ID   ATP6_DIDVI              Reviewed;         226 AA.
AC   P41313;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS   Didelphis virginiana (North American opossum) (Didelphis marsupialis
OS   virginiana).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Didelphimorphia; Didelphidae; Didelphis.
OX   NCBI_TaxID=9267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=8056314; DOI=10.1093/genetics/137.1.243;
RA   Janke A., Feldmaier-Fuchs G., Thomas K., von Haeseler A., Paabo S.;
RT   "The marsupial mitochondrial genome and the evolution of placental
RT   mammals.";
RL   Genetics 137:243-256(1994).
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. Component of an ATP synthase complex composed of
CC       ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC       ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC       ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct
CC       (By similarity). {ECO:0000250|UniProtKB:P00846,
CC       ECO:0000250|UniProtKB:P00847}.
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; Z29573; CAA82682.1; -; Genomic_DNA.
DR   PIR; S47875; S47875.
DR   RefSeq; NP_007100.1; NC_001610.1.
DR   AlphaFoldDB; P41313; -.
DR   SMR; P41313; -.
DR   GeneID; 807785; -.
DR   CTD; 4508; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
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..226
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082114"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  25145 MW;  46D86EC1E2C6CEE4 CRC64;
     MNENLFAPFI TPTILGITTL PIIITFPCLI LSSPKRWLPN RIQILQMWLI RLITKQMMTM
     HNKQGRTWTL MLMSLILFIA STNLLGLLPY SFTPTTQLSM NIGMAIPLWA GTVIMGFRNK
     PKMSLAHFLP QGTPTPLIPM LIIIETISLF IQPLALAVRL TANITAGHLL IHLIGSATLA
     LSSISMTVST ITFSILFLLT LLEIAVAMIQ AYVFTLLVSL YLHDNS