ATPO_SORAR
ID ATPO_SORAR Reviewed; 213 AA.
AC B3EX21;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000305};
DE AltName: Full=ATP synthase peripheral stalk subunit OSCP {ECO:0000305};
DE AltName: Full=Oligomycin sensitivity conferral protein;
DE Short=OSCP;
DE Flags: Precursor;
GN Name=ATP5PO {ECO:0000250|UniProtKB:P48047}; Synonyms=ATP5O;
OS Sorex araneus (Eurasian common shrew) (European shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Soricidae; Soricinae; Sorex.
OX NCBI_TaxID=42254;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (JUN-2008) 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 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 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. 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. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR EMBL; DP000755; ACE60217.1; -; Genomic_DNA.
DR RefSeq; XP_004620391.1; XM_004620334.1.
DR AlphaFoldDB; B3EX21; -.
DR SMR; B3EX21; -.
DR GeneID; 101557303; -.
DR KEGG; sara:101557303; -.
DR CTD; 539; -.
DR OrthoDB; 1178688at2759; -.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR Gene3D; 1.10.520.20; -; 1.
DR HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR InterPro; IPR020781; ATPase_OSCP/d_CS.
DR InterPro; IPR000711; ATPase_OSCP/dsu.
DR PANTHER; PTHR11910; PTHR11910; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; SSF47928; 1.
DR TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP synthesis; Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Transit peptide;
KW Transport.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 24..213
FT /note="ATP synthase subunit O, mitochondrial"
FT /id="PRO_0000350578"
FT MOD_RES 54
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 73
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 90
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 100
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 100
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 158
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 158
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 172
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48047"
FT MOD_RES 176
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT MOD_RES 192
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48047"
SQ SEQUENCE 213 AA; 23231 MW; E95282C67DE94B37 CRC64;
MAAPVVSGLS RQVRSFSTSV ARPFAKLVRP PIQIYGVEGR YATALYSAAS KQNKLDQVEK
ELLRVAQLLK EPKLAASILN PHVKRAIKVK SIGDLTAREK LSPITTNLIN LLAENGRLNN
TPGIISAFST MMSVHRGEVP CTVTTASALP EATLSELKTV LQSFLSKNQV LKLEVKTDPS
IMGGMIVRIG EKYVDMSART KIQKLSKAMR EAM
