ID   VA0D_SCHPO              Reviewed;         343 AA.
AC   O13753;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 149.
DE   RecName: Full=V-type proton ATPase subunit d;
DE            Short=V-ATPase subunit d;
DE   AltName: Full=V-ATPase 39 kDa subunit;
DE   AltName: Full=V-ATPase subunit M39;
DE   AltName: Full=Vacuolar proton pump subunit d;
GN   Name=vma6; ORFNames=SPAC17A2.03c;
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 V0 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). This
CC       subunit is a non-integral membrane component of the membrane pore
CC       domain and is required for proper assembly of the V0 sector (By
CC       similarity). Might be involved in the regulated assembly of V1 subunits
CC       onto the membrane sector or alternatively may prevent the passage of
CC       protons through V0 pores (By similarity).
CC       {ECO:0000250|UniProtKB:P32366}.
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:P32366}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P32366};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P32366}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {ECO:0000305}.
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DR   EMBL; CU329670; CAB16567.1; -; Genomic_DNA.
DR   PIR; T37804; T37804.
DR   RefSeq; NP_594237.1; NM_001019660.2.
DR   AlphaFoldDB; O13753; -.
DR   SMR; O13753; -.
DR   BioGRID; 278848; 1.
DR   STRING; 4896.SPAC17A2.03c.1; -.
DR   iPTMnet; O13753; -.
DR   MaxQB; O13753; -.
DR   PaxDb; O13753; -.
DR   EnsemblFungi; SPAC17A2.03c.1; SPAC17A2.03c.1:pep; SPAC17A2.03c.
DR   GeneID; 2542384; -.
DR   KEGG; spo:SPAC17A2.03c; -.
DR   PomBase; SPAC17A2.03c; vma6.
DR   VEuPathDB; FungiDB:SPAC17A2.03c; -.
DR   eggNOG; KOG2957; Eukaryota.
DR   HOGENOM; CLU_051277_0_0_1; -.
DR   InParanoid; O13753; -.
DR   OMA; MLSRAED; -.
DR   PhylomeDB; O13753; -.
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:O13753; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 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; ISO:PomBase.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport; Vacuole.
FT   CHAIN           1..343
FT                   /note="V-type proton ATPase subunit d"
FT                   /id="PRO_0000119359"
SQ   SEQUENCE   343 AA;  39323 MW;  F8936922C7EBA691 CRC64;
     MDALSFNTNS GYIEALVRGY ESALLEQHIY SNLSQCESLE DFRLQLSSTD YGGFLANQSK
     LTSSIISAKA TEKLLDEFDL IRRQADETLS KFMDYITYAY MIDNIMLLLT GTVNGQDTHD
     LLERCHPLGW FETLPALCVA TNVEELYSVV LIETPLAPYF KDCLSADDLD EQHIEIIRNT
     LYKAYLEDFY NFCKKIGACT ADTMLPILEF EADRRAITIT INSFGTELSK EERAKMYPSF
     GRLYPFSTSI LARAENAGDV ENACSLVKEY SDFFDQNSQK SLDDHFNEKE VELNKLAFLQ
     QFHYGIVYAF LKLREQEIRN LTWIAECISQ NQRDRALNIV PIL