ID   ATP8_BOSMU              Reviewed;          66 AA.
AC   Q5Y4Q6; Q6VUQ7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
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   Bos mutus grunniens (Wild yak) (Bos grunniens).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=30521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Zhao X., Li Q., Li N.;
RT   "Cloning of Yak mtDNA ATPase 8 and ATPase 6.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gu Z., Zhao X., Li N., Wu C.;
RT   "Complete sequence of the Yak (Bos grunniens.) mitochondrial genome and its
RT   genetic relationship with related species.";
RL   Submitted (OCT-2004) 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. 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; AY325805; AAP87309.2; -; Genomic_DNA.
DR   EMBL; AY684273; AAU89110.1; -; Genomic_DNA.
DR   RefSeq; YP_001218795.1; NC_006380.3.
DR   AlphaFoldDB; Q5Y4Q6; -.
DR   SMR; Q5Y4Q6; -.
DR   GeneID; 3119744; -.
DR   CTD; 4509; -.
DR   OrthoDB; 1621322at2759; -.
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; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..66
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000253506"
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"
FT   CONFLICT        38
FT                   /note="E -> K (in Ref. 1; AAP87309)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        52
FT                   /note="E -> K (in Ref. 1; AAP87309)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   66 AA;  7967 MW;  35CCC69EEF5D9876 CRC64;
     MPQLDTSTWL TMILSMFLTL FIIFQLKISK HNFYYNPELT STKMLKQNTP WETKWTKIYL
     PLLLPL