ID W5PTA0_SHEEP Unreviewed; 213 AA.
AC W5PTA0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000256|ARBA:ARBA00021447};
DE AltName: Full=ATP synthase peripheral stalk subunit OSCP {ECO:0000256|ARBA:ARBA00032173};
DE AltName: Full=Oligomycin sensitivity conferral protein {ECO:0000256|ARBA:ARBA00033369};
GN Name=ATP5PO {ECO:0000313|Ensembl:ENSOARP00000013681.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000013681.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000013681.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000013681.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0007829|PDB:6TT7}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS).
RX PubMed=32929284; DOI=10.1038/s41594-020-0503-8;
RA Pinke G., Zhou L., Sazanov L.A.;
RT "Cryo-EM structure of the entire mammalian F-type ATP synthase.";
RL Nat. Struct. Mol. Biol. 27:1077-1085(2020).
RN [3] {ECO:0000313|Ensembl:ENSOARP00000013681.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025371}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004273}.
CC -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC {ECO:0000256|ARBA:ARBA00007046}.
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DR EMBL; AMGL01005673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PDB; 6TT7; EM; 3.50 A; J=1-213.
DR AlphaFoldDB; W5PTA0; -.
DR EMDB; EMD-10573; -.
DR SMR; W5PTA0; -.
DR Ensembl; ENSOART00000013886.1; ENSOARP00000013681.1; ENSOARG00000012773.1.
DR HOGENOM; CLU_085114_0_0_1; -.
DR Proteomes; UP000002356; Chromosome 1.
DR Bgee; ENSOARG00000012773; Expressed in heart right ventricle and 54 other cell types or tissues.
DR ExpressionAtlas; W5PTA0; baseline and differential.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:Ensembl.
DR Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 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 NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR Pfam; PF00213; OSCP; 1.
DR PRINTS; PR00125; ATPASEDELTA.
DR SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR PROSITE; PS00389; ATPASE_DELTA; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:6TT7};
KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ SEQUENCE 213 AA; 23404 MW; DE79103FC78FDF95 CRC64;
MAALAVSGLS QQVRCFSTSV VRPFAKLVRP PVQIYGIEGR YATALYSAAS KQNKLEQVEK
ELLRVGQILK EPKMAASLMN PYVKRSVKVK SLNDMTAKEK FSPLTSNLIN LLAENGRLNN
TPAVISAFST MMSVHRGEVP CTVTTASPLD EATLTELKTV LKSFLSKGQV LKLEVKIDPS
IMGGMIVRIG EKYVDMSAKT KIQKLSRAMR EIL
//
