ID   ATP6_MYXGL              Reviewed;         228 AA.
AC   O63912;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS   Myxine glutinosa (Atlantic hagfish).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata; Myxini;
OC   Myxiniformes; Myxinidae; Myxininae; Myxine.
OX   NCBI_TaxID=7769;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9541532; DOI=10.1007/pl00006317;
RA   Rasmussen A.S., Janke A., Arnason U.;
RT   "The mitochondrial DNA molecule of the hagfish (Myxine glutinosa) and
RT   vertebrate phylogeny.";
RL   J. Mol. Evol. 46:382-388(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11677623; DOI=10.1007/s002390010250;
RA   Delarbre C., Rasmussen A.S., Arnason U., Gachelin G.;
RT   "The complete mitochondrial genome of the hagfish Myxine glutinosa: unique
RT   features of the control region.";
RL   J. Mol. Evol. 53:634-641(2001).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
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; Y15180; CAA75479.1; -; Genomic_DNA.
DR   EMBL; AJ404477; CAC20654.1; -; Genomic_DNA.
DR   RefSeq; NP_073278.1; NC_002639.1.
DR   AlphaFoldDB; O63912; -.
DR   SMR; O63912; -.
DR   GeneID; 802341; -.
DR   CTD; 4508; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..228
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082141"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   228 AA;  25341 MW;  3A9F826238C55539 CRC64;
     MMMSLFNTFE SPYFLGFPLM IFIAILISLT MFIPDNNLLI KNQSSMLAST FLKTMTKEIF
     SPIKKSGHSW ALLLMTTLMF IFLNNITGLL PYTFTVTSQL SLNMAMAIPL WLGTIIMGAT
     SQPSHSLAHL LPEGTPMTLA PFLIVIESIS IIIRPLALGV RLTANITAGH LLIHLVSLAL
     INLTKSLPLL FLTFSVFILL LILELAVSFI QAYVFVMLVS LYLEENLI