ID   ATP7_NEUCR              Reviewed;         173 AA.
AC   Q7SI16; V5IRE7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=ATP synthase subunit d, mitochondrial;
GN   Name=atp7; ORFNames=NCU00636;
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 [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: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core, and
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/atp6 static
CC       relative to the rotary elements (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase d subunit family. {ECO:0000305}.
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DR   EMBL; CM002236; ESA44299.1; -; Genomic_DNA.
DR   EMBL; CM002236; ESA44300.1; -; Genomic_DNA.
DR   RefSeq; XP_011392798.1; XM_011394496.1.
DR   RefSeq; XP_011392799.1; XM_011394497.1.
DR   AlphaFoldDB; Q7SI16; -.
DR   SMR; Q7SI16; -.
DR   STRING; 5141.EFNCRP00000000926; -.
DR   EnsemblFungi; ESA44299; ESA44299; NCU00636.
DR   EnsemblFungi; ESA44300; ESA44300; NCU00636.
DR   GeneID; 3881973; -.
DR   KEGG; ncr:NCU00636; -.
DR   VEuPathDB; FungiDB:NCU00636; -.
DR   HOGENOM; CLU_080463_0_0_1; -.
DR   InParanoid; Q7SI16; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:EnsemblFungi.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   Gene3D; 6.10.280.70; -; 1.
DR   InterPro; IPR008689; ATP_synth_F0_dsu_mt.
DR   InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
DR   PANTHER; PTHR12700; PTHR12700; 1.
DR   Pfam; PF05873; Mt_ATP-synt_D; 1.
DR   PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
DR   SUPFAM; SSF161065; SSF161065; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome; Transport.
FT   CHAIN           1..173
FT                   /note="ATP synthase subunit d, mitochondrial"
FT                   /id="PRO_0000071679"
SQ   SEQUENCE   173 AA;  19365 MW;  99DA81C7FE006440 CRC64;
     MAARNAALKV DWAKITTSLG LRGQTAASLQ AFKKRNDDAR RKLQQLSELP TTVDFAAYRS
     TLKNQAIVNE IEKRFTSFKP ATYDVNRQLK AIEAFEVEAI KNAEATKTKV DLELKDLEKT
     LTNIETARPF DELTVDEVAA AEPSIDEKTS KLVSKGRWSV PGYKERFGDL SVL