DR EnsemblFungi; SPAC11E3.07.1; SPAC11E3.07.1:pep; SPAC11E3.07.
DR GeneID; 2543000; -.
DR KEGG; spo:SPAC11E3.07; -.
DR PomBase; SPAC11E3.07; vma4.
DR VEuPathDB; FungiDB:SPAC11E3.07; -.
DR eggNOG; KOG1664; Eukaryota.
DR HOGENOM; CLU_073641_0_0_1; -.
DR InParanoid; O13687; -.
DR OMA; AIDTQYE; -.
DR PhylomeDB; O13687; -.
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:O13687; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000329; C:fungal-type vacuole membrane; 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; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IC:PomBase.
DR GO; GO:0007035; P:vacuolar acidification; ISO:PomBase.
DR Gene3D; 3.30.2320.30; -; 1.
DR HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
DR PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport; Vacuole.
FT CHAIN 1..227
FT /note="V-type proton ATPase subunit E"
FT /id="PRO_0000117309"
SQ SEQUENCE 227 AA; 25742 MW; B5180B4FC02080CB CRC64;
MSLSDEQVQA EMHKMVSFIK QEALEKAKEI HTLSEEEFQV EKAKIVREQC DAIDQTYDMK
LKRASMAQKI AKSNVLNKSR LEILNSKQKV IDDIFSRVEK KLDGIEQKKD AYTKFMADLI
VQAMELLGEP VGIVYSRQRD AEIVKAAIPK ATEVLKSKNG SIDYELDAET DDFLNDSVLG
GVVLVGLGGK IRVDNTLRAR LEIVKEEALP EIRRLLFGEN PNRKFDN