ATPO_BOVIN
ID ATPO_BOVIN Reviewed; 213 AA.
AC P13621; Q3T0Y7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 168.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2894843; DOI=10.1021/bi00400a018;
RA Walker J.E., Gay N.J., Powell S.J., Kostina M., Dyer M.R.;
RT "ATP synthase from bovine mitochondria: sequences of imported precursors of
RT oligomycin sensitivity conferral protein, factor 6, and
RT adenosinetriphosphatase inhibitor protein.";
RL Biochemistry 26:8613-8619(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-28.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [4]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
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.
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. {ECO:0000269|PubMed:17570365, ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- PTM: Acetylation at Lys-162 decreases ATP production. Deacetylated by
CC SIRT3 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family. {ECO:0000305}.
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DR EMBL; M18753; AAA30676.1; -; mRNA.
DR EMBL; BC102204; AAI02205.1; -; mRNA.
DR PIR; A27382; A27382.
DR RefSeq; NP_776669.1; NM_174244.1.
DR PDB; 2BO5; NMR; -; A=24-143.
DR PDB; 2JMX; NMR; -; A=24-143.
DR PDB; 2WSS; X-ray; 3.20 A; S/W=24-213.
DR PDB; 4B2Q; EM; 37.00 A; W/w=24-143.
DR PDB; 5ARA; EM; 6.70 A; S=24-213.
DR PDB; 5ARE; EM; 7.40 A; S=24-213.
DR PDB; 5ARH; EM; 7.20 A; S=24-213.
DR PDB; 5ARI; EM; 7.40 A; S=24-213.
DR PDB; 5FIJ; EM; 7.40 A; S=24-213.
DR PDB; 5FIK; EM; 6.40 A; S=24-213.
DR PDB; 5FIL; EM; 7.10 A; S=24-213.
DR PDB; 6YY0; EM; 3.23 A; S=24-213.
DR PDB; 6Z1R; EM; 3.29 A; S=24-213.
DR PDB; 6Z1U; EM; 3.47 A; S=24-213.
DR PDB; 6ZIQ; EM; 4.33 A; S=24-213.
DR PDB; 6ZIT; EM; 3.49 A; S=24-213.
DR PDB; 6ZIU; EM; 6.02 A; S=24-213.
DR PDB; 6ZPO; EM; 4.00 A; S=24-213.
DR PDB; 6ZQM; EM; 3.29 A; S=24-213.
DR PDB; 6ZQN; EM; 4.00 A; S=24-213.
DR PDB; 7AJB; EM; 9.20 A; AS/S=24-213.
DR PDB; 7AJC; EM; 11.90 A; AS/S=24-213.
DR PDB; 7AJD; EM; 9.00 A; AS/S=24-213.
DR PDB; 7AJE; EM; 9.40 A; AS/S=24-213.
DR PDB; 7AJF; EM; 8.45 A; AS/S=24-213.
DR PDB; 7AJG; EM; 10.70 A; AS/S=24-213.
DR PDB; 7AJH; EM; 9.70 A; AS/S=24-213.
DR PDB; 7AJI; EM; 11.40 A; AS/S=24-213.
DR PDB; 7AJJ; EM; 13.10 A; AS/S=24-213.
DR PDBsum; 2BO5; -.
DR PDBsum; 2JMX; -.
DR PDBsum; 2WSS; -.
DR PDBsum; 4B2Q; -.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6YY0; -.
DR PDBsum; 6Z1R; -.
DR PDBsum; 6Z1U; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P13621; -.
DR BMRB; P13621; -.
DR SMR; P13621; -.
DR CORUM; P13621; -.
DR DIP; DIP-39019N; -.
DR IntAct; P13621; 2.
DR MINT; P13621; -.
DR STRING; 9913.ENSBTAP00000024326; -.
DR Allergome; 1548; Bos d OSCP.
DR PaxDb; P13621; -.
DR PeptideAtlas; P13621; -.
DR PRIDE; P13621; -.
DR Ensembl; ENSBTAT00000024326; ENSBTAP00000024326; ENSBTAG00000018278.
DR GeneID; 281640; -.
DR KEGG; bta:281640; -.
DR CTD; 539; -.
DR VEuPathDB; HostDB:ENSBTAG00000018278; -.
DR VGNC; VGNC:103017; ATP5PO.
DR eggNOG; KOG1662; Eukaryota.
DR GeneTree; ENSGT00390000015060; -.
DR HOGENOM; CLU_085114_0_0_1; -.
DR InParanoid; P13621; -.
DR OMA; MVDNIQD; -.
DR OrthoDB; 1178688at2759; -.
DR TreeFam; TF106241; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR EvolutionaryTrace; P13621; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000018278; Expressed in cardiac ventricle and 105 other tissues.
DR ExpressionAtlas; P13621; baseline and differential.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transport.
FT TRANSIT 1..23
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:1827992"
FT CHAIN 24..213
FT /note="ATP synthase subunit O, mitochondrial"
FT /id="PRO_0000002645"
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 162
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P48047"
FT MOD_RES 162
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"
FT MOD_RES 199
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB20"
FT CONFLICT 152
FT /note="A -> T (in Ref. 1; AAA30676)"
FT /evidence="ECO:0000305"
FT HELIX 37..50
FT /evidence="ECO:0007829|PDB:6YY0"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2JMX"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 121..135
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 183..189
FT /evidence="ECO:0007829|PDB:6YY0"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:6YY0"
FT HELIX 198..210
FT /evidence="ECO:0007829|PDB:6YY0"
SQ SEQUENCE 213 AA; 23320 MW; C769EC7B778069DA CRC64;
MAALAVSGLS QQVRCFSTSV VRPFAKLVRP PVQIYGIEGR YATALYSAAS KQNKLEQVEK
ELLRVGQILK EPKMAASLLN PYVKRSVKVK SLSDMTAKEK FSPLTSNLIN LLAENGRLTN
TPAVISAFST MMSVHRGEVP CTVTTASALD EATLTELKTV LKSFLSKGQV LKLEVKIDPS
IMGGMIVRIG EKYVDMSAKT KIQKLSRAMR EIL
