ID   ATP8_BRALA              Reviewed;          54 AA.
AC   O21003; O79418;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 80.
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   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9332712; DOI=10.1023/a:1021954109452;
RA   Delarbre C., Gachelin G.;
RT   "A unique cDNA coding for subunits 8 and 6 of mitochondrial adenosine
RT   triphosphatase of the lancelet Branchiostoma lanceolatum, an ancestor of
RT   vertebrates.";
RL   Biochem. Genet. 35:181-187(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9628930; DOI=10.1093/nar/26.13.3279;
RA   Spruyt N., Delarbre C., Gachelin G., Laudet V.;
RT   "Complete sequence of the amphioxus (Branchiostoma lanceolatum)
RT   mitochondrial genome: relations to vertebrates.";
RL   Nucleic Acids Res. 26:3279-3285(1998).
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; Y09525; CAA70711.1; -; Genomic_DNA.
DR   EMBL; Y16474; CAA76251.1; -; Genomic_DNA.
DR   PIR; F71390; F71390.
DR   RefSeq; NP_007541.1; NC_001912.1.
DR   AlphaFoldDB; O21003; -.
DR   SMR; O21003; -.
DR   GeneID; 808216; -.
DR   CTD; 4509; -.
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..54
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195497"
FT   TRANSMEM        9..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        11..12
FT                   /note="FL -> LR (in Ref. 1; CAA70711)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   54 AA;  6349 MW;  2B9E1DEECFB50A5B CRC64;
     MPQLNPIPWV FLFFLVWLVL GFLGLQKFTS VVTTTLDDSS EEVEVKSKEY SWPW