ID   ATP8_LOCMI              Reviewed;          52 AA.
AC   P14570;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   03-AUG-2022, entry version 90.
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   Locusta migratoria (Migratory locust).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Orthoptera; Caelifera; Acrididea; Acridomorpha;
OC   Acridoidea; Acrididae; Oedipodinae; Locusta.
OX   NCBI_TaxID=7004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2852067; DOI=10.1007/bf00521271;
RA   Haucke H.R., Gellissen G.;
RT   "Different mitochondrial gene orders among insects: exchanged tRNA gene
RT   positions in the COII/COIII region between an orthopteran and a dipteran
RT   species.";
RL   Curr. Genet. 14:471-476(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8587138; DOI=10.1007/bf00173173;
RA   Flook P.K., Rowell C.H.F., Gellissen G.;
RT   "The sequence, organization, and evolution of the Locusta migratoria
RT   mitochondrial genome.";
RL   J. Mol. Evol. 41:928-941(1995).
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAA32154.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X13975; CAA32154.1; ALT_INIT; Genomic_DNA.
DR   EMBL; X80245; CAA56533.1; -; Genomic_DNA.
DR   PIR; T11473; T11473.
DR   RefSeq; NP_007293.1; NC_001712.1.
DR   AlphaFoldDB; P14570; -.
DR   GeneID; 807956; -.
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..52
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195544"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   52 AA;  6466 MW;  5193D3D04EF0FDCD CRC64;
     MPQMSPMMWF SLFIMFSMTM MLFNQLNFFS YKPNKIMSSN NKIKKKNINW MW