ID   ATP8_LOXAF              Reviewed;          66 AA.
AC   Q9TA25; Q2I3F7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 75.
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   Loxodonta africana (African elephant).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RA   Hauf J., Waddell P.J., Chalwatzis N., Joger U., Zimmermann F.K.;
RT   "The complete mitochondrial genome sequence of the African elephant
RT   (Loxodonta africana), phylogenetic relationships of Proboscidea to other
RT   mammals and D-loop heteroplasmy.";
RL   Zoology 102:184-195(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Blood;
RX   PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA   Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA   Chumakov I., Grigorenko A.P.;
RT   "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT   Mammuthus primigenius.";
RL   PLoS Biol. 4:403-410(2006).
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; AJ224821; CAA12142.1; -; Genomic_DNA.
DR   EMBL; DQ316069; ABC17908.1; -; Genomic_DNA.
DR   PIR; T45554; T45554.
DR   RefSeq; NP_009283.1; NC_000934.1.
DR   AlphaFoldDB; Q9TA25; -.
DR   Ensembl; ENSLAFT00000038055; ENSLAFP00000029495; ENSLAFG00000033289.
DR   GeneID; 808789; -.
DR   KEGG; lav:808789; -.
DR   CTD; 4509; -.
DR   HOGENOM; CLU_2830543_0_0_1; -.
DR   InParanoid; Q9TA25; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
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..66
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195545"
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   66 AA;  7893 MW;  CF057B67F70877F5 CRC64;
     MERMDIIIWL LAVVIVLTTL MIFLHLKTLK IIRLLFPISK ELSKKSCVFP WKKKWTKNYP
     PSSMYP