ATP6_NEUCR
ID ATP6_NEUCR Reviewed; 261 AA.
AC P37212; M1RM82; Q35133;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Precursor;
GN Name=atp-6; Synonyms=oli2; ORFNames=NCM020, NCU16025;
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], AND REVISION OF GENE MODEL.
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. Key component of the
CC proton channel; it may play a direct role in the translocation of
CC protons across the membrane.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA31964.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; K02655; AAA31964.2; ALT_SEQ; Genomic_DNA.
DR EMBL; L14642; AAA66053.1; -; Genomic_DNA.
DR EMBL; KC683708; AGG16014.1; -; Genomic_DNA.
DR PIR; S44066; S44066.
DR PIR; T50467; T50467.
DR RefSeq; YP_009126726.1; NC_026614.1.
DR AlphaFoldDB; P37212; -.
DR SMR; P37212; -.
DR STRING; 367110.P37212; -.
DR EnsemblFungi; AGG16014; AGG16014; NCU16025.
DR GeneID; 23681580; -.
DR KEGG; ncr:NCU16025; -.
DR VEuPathDB; FungiDB:NCU16025; -.
DR InParanoid; P37212; -.
DR Proteomes; UP000001805; Mitochondrion.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
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 Gene3D; 1.20.120.220; -; 1.
DR HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR InterPro; IPR000568; ATP_synth_F0_asu.
DR InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR InterPro; IPR035908; F0_ATP_A_sf.
DR PANTHER; PTHR11410; PTHR11410; 1.
DR Pfam; PF00119; ATP-synt_A; 1.
DR PRINTS; PR00123; ATPASEA.
DR SUPFAM; SSF81336; SSF81336; 1.
DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR PROSITE; PS00449; ATPASE_A; 1.
PE 3: Inferred from homology;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT PROPEP 1..14
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002616"
FT CHAIN 15..261
FT /note="ATP synthase subunit a"
FT /id="PRO_0000002617"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 30
FT /note="A -> T (in Ref. 1; AAA31964)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="H -> Y (in Ref. 1; AAA31964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 28858 MW; 8F0283DC4F3CFFE9 CRC64;
MSTLSFNNIS TEVLSPLNQF EIRDLLSIDA LGNLHISITN IGFYLTIGAF FFLVINLLSI
NYNRLVSNSW SISQESLYAT IHSIVTSQIN PRNGQIYFPF IYTLFIFILI NNLIGMVPYS
FASTSHFVVT FALSFTIVLG ATILGFQKHG LEFFSLLVPA GCPLALLPLL VLIEFISYLA
RNISLGLRLA ANILSGHMLL HILAGFTYNI MTSGIIFFFL GLIPLAFIIA FSGLELGIAF
IQAQVFVVLT SGYIKDALDL H
