ID   ATP8_LATCH              Reviewed;          55 AA.
AC   O03168;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 104.
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   Latimeria chalumnae (Coelacanth).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Coelacanthiformes; Coelacanthidae; Latimeria.
OX   NCBI_TaxID=7897;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9215903; DOI=10.1093/genetics/146.3.995;
RA   Zardoya R., Meyer A.;
RT   "The complete DNA sequence of the mitochondrial genome of a 'living
RT   fossil,' the coelacanth (Latimeria chalumnae).";
RL   Genetics 146:995-1010(1997).
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; U82228; AAC60322.1; -; Genomic_DNA.
DR   PIR; E58892; E58892.
DR   RefSeq; NP_008333.1; NC_001804.1.
DR   AlphaFoldDB; O03168; -.
DR   SMR; O03168; -.
DR   STRING; 7897.ENSLACP00000023658; -.
DR   Ensembl; ENSLACT00000026718; ENSLACP00000023658; ENSLACG00000022688.
DR   GeneID; 808087; -.
DR   KEGG; lcm:808087; -.
DR   CTD; 4509; -.
DR   eggNOG; ENOG502SGKX; Eukaryota.
DR   GeneTree; ENSGT00400000025179; -.
DR   HOGENOM; CLU_212888_0_0_1; -.
DR   InParanoid; O03168; -.
DR   OMA; MPQLNPN; -.
DR   OrthoDB; 1621322at2759; -.
DR   Proteomes; UP000008672; Mitochondrion.
DR   Bgee; ENSLACG00000022688; Expressed in pelvic fin and 6 other tissues.
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..55
FT                   /note="ATP synthase protein 8"
FT                   /id="PRO_0000195541"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          36..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   55 AA;  6569 MW;  7FE36319E8AF825B CRC64;
     MPQLNPSPWL LILLFSWLIF LTMLPSKTQL HTFPNMPSTQ NMCKQEPEPW TWPWA