ID   ATP8_OPIHO              Reviewed;          55 AA.
AC   Q9TBI5; Q7J3X4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 73.
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   Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC   Opisthocomus.
OX   NCBI_TaxID=30419;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12572620; DOI=10.1093/oxfordjournals.molbev.a025884;
RA   Mindell D.P., Sorenson M.D., Dimcheff D.E.;
RT   "An extra nucleotide is not translated in mitochondrial ND3 of some birds
RT   and turtles.";
RL   Mol. Biol. Evol. 15:1568-1571(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10486983; DOI=10.1093/oxfordjournals.molbev.a026220;
RA   Hughes J.M., Baker A.J.;
RT   "Phylogenetic relationships of the enigmatic hoatzin (Opisthocomus hoazin)
RT   resolved using mitochondrial and nuclear gene sequences.";
RL   Mol. Biol. Evol. 16:1300-1307(1999).
RN   [3]
RP   SEQUENCE REVISION TO 7 AND 14-15.
RA   Hughes J.M., Baker A.J.;
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12777516; DOI=10.1093/molbev/msg157;
RA   Sorenson M.D., Oneal E., Garcia-Moreno J., Mindell D.P.;
RT   "More taxa, more characters: the hoatzin problem is still unresolved.";
RL   Mol. Biol. Evol. 20:1484-1498(2003).
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}.
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; AF076363; AAQ92325.1; -; Genomic_DNA.
DR   EMBL; AF168040; AAD56468.2; -; Genomic_DNA.
DR   EMBL; AY274300; AAP33117.1; -; Genomic_DNA.
DR   EMBL; AY274301; AAP33125.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9TBI5; -.
DR   SMR; Q9TBI5; -.
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_0000195557"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          35..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        20
FT                   /note="F -> L (in Ref. 1; AAQ92325 and 4; AAP33117/
FT                   AAP33125)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        43..44
FT                   /note="TT -> ATN (in Ref. 1; AAQ92325 and 4; AAP33117/
FT                   AAP33125)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   55 AA;  6485 MW;  18766C186EC1A33E CRC64;
     MPQLNPTPWF PIMMLSWLIF SLIIQPKLLL FTPTNPPSNK TTTTTRSNPW TWPWT