ID   ATP8_XENLA              Reviewed;          55 AA.
AC   P03931;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 101.
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   Xenopus laevis (African clawed frog).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=4019494; DOI=10.1016/s0021-9258(17)39303-1;
RA   Roe B.A., Ma D.-P., Wilson R.K., Wong J.F.-H.;
RT   "The complete nucleotide sequence of the Xenopus laevis mitochondrial
RT   genome.";
RL   J. Biol. Chem. 260:9759-9774(1985).
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; M10217; AAA66462.1; -; Genomic_DNA.
DR   PIR; A01065; PWXL8.
DR   RefSeq; NP_008138.1; NC_001573.1.
DR   AlphaFoldDB; P03931; -.
DR   SMR; P03931; -.
DR   BioGRID; 106516; 1.
DR   GeneID; 2642082; -.
DR   KEGG; xla:2642082; -.
DR   CTD; 4509; -.
DR   Xenbase; XB-GENE-6251963; atp8.L.
DR   OrthoDB; 1621322at2759; -.
DR   Proteomes; UP000186698; Mitochondrion MT.
DR   Bgee; 2642082; Expressed in egg cell and 19 other tissues.
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..55
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195594"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          35..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   55 AA;  6531 MW;  8AB4FE1050260994 CRC64;
     MPQLNPGPWF LILIFSWLVL LTFIPPKVLK HKAFNEPTTQ TTEKSKPNPW NWPWT