ATPO_PIG
ID ATPO_PIG Reviewed; 213 AA.
AC Q2EN81; A1XQT0; Q9T2U6;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chen C.H., Ding S.T.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Longissimus dorsi muscle;
RA Cai G., Chen Y., Wang C., Li J., Peng G., Zhang H.;
RT "Generation and analysis of cDNA sequences derived from a porcine skeletal
RT muscle library.";
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 24-213.
RC TISSUE=Heart;
RX PubMed=7530007;
RA Grinkevich V.A., Zaitsev V.G., Pavlov P.F., Nazimov I.V., Il'ina E.F.;
RT "Study of the structural organization of OSCP -- subunits of H+-ATPase of
RT porcine heart mitochondria.";
RL Bioorg. Khim. 20:842-856(1994).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ372076; ABD18451.1; -; mRNA.
DR EMBL; DQ629152; ABK55636.1; -; mRNA.
DR RefSeq; NP_001038071.1; NM_001044606.2.
DR PDB; 6J5I; EM; 3.34 A; S=24-210.
DR PDB; 6J5J; EM; 3.45 A; S=24-210.
DR PDB; 6J5K; EM; 6.20 A; AS/BS/CS/S=24-210.
DR PDBsum; 6J5I; -.
DR PDBsum; 6J5J; -.
DR PDBsum; 6J5K; -.
DR AlphaFoldDB; Q2EN81; -.
DR SMR; Q2EN81; -.
DR IntAct; Q2EN81; 1.
DR STRING; 9823.ENSSSCP00000012823; -.
DR iPTMnet; Q2EN81; -.
DR PaxDb; Q2EN81; -.
DR PeptideAtlas; Q2EN81; -.
DR PRIDE; Q2EN81; -.
DR Ensembl; ENSSSCT00015018838; ENSSSCP00015007400; ENSSSCG00015014218.
DR Ensembl; ENSSSCT00045040050; ENSSSCP00045027906; ENSSSCG00045023435.
DR Ensembl; ENSSSCT00050025904; ENSSSCP00050010735; ENSSSCG00050019184.
DR Ensembl; ENSSSCT00055047322; ENSSSCP00055037761; ENSSSCG00055024030.
DR Ensembl; ENSSSCT00060103661; ENSSSCP00060045329; ENSSSCG00060075675.
DR Ensembl; ENSSSCT00065042587; ENSSSCP00065018055; ENSSSCG00065031487.
DR GeneID; 733678; -.
DR KEGG; ssc:733678; -.
DR CTD; 539; -.
DR eggNOG; KOG1662; Eukaryota.
DR HOGENOM; CLU_085114_0_0_1; -.
DR InParanoid; Q2EN81; -.
DR OrthoDB; 1178688at2759; -.
DR TreeFam; TF106241; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; Q2EN81; SS.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
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:InterPro.
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:7530007"
FT CHAIN 24..213
FT /note="ATP synthase subunit O, mitochondrial"
FT /id="PRO_0000350579"
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 110
FT /note="N -> S (in Ref. 2; ABK55636)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="P -> A (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="Q -> E (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="R -> Q (in Ref. 2; ABK55636)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="F -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 87..98
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:6J5J"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:6J5I"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:6J5I"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:6J5I"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:6J5I"
SQ SEQUENCE 213 AA; 23370 MW; F55A40E8850431EF CRC64;
MASQAVSGLS RQVRCFSTSV VRPFAKLVRP PVQIYGIEGR YATALYSAAS KQNKLEQVEK
ELLRVAQILK EPKVAASIMN PYVKRSVKVK SLSDMTAKEK FSPLTSNLIN LLAENGRLSS
TPGVISAFST MMSVHRGEVP CSVTTASPLD EATLTELKTV LKSFLSKGQI LKLEVKVDPS
IMGGMIVRIG EKYVDMSAKT KIQKLSRAMR EIF
