ID   ATP6_DANRE              Reviewed;         227 AA.
AC   Q9MIY5;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=ATP synthase subunit a;
DE   AltName: Full=F-ATPase protein 6;
GN   Name=mt-atp6; Synonyms=atp6, atpase6, mtatp6;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX   PubMed=11691861; DOI=10.1101/gr.156801;
RA   Broughton R.E., Milam J.E., Roe B.A.;
RT   "The complete sequence of the zebrafish (Danio rerio) mitochondrial genome
RT   and evolutionary patterns in vertebrate mitochondrial DNA.";
RL   Genome Res. 11:1958-1967(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.
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.
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; AC024175; AAF74302.1; -; Genomic_DNA.
DR   RefSeq; NP_059336.1; NC_002333.2.
DR   AlphaFoldDB; Q9MIY5; -.
DR   SMR; Q9MIY5; -.
DR   STRING; 7955.ENSDARP00000087874; -.
DR   PaxDb; Q9MIY5; -.
DR   Ensembl; ENSDART00000093612; ENSDARP00000087874; ENSDARG00000063911.
DR   GeneID; 140519; -.
DR   KEGG; dre:140519; -.
DR   CTD; 4508; -.
DR   ZFIN; ZDB-GENE-011205-18; mt-atp6.
DR   eggNOG; KOG4665; Eukaryota.
DR   GeneTree; ENSGT00390000005568; -.
DR   HOGENOM; CLU_041018_0_2_1; -.
DR   InParanoid; Q9MIY5; -.
DR   OMA; FFDQFMS; -.
DR   OrthoDB; 1095315at2759; -.
DR   PhylomeDB; Q9MIY5; -.
DR   TreeFam; TF343395; -.
DR   Reactome; R-DRE-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-DRE-8949613; Cristae formation.
DR   PRO; PR:Q9MIY5; -.
DR   Proteomes; UP000000437; Mitochondrion MT.
DR   Proteomes; UP000814640; Mitochondrion.
DR   Bgee; ENSDARG00000063911; Expressed in early embryo and 22 other tissues.
DR   ExpressionAtlas; Q9MIY5; baseline.
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; IBA:GO_Central.
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..227
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082099"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   227 AA;  25093 MW;  FE49495C77C8BCC4 CRC64;
     MMTSFFDQFA SPYLLGIPLI LVAMLLPWLL FPAPTSRWIN NRLITVQTWL TGRFTNQLMT
     PLNFSGHKWA LLFASLMVFL ITINLLGLLP YTFTPTTQLS LNMGFAVPLW LATVIIGMKN
     QPTIALGHLL PEGTPIPLIP ALIIIETISL FIRPLALGVR LTANLTAGHL LIQLIATAVF
     VLLPMMPAVA ILTASVLFLL TLLEVAVAMI QAYVFILLLS LYLQENI