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VA0D_NEUCR
ID   VA0D_NEUCR              Reviewed;         364 AA.
AC   P53659; Q7RV58;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=V-type proton ATPase subunit d;
DE            Short=V-ATPase subunit d;
DE   AltName: Full=V-ATPase 41 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit d;
GN   Name=vma-6 {ECO:0000303|PubMed:8611592}; ORFNames=B19C19.060, NCU03395;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8611592; DOI=10.1016/0005-2728(95)00144-1;
RA   Melnik V.I., Bowman B.J.;
RT   "Isolation of the vma-6 gene encoding a 41 kDa subunit of the Neurospora
RT   crassa vacuolar ATPase, and an adjoining gene encoding a ribosome-
RT   associated protein.";
RL   Biochim. Biophys. Acta 1273:77-83(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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; U36470; AAB02771.1; -; Genomic_DNA.
DR   EMBL; AL669992; CAD21144.1; -; Genomic_DNA.
DR   EMBL; CM002237; EAA27606.1; -; Genomic_DNA.
DR   PIR; T47198; T47198.
DR   RefSeq; XP_956842.1; XM_951749.2.
DR   AlphaFoldDB; P53659; -.
DR   SMR; P53659; -.
DR   STRING; 5141.EFNCRP00000002659; -.
DR   PRIDE; P53659; -.
DR   EnsemblFungi; EAA27606; EAA27606; NCU03395.
DR   GeneID; 3872989; -.
DR   KEGG; ncr:NCU03395; -.
DR   VEuPathDB; FungiDB:NCU03395; -.
DR   HOGENOM; CLU_051277_0_0_1; -.
DR   InParanoid; P53659; -.
DR   OMA; MLSRAED; -.
DR   Proteomes; UP000001805; Chromosome 6, Linkage Group II.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
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; IEA:EnsemblFungi.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
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..364
FT                   /note="V-type proton ATPase subunit d"
FT                   /id="PRO_0000119358"
SQ   SEQUENCE   364 AA;  41008 MW;  78F32528C39299A8 CRC64;
     MEGLLFNVNN GYIEGIVRGY RNSLLTSTNY TNMTQCESID DLKLQLGPAY GDFLASLPPK
     PSTSALAAKT TDKLVSEFRY VRANAAGSLA KFMDYLTYGY MIDNVALLIT GTLHERDTRE
     LLERCHPLGW FETMPVLCVA TNIEELYNSV MIETPLAPYF KSSLSLQDLD ELNIEIVRNT
     LYKNYLEDFY HFVNTHPDMA GTPTAEVMSE LLEFEADRRA INITLNSFGT ELSKADRKKL
     YPNFGQLYPE GTLMLSRADD FEGVRLAVEG VADYKSFFDA AGLGGGPSGP GNMGGGGTEG
     KSLEDMFYQK EMEISKMAFT RQFTYAIVYA WVKLREQEIR NITWIAECIA QNQKERINNY
     ISVF
 
 
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