ATP7_ASPTN
ID ATP7_ASPTN Reviewed; 173 AA.
AC P0C2C8; Q0CGW2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=ATP synthase subunit d, mitochondrial;
DE Flags: Precursor;
GN Name=atp7; ORFNames=ATEG_07080.2;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. In yeast, the dimeric form
CC of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta,
CC epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j
CC and k.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU32464.1; Type=Erroneous gene model prediction; Note=The predicted gene ATEG_07080 has been split into 2 genes: ATEG_07080.1 and ATEG_07080.2.; Evidence={ECO:0000305};
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DR EMBL; CH476603; EAU32464.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; P0C2C8; -.
DR SMR; P0C2C8; -.
DR STRING; 341663.P0C2C8; -.
DR PRIDE; P0C2C8; -.
DR EnsemblFungi; EAU32464; EAU32464; ATEG_07080.
DR OrthoDB; 1097026at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
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;
KW Transit peptide; Transport.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 24..173
FT /note="ATP synthase subunit d, mitochondrial"
FT /id="PRO_0000273478"
SQ SEQUENCE 173 AA; 19456 MW; F9E242953FC88CA0 CRC64;
MAARSAALKI DWVKVTSSLG LRGQTAASLQ AFKKRNDDAR RKVQILSEQP QTVDFAHYRQ
ILKNQAVVDE IENQFKNFKP ATYDVSRQLK AIEAFEAQAV QNAEQTKGKV EAELRNLQKT
LENIETARPF DELTVDEVAA AQPEIDEKTA SLVSKGRWMP AGYKERFGDM SVV