ID   ATP8_GORGO              Reviewed;          68 AA.
AC   Q34571;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 103.
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   Gorilla gorilla gorilla (Western lowland gorilla).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA   Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT   "Recent African origin of modern humans revealed by complete sequences of
RT   hominoid mitochondrial DNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:532-536(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. Component of an ATP synthase
CC       complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF,
CC       ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO,
CC       ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By
CC       similarity). {ECO:0000250|UniProtKB:P03928}.
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; D38114; BAA07304.1; -; Genomic_DNA.
DR   PIR; E59153; E59153.
DR   PIR; T14024; T14024.
DR   RefSeq; NP_008216.1; NC_001645.1.
DR   AlphaFoldDB; Q34571; -.
DR   SMR; Q34571; -.
DR   STRING; 9593.ENSGGOP00000027294; -.
DR   GeneID; 807890; -.
DR   CTD; 4509; -.
DR   eggNOG; ENOG502T21P; Eukaryota.
DR   InParanoid; Q34571; -.
DR   Proteomes; UP000001519; Mitochondrion.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
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; IPR039017; ATP8_mammal.
DR   InterPro; IPR001421; ATP8_metazoa.
DR   PANTHER; PTHR13722; PTHR13722; 1.
DR   Pfam; PF00895; ATP-synt_8; 1.
PE   3: Inferred from homology;
KW   Acetylation; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..68
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195531"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         54
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P03930"
FT   MOD_RES         54
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P03930"
FT   MOD_RES         57
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P03930"
SQ   SEQUENCE   68 AA;  7993 MW;  EAC42F9272E831A7 CRC64;
     MPQLNTTVWP TMIAPMLLTL FLITQLKVLN TNYHLPPLPK TMKMKNFCKP WEPKWTKIYS
     LHSLPPQS