ID   ATP6_ONCMY              Reviewed;         223 AA.
AC   P48178;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=mt-atp6; Synonyms=atp6, atpase6, mtatp6;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=8587139; DOI=10.1007/bf00173174;
RA   Zardoya R., Garrido-Pertierra A., Bautista J.M.;
RT   "The complete nucleotide sequence of the mitochondrial DNA genome of the
RT   rainbow trout, Oncorhynchus mykiss.";
RL   J. Mol. Evol. 41:942-951(1995).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE.
RX   PubMed=2550657; DOI=10.1007/bf02100207;
RA   Thomas W.K., Beckenbach A.T.;
RT   "Variation in salmonid mitochondrial DNA: evolutionary constraints and
RT   mechanisms of substitution.";
RL   J. Mol. Evol. 29:233-245(1989).
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}.
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DR   EMBL; L29771; AAB03352.1; -; Genomic_DNA.
DR   PIR; T09862; T09862.
DR   RefSeq; NP_008295.1; NC_001717.1.
DR   AlphaFoldDB; P48178; -.
DR   SMR; P48178; -.
DR   GeneID; 807976; -.
DR   KEGG; omy:807976; -.
DR   CTD; 4508; -.
DR   OrthoDB; 1095315at2759; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
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..223
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082145"
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        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   223 AA;  24597 MW;  7E63CE56B4EEE6D9 CRC64;
     MTLSFFDQFM SPTYLGIPLI AVALTLPWIL FPTPSARWLN NRLITLQGWF INRFTQQLLL
     PLNLGGHKWA ALLTSLMLFL ITLNMLGLLP YTFTPTTQLS LNMGLAVPLW LATVIIGMRN
     QPTAALGHLL PEGTPVPLIP VLIIIETISL FIRPALGVRL TANLTAGHQL IATAAFVLLP
     MMPTVAILTS IVLFLLTLLE IAVAMIQAYV FVLLLSLYLQ ENV