ID T1DPR0_ANOAQ Unreviewed; 213 AA.
AC T1DPR0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000256|ARBA:ARBA00021447};
DE AltName: Full=Oligomycin sensitivity conferral protein {ECO:0000256|ARBA:ARBA00033369};
OS Anopheles aquasalis (Malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=42839 {ECO:0000313|EMBL:JAA98466.1};
RN [1] {ECO:0000313|EMBL:JAA98466.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Whole body {ECO:0000313|EMBL:JAA98466.1};
RG Brazilian Malaria Network (MCT/CNPq/MS/SCTIE/DECIT/PRONEX 555648/2009-5) and Research Network on Bioactive Molecules from Arthropod Vectors (NAP-MOBIARVE;
RG University of Sao Paulo);
RA Marinotti O., Ribeiro J.M.C., Costa-da-Silva A.L., Silva M.C.P.,
RA Lopes A.R., Barros M.S., Sa-Nunes A., Konjin B.B., Carvalho E., Suesdek L.,
RA Silva-Neto M.A.C., Capurro M.L.;
RT "Transcriptome sequencing and developmental regulation of gene expression
RT in Anopheles aquasalis.";
RL Submitted (JUL-2013) 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. {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; GAMD01003124; JAA98466.1; -; mRNA.
DR AlphaFoldDB; T1DPR0; -.
DR VEuPathDB; VectorBase:AAQUA_012453; -.
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 2: Evidence at transcript level;
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 Transport {ECO:0000256|ARBA:ARBA00022448}.
SQ SEQUENCE 213 AA; 22902 MW; 30EB6B10E4D4ED7F CRC64;
MAASGKLTVF ARQLSTSSAA AQLVKPPVQV FGLEGRYACA LYSAASKTKA LDAVEKDLKG
LQNQMRTDPK VRDLLRDPTT KRNVKAAALK DVAAKVKFNA ATGNLLTVLA ENGRLSRLDG
IINAFSLIMA AERGEVVCEV KTAKPLDDGQ RKQLENALKA FLKPNQTIQL TAKVDPALIG
GMVVSIGDKY VDMSVASKIK KYTDIIRIPP SEC
//
