ID   ATP8_LOXNO              Reviewed;          55 AA.
AC   Q9MDJ1;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=ATP synthase protein 8;
DE   AltName: Full=A6L;
DE   AltName: Full=F-ATPase subunit 8;
GN   Name=MT-ATP8; Synonyms=ATP8, ATPASE8, MTATP8;
OS   Loxigilla noctis (Lesser Antillean bullfinch) (Fringilla noctis).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Thraupidae; Loxigilla.
OX   NCBI_TaxID=111865;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Various strains;
RX   AGRICOLA=IND23252729; DOI=10.1023/A:1010090414598;
RA   Lovette I.J., Seutin G., Ricklefs R.E., Bermingham E.;
RT   "The assembly of an island fauna by natural invasion: sources and temporal
RT   patterns in the avian colonization of Barbados.";
RL   Biol. Invasions 1:33-41(1999).
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. Minor subunit located with subunit a in the membrane (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR   EMBL; AF132376; AAF37028.1; -; Genomic_DNA.
DR   EMBL; AF132365; AAF37006.1; -; Genomic_DNA.
DR   EMBL; AF132367; AAF37010.1; -; Genomic_DNA.
DR   EMBL; AF132368; AAF37012.1; -; Genomic_DNA.
DR   EMBL; AF132369; AAF37014.1; -; Genomic_DNA.
DR   EMBL; AF132370; AAF37016.1; -; Genomic_DNA.
DR   EMBL; AF132371; AAF37018.1; -; Genomic_DNA.
DR   EMBL; AF132375; AAF37026.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9MDJ1; -.
DR   SMR; Q9MDJ1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
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   InterPro; IPR001421; ATP8_metazoa.
DR   Pfam; PF00895; ATP-synt_8; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..55
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195546"
FT   TRANSMEM        10..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   55 AA;  6421 MW;  C348853D22E2C37F CRC64;
     MPQLNPHPWF FIMLASWLTF SLIIQPKLLT FVTMNPPSNK PPIAPSTTPW TWPWT