ATP9_NEUCR
ID ATP9_NEUCR Reviewed; 147 AA.
AC P00842; Q7S5B4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=ATP synthase subunit 9, mitochondrial;
DE AltName: Full=Lipid-binding protein;
DE Flags: Precursor;
GN Name=oli; Synonyms=atp-9, atp9, prl-1; ORFNames=B13D24.340, NCU02250;
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 [MRNA].
RX PubMed=6329691; DOI=10.1002/j.1460-2075.1982.tb01209.x;
RA Viebrock A., Perz A., Sebald W.;
RT "The imported preprotein of the proteolipid subunit of the mitochondrial
RT ATP synthase from Neurospora crassa. Molecular cloning and sequencing of
RT the mRNA.";
RL EMBO J. 1:565-571(1982).
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).
RN [4]
RP PROTEIN SEQUENCE OF 67-147.
RA Sebald W., Hoppe J., Wachter E.;
RT "Amino acid sequence of the ATPase proteolipid from mitochondria,
RT chloroplasts and bacteria (wild type and mutants).";
RL (In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
RL Function and molecular aspects of biomembrane transport, pp.63-74,
RL Elsevier, Amsterdam (1979).
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. A homomeric c-ring of probably 10 subunits is part of the
CC complex rotary element.
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 -!- INTERACTION:
CC P00842; Q02776: TIM50; Xeno; NbExp=5; IntAct=EBI-9084292, EBI-30302;
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
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DR EMBL; V00864; CAA24230.1; -; mRNA.
DR EMBL; BX908789; CAF05899.1; -; Genomic_DNA.
DR EMBL; CM002242; EAA30658.1; -; Genomic_DNA.
DR PIR; S07173; LWNCA.
DR RefSeq; XP_959894.1; XM_954801.3.
DR AlphaFoldDB; P00842; -.
DR SMR; P00842; -.
DR BioGRID; 1977663; 7.
DR IntAct; P00842; 2.
DR MINT; P00842; -.
DR STRING; 5141.EFNCRP00000003180; -.
DR EnsemblFungi; EAA30658; EAA30658; NCU02250.
DR GeneID; 3876057; -.
DR KEGG; ncr:NCU02250; -.
DR VEuPathDB; FungiDB:NCU02250; -.
DR HOGENOM; CLU_116822_0_0_1; -.
DR InParanoid; P00842; -.
DR OMA; ASQMATK; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; 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; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW CF(0); Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Mitochondrion; Reference proteome;
KW Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT TRANSIT 1..66
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:6329691, ECO:0000269|Ref.4"
FT CHAIN 67..147
FT /note="ATP synthase subunit 9, mitochondrial"
FT /id="PRO_0000002573"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 131
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
FT VARIANT 127
FT /note="F -> S (in oligomycin-resistant mutant)"
FT VARIANT 127
FT /note="F -> Y (in oligomycin-resistant mutant)"
FT VARIANT 136
FT /note="F -> Y (in oligomycin-resistant mutant)"
SQ SEQUENCE 147 AA; 15408 MW; 750957A624F50500 CRC64;
MASTRVLASR LASQMAASAK VARPAVRVAQ VSKRTIQTGS PLQTLKRTQM TSIVNATTRQ
AFQKRAYSSE IAQAMVEVSK NLGMGSAAIG LTGAGIGIGL VFAALLNGVA RNPALRGQLF
SYAILGFAFV EAIGLFDLMV ALMAKFT
