ID   ATP6_COTJA              Reviewed;         227 AA.
AC   P50681; Q8SEW9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=11736810; DOI=10.1046/j.1365-2052.2001.00795.x;
RA   Nishibori M., Hayashi T., Tsudzuki M., Yamamoto Y., Yasue H.;
RT   "Complete sequence of the Japanese quail (Coturnix japonica) mitochondrial
RT   genome and its genetic relationship with related species.";
RL   Anim. Genet. 32:380-385(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC   TISSUE=Liver;
RA   Ramirez V., Morais R.;
RT   "Nucleotide sequence of mitochondrial genes for COI, tRNAs Lys, Asp, Ser
RT   (UCN), COII and ATPases 8 and 6 of the quail Coturnix japonica.";
RL   Submitted (SEP-1995) 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. Key component of the
CC       proton channel; it may play a direct role in the translocation of
CC       protons across the membrane.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase A 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; AP003195; BAB62920.1; -; Genomic_DNA.
DR   EMBL; U36794; AAA76732.1; -; Genomic_DNA.
DR   RefSeq; NP_572019.1; NC_003408.1.
DR   AlphaFoldDB; P50681; -.
DR   SMR; P50681; -.
DR   Ensembl; ENSCJPT00005000023; ENSCJPP00005000007; ENSCJPG00005000023.
DR   GeneID; 804661; -.
DR   KEGG; cjo:804661; -.
DR   CTD; 4508; -.
DR   GeneTree; ENSGT00390000005568; -.
DR   OrthoDB; 1095315at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:Ensembl.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
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; 1.20.120.220; -; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..227
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082109"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   227 AA;  25026 MW;  66C9256FC8132F93 CRC64;
     MNLSFFDQFS SPYLMGMPLI LPSLLLPTLL FPTPGRRWIS NRLSTLQLWV INLITKQLMT
     PLNKTGHKWA LLLTSLILLL LSINLMGLLP YTFTPTTQLS MNMALAFPLW LATLLIGLRN
     QPSASLAHLL PEGTPTPLIP ILIMIETTSL LIRPLALGVR LTANLTAGHL LIQLISTATI
     ALLPTMPSIS TLTALILLLL TILEVAVAMI QAYVFVLLLS LYLQENI