ID   VATD_SCHPO              Reviewed;         285 AA.
AC   O59823;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 141.
DE   RecName: Full=V-type proton ATPase subunit D;
DE            Short=V-ATPase subunit D;
DE   AltName: Full=Vacuolar proton pump subunit D;
GN   Name=vma8; ORFNames=SPCC965.03;
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).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
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:P32610}.
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:P32610}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:16823372};
CC       Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA19063.1; -; Genomic_DNA.
DR   PIR; T41656; T41656.
DR   RefSeq; NP_588513.1; NM_001023502.2.
DR   AlphaFoldDB; O59823; -.
DR   SMR; O59823; -.
DR   BioGRID; 276140; 5.
DR   STRING; 4896.SPCC965.03.1; -.
DR   iPTMnet; O59823; -.
DR   MaxQB; O59823; -.
DR   PaxDb; O59823; -.
DR   PRIDE; O59823; -.
DR   EnsemblFungi; SPCC965.03.1; SPCC965.03.1:pep; SPCC965.03.
DR   GeneID; 2539581; -.
DR   KEGG; spo:SPCC965.03; -.
DR   PomBase; SPCC965.03; vma8.
DR   VEuPathDB; FungiDB:SPCC965.03; -.
DR   eggNOG; KOG1647; Eukaryota.
DR   HOGENOM; CLU_069688_0_1_1; -.
DR   InParanoid; O59823; -.
DR   OMA; SKNIMGV; -.
DR   PhylomeDB; O59823; -.
DR   Reactome; R-SPO-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
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:O59823; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0032153; C:cell division site; HDA:PomBase.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:PomBase.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
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; IEA:InterPro.
DR   GO; GO:1902600; P:proton transmembrane transport; IC:PomBase.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   HAMAP; MF_00271; ATP_synth_D_arch; 1.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   1: Evidence at protein level;
KW   Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transport; Vacuole.
FT   CHAIN           1..285
FT                   /note="V-type proton ATPase subunit D"
FT                   /id="PRO_0000144243"
FT   REGION          208..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..285
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         219
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   285 AA;  32219 MW;  5B95DF17D1887DD9 CRC64;
     MASKQRENVF PTRMTLTTMK TRLKGAQTGH SLLKRKSEAL KKRFREIVVN IEQAKQKMGR
     VMQIAAFSMA EVGFAMGNNI NFEIQQSVKQ PRLRVRSKQE NISGVFLPTF EMNLDESIDD
     FQLTGLGKGG QQIQKARQVY EKAVETLVQL ASYQSAFVLL GDVLQMTNRR VNSIEHIIIP
     RLENTIKYIE SELEELERED FTRLKKVQKT KENAEKADSV TKEEHQGGSN TLQQTKDVGG
     AIAPAAEVGK EVINEVENSK DDTYSLPSTS TDDEEENDSD EEVIF