ID   ATP8_CHICK              Reviewed;          54 AA.
AC   P14093;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 134.
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   Gallus gallus (Chicken).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2474659; DOI=10.1016/0022-2836(89)90471-3;
RA   Desjardins P., L'Abbe D., Lang B.F., Morais R.;
RT   "Putative chicken 'muscle-specific 7 S RNA' is related to the mitochondrial
RT   ATPase 6 gene.";
RL   J. Mol. Biol. 207:625-629(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Red jungle fowl {ECO:0000312|Proteomes:UP000000539};
RX   PubMed=2329578; DOI=10.1016/0022-2836(90)90225-b;
RA   Desjardins P., Morais R.;
RT   "Sequence and gene organization of the chicken mitochondrial genome. A
RT   novel gene order in higher vertebrates.";
RL   J. Mol. Biol. 212:599-634(1990).
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; X15841; CAA33841.1; -; Genomic_DNA.
DR   EMBL; X52392; CAA36629.1; -; Genomic_DNA.
DR   PIR; S04619; S04619.
DR   RefSeq; NP_006919.1; NC_001323.1.
DR   AlphaFoldDB; P14093; -.
DR   SMR; P14093; -.
DR   STRING; 9031.ENSGALP00000034616; -.
DR   PaxDb; P14093; -.
DR   Ensembl; ENSGALT00000054361; ENSGALP00000055032; ENSGALG00000032465.
DR   VEuPathDB; HostDB:geneid_63549490; -.
DR   eggNOG; ENOG502TDJG; Eukaryota.
DR   GeneTree; ENSGT00730000112785; -.
DR   HOGENOM; CLU_212888_0_0_1; -.
DR   InParanoid; P14093; -.
DR   OMA; MPQLNPN; -.
DR   OrthoDB; 1621322at2759; -.
DR   PhylomeDB; P14093; -.
DR   PRO; PR:P14093; -.
DR   Proteomes; UP000000539; Mitochondrion.
DR   Bgee; ENSGALG00000032465; Expressed in granulocyte and 13 other tissues.
DR   ExpressionAtlas; P14093; baseline and differential.
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..54
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195509"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   54 AA;  6377 MW;  364BFEADA0B63E8B CRC64;
     MPQLNPNPWF SIMLLTWFTF SLLIQPKLLS FTLTNNPANK ITTTKPTPWT WPWT