ID   ATP8_ALLMI              Reviewed;          53 AA.
AC   O47871;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Alligator mississippiensis (American alligator).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC   Alligator.
OX   NCBI_TaxID=8496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   PubMed=9402737; DOI=10.1093/oxfordjournals.molbev.a025736;
RA   Janke A., Arnason U.;
RT   "The complete mitochondrial genome of Alligator mississippiensis and the
RT   separation between recent archosauria (birds and crocodiles).";
RL   Mol. Biol. Evol. 14:1266-1272(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12078637; DOI=10.1080/106351599260490;
RA   Mindell D.P., Sorenson M.D., Dimcheff D.E., Hasegawa M., Ast J.C., Yuri T.;
RT   "Interordinal relationships of birds and other reptiles based on whole
RT   mitochondrial genomes.";
RL   Syst. Biol. 48:138-152(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; Y13113; CAA73565.1; -; Genomic_DNA.
DR   EMBL; AF069428; AAD09984.1; -; Genomic_DNA.
DR   PIR; T11278; T11278.
DR   RefSeq; NP_007566.1; NC_001922.1.
DR   AlphaFoldDB; O47871; -.
DR   SMR; O47871; -.
DR   GeneID; 808243; -.
DR   KEGG; amj:808243; -.
DR   CTD; 4509; -.
DR   OrthoDB; 1621322at2759; -.
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..53
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195480"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   53 AA;  6181 MW;  75AE3E79B7EBFD5E CRC64;
     MPQLNPEPWL TTFLIVWISL IVILQPKIAS LMLTSSPTPY KAMTIKTWPW PWT