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ATP6_BOSIN
ID   ATP6_BOSIN              Reviewed;         226 AA.
AC   Q8LTZ5;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS   Bos indicus (Zebu).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Isolate E1, Isolate E4, and Isolate Elisabeth;
RX   PubMed=12399392; DOI=10.1093/genetics/162.2.823;
RA   Steinborn R., Schinogl P., Wells D.N., Bergthaler A., Mueller M., Brem G.;
RT   "Coexistence of Bos taurus and B. indicus mitochondrial DNAs in nuclear
RT   transfer-derived somatic cattle clones.";
RL   Genetics 162:823-829(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Hiendleder S., Lewalski H., Wolf E.;
RT   "Complete sequence of the Bos indicus mitochondrial genome.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Miretti M.M., Pereira H.A. Jr., Greggio C., Suzuki J. Jr., Ferro J.A.,
RA   Ferro M.I., Meirelles F., Garcia J.M., Smith L.C.;
RT   "The complete mitochondrial genome nucleotide sequence of Bos indicus.";
RL   Submitted (JUN-2002) 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. Key component of the
CC       proton channel; it may play a direct role in the translocation of
CC       protons across the membrane.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c. Component of an ATP synthase complex composed of
CC       ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC       ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC       ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct
CC       (By similarity). {ECO:0000250|UniProtKB:P00846,
CC       ECO:0000250|UniProtKB:P00847}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}.
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DR   EMBL; AF384022; AAM49067.1; -; Genomic_DNA.
DR   EMBL; AF384023; AAM49069.1; -; Genomic_DNA.
DR   EMBL; AF384024; AAM49071.1; -; Genomic_DNA.
DR   EMBL; AF492350; AAQ06585.1; -; Genomic_DNA.
DR   EMBL; AY126697; AAM95735.1; -; Genomic_DNA.
DR   RefSeq; YP_052702.1; NC_005971.1.
DR   AlphaFoldDB; Q8LTZ5; -.
DR   SMR; Q8LTZ5; -.
DR   GeneID; 2885970; -.
DR   KEGG; biu:2885970; -.
DR   CTD; 4508; -.
DR   OrthoDB; 1095315at2759; -.
DR   Proteomes; UP000515132; Mitochondrion MT.
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:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro.
DR   Gene3D; 1.20.120.220; -; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   PANTHER; PTHR11410; PTHR11410; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; SSF81336; 1.
DR   TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..226
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000253507"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   226 AA;  24696 MW;  FBA0E9E38680A98D CRC64;
     MNENLFASFI TPVILGLPLV TLIVLFPSLL FPTSNRLVSN RFVTLQQWML QLVSKQMMSI
     HNSKGQTWAL MLMSLILFIG STNLLGLLPH SFTPTTQLSM NLGMAIPLWA GAVITGFRNK
     TKASLAHFLP QGTPTPLIPM LVIIETISLF IQPVALAVRL TANITAGHLL IHLIGGATLA
     LMSISTTTAL ITFTILILLT ILEFAVAMIQ AYVFTLLVSL YLHDNT
 
 
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