ID   ATP8_NEUCR              Reviewed;          54 AA.
AC   Q08656; M1QL73;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=ATP synthase protein 8;
DE   AltName: Full=A6L;
DE   AltName: Full=F-ATPase subunit 8;
GN   Name=atp-8; ORFNames=NCM022, NCU16024;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OG   Mitochondrion.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=6238172; DOI=10.1016/0022-2836(84)90235-3;
RA   Morelli G., Macino G.;
RT   "Two intervening sequences in the ATPase subunit 6 gene of Neurospora
RT   crassa. A short intron (93 base-pairs) and a long intron that is stable
RT   after excision.";
RL   J. Mol. Biol. 178:491-507(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=8082202; DOI=10.1007/bf00351671;
RA   Collins R.A., Olive J.E.;
RT   "Revision of the nucleotide sequence and RNA splicing pathway of the
RT   Neurospora mitochondrial gene encoding ATPase subunit 6.";
RL   Curr. Genet. 25:514-518(1994).
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).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RA   Kennell J.C., Collins R.A., Griffiths A.J.F., Nargang F.E.;
RT   "Mitochondrial genetics of Neurospora.";
RL   (In) Kueck U. (eds.);
RL   The Mycota II, Genetics and Biotechnology (2nd edition), pp.95-112,
RL   Springer-Verlag, Berlin-Heidelberg (2004).
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 F(0)
CC       - containing the membrane proton channel, linked together by a central
CC       stalk and a peripheral stalk. During catalysis, ATP synthesis in the
CC       catalytic domain of F(1) is coupled via a rotary mechanism of the
CC       central stalk subunits to proton translocation. Part of the complex
CC       F(0) domain. Minor subunit located with subunit a in the membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR   EMBL; K02655; AAA31965.2; -; Genomic_DNA.
DR   EMBL; L14642; AAA66052.1; -; Genomic_DNA.
DR   EMBL; KC683708; AGG16013.1; -; Genomic_DNA.
DR   PIR; S44065; S44065.
DR   RefSeq; YP_009126725.1; NC_026614.1.
DR   AlphaFoldDB; Q08656; -.
DR   SMR; Q08656; -.
DR   STRING; 367110.Q08656; -.
DR   EnsemblFungi; AGG16013; AGG16013; NCU16024.
DR   GeneID; 23681579; -.
DR   KEGG; ncr:NCU16024; -.
DR   VEuPathDB; FungiDB:NCU16024; -.
DR   InParanoid; Q08656; -.
DR   Proteomes; UP000001805; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   InterPro; IPR009230; ATP_synth_su8_fun.
DR   PANTHER; PTHR36101; PTHR36101; 1.
DR   Pfam; PF05933; Fun_ATP-synt_8; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..54
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195602"
FT   TRANSMEM        13..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   54 AA;  6479 MW;  3AB1E03E63F3D87D CRC64;
     MPQLVPFYFV NEITFTFVII TLMVYILSKY ILPRFVRLFL SRTFISKLSD ISKK