ID   ATP8_CARAU              Reviewed;          54 AA.
AC   O78683;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 78.
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   Carassius auratus (Goldfish).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Carassius.
OX   NCBI_TaxID=7957;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AZ3 / Langsdorfi; TISSUE=Oocyte;
RA   Murakami M., Yamashita Y., Fujitani H.;
RT   "The complete sequence of mitochondrial genome from a gynogenetic triploid
RT   'ginbuna' (Carassius auratus langsdorfi).";
RL   Zool. Sci. 15:335-337(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Cuvieri;
RA   Murakami M.;
RT   "Carassius auratus cuvieri mitochondrial DNA, complete sequence.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
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; AB006953; BAA31242.1; -; Genomic_DNA.
DR   EMBL; AB045144; BAB40352.1; -; Genomic_DNA.
DR   RefSeq; NP_008592.1; NC_002079.1.
DR   AlphaFoldDB; O78683; -.
DR   SMR; O78683; -.
DR   Ensembl; ENSCART00000000022; ENSCARP00000000006; ENSCARG00000000022.
DR   GeneID; 808420; -.
DR   CTD; 4509; -.
DR   Proteomes; UP000515129; Mitochondrion MT.
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; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..54
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195502"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          35..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   54 AA;  6284 MW;  261A1D3C5AA7196B CRC64;
     MPQLNPGPWF AILVFSWLVF LTIIPTKILS HISPNEPTPV SAEKHKTESW DWPW