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ATP synthase subunit 9, mitochondrial (Lipid-binding protein)

 ATP9_NEUCR              Reviewed;         147 AA.
P00842; Q7S5B4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
25-APR-2018, entry version 142.
RecName: Full=ATP synthase subunit 9, mitochondrial;
AltName: Full=Lipid-binding protein;
Flags: Precursor;
Name=oli; Synonyms=atp-9, atp9, prl-1; ORFNames=B13D24.340, NCU02250;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6329691;
Viebrock A., Perz A., Sebald W.;
"The imported preprotein of the proteolipid subunit of the
mitochondrial ATP synthase from Neurospora crassa. Molecular cloning
and sequencing of the mRNA.";
EMBO J. 1:565-571(1982).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[4]
PROTEIN SEQUENCE OF 67-147.
Sebald W., Hoppe J., Wachter E.;
"Amino acid sequence of the ATPase proteolipid from mitochondria,
chloroplasts and bacteria (wild type and mutants).";
(In) Quagliariello E., Palmieri F., Papa S., Klingenberg M. (eds.);
Function and molecular aspects of biomembrane transport, pp.63-74,
Elsevier, Amsterdam (1979).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
synthase or Complex V) produces ATP from ADP in the presence of a
proton gradient across the membrane which is generated by electron
transport complexes of the respiratory chain. F-type ATPases
consist of two structural domains, F(1) - containing the
extramembraneous catalytic core and F(0) - containing the membrane
proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Part of the complex F(0)
domain. A homomeric c-ring of probably 10 subunits is part of the
complex rotary element.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has three main subunits: a, b and c.
-!- INTERACTION:
Q02776:TIM50 (xeno); NbExp=5; IntAct=EBI-9084292, EBI-30302;
-!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Multi-
pass membrane protein {ECO:0000305}.
-!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; V00864; CAA24230.1; -; mRNA.
EMBL; BX908789; CAF05899.1; -; Genomic_DNA.
EMBL; CM002242; EAA30658.1; -; Genomic_DNA.
PIR; S07173; LWNCA.
RefSeq; XP_959894.1; XM_954801.3.
ProteinModelPortal; P00842; -.
SMR; P00842; -.
BioGrid; 1977663; 7.
IntAct; P00842; 2.
MINT; P00842; -.
PRIDE; P00842; -.
EnsemblFungi; EAA30658; EAA30658; NCU02250.
GeneID; 3876057; -.
KEGG; ncr:NCU02250; -.
EuPathDB; FungiDB:NCU02250; -.
HOGENOM; HOG000235246; -.
InParanoid; P00842; -.
KO; K02128; -.
OMA; QVFANVQ; -.
OrthoDB; EOG092C5ZJA; -.
Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IBA:GO_Central.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
Gene3D; 1.20.20.10; -; 1.
HAMAP; MF_01396; ATP_synth_c_bact; 1.
InterPro; IPR000454; ATP_synth_F0_csu.
InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
InterPro; IPR038662; ATP_synth_F0_csu_sf.
InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
InterPro; IPR035921; F/V-ATP_Csub_sf.
PANTHER; PTHR10031; PTHR10031; 1.
Pfam; PF00137; ATP-synt_C; 1.
PRINTS; PR00124; ATPASEC.
SUPFAM; SSF81333; SSF81333; 1.
PROSITE; PS00605; ATPASE_C; 1.
1: Evidence at protein level;
CF(0); Complete proteome; Direct protein sequencing;
Hydrogen ion transport; Ion transport; Lipid-binding; Membrane;
Mitochondrion; Reference proteome; Transit peptide; Transmembrane;
Transmembrane helix; Transport.
TRANSIT 1 66 Mitochondrion.
{ECO:0000269|PubMed:6329691,
ECO:0000269|Ref.4}.
CHAIN 67 147 ATP synthase subunit 9, mitochondrial.
/FTId=PRO_0000002573.
TRANSMEM 86 106 Helical. {ECO:0000255}.
TRANSMEM 123 143 Helical. {ECO:0000255}.
SITE 131 131 Reversibly protonated during proton
transport. {ECO:0000250}.
VARIANT 127 127 F -> S (in oligomycin-resistant mutant).
VARIANT 127 127 F -> Y (in oligomycin-resistant mutant).
VARIANT 136 136 F -> Y (in oligomycin-resistant mutant).
SEQUENCE 147 AA; 15408 MW; 750957A624F50500 CRC64;
MASTRVLASR LASQMAASAK VARPAVRVAQ VSKRTIQTGS PLQTLKRTQM TSIVNATTRQ
AFQKRAYSSE IAQAMVEVSK NLGMGSAAIG LTGAGIGIGL VFAALLNGVA RNPALRGQLF
SYAILGFAFV EAIGLFDLMV ALMAKFT


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