ID A0A087Y1W3_POEFO Unreviewed; 209 AA.
AC A0A087Y1W3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000256|ARBA:ARBA00021447};
DE AltName: Full=Oligomycin sensitivity conferral protein {ECO:0000256|ARBA:ARBA00033369};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000012016.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000012016.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; AYCK01003032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007548480.1; XM_007548418.2.
DR AlphaFoldDB; A0A087Y1W3; -.
DR STRING; 48698.ENSPFOP00000012016; -.
DR Ensembl; ENSPFOT00000012033.1; ENSPFOP00000012016.2; ENSPFOG00000012009.1.
DR GeneID; 103135604; -.
DR KEGG; pfor:103135604; -.
DR CTD; 539; -.
DR eggNOG; KOG1662; Eukaryota.
DR GeneTree; ENSGT00390000015060; -.
DR OMA; MVDNIQD; -.
DR OrthoDB; 312519at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
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; 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.
PE 3: Inferred from homology;
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:UP000028760};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ SEQUENCE 209 AA; 22675 MW; 16AFEAA1D3DF80FA CRC64;
MAAHMLGQQA RRFSTSVIRP AAKLVKPPIQ VYGVEGRYAT ALFSAASKQN KLDQVEQELG
KVSALIKDPK MSGIIMNPHV KRSIKQKTFH DALAKANVSP ITVNLINVLA DNGRLTLTGD
VISAFEKMMS AHRGEVICSV TTAQPLDKSS LAELKVALNG FLQKGESIKL ETKSDPSILG
GMIVSIGDKY VDMSTKTKVQ KLTQLIRDT
//
