ATP6_CHICK
ID ATP6_CHICK Reviewed; 227 AA.
AC P14092;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
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. 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; X15841; CAA33842.1; -; Genomic_DNA.
DR EMBL; X52392; CAA36630.1; -; Genomic_DNA.
DR PIR; S10192; S10192.
DR RefSeq; NP_006920.1; NC_001323.1.
DR AlphaFoldDB; P14092; -.
DR SMR; P14092; -.
DR STRING; 9031.ENSGALP00000034617; -.
DR PaxDb; P14092; -.
DR Ensembl; ENSGALT00000076413; ENSGALP00000057531; ENSGALG00000041091.
DR VEuPathDB; HostDB:geneid_63549466; -.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P14092; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR PhylomeDB; P14092; -.
DR TreeFam; TF343395; -.
DR Reactome; R-GGA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-GGA-8949613; Cristae formation.
DR PRO; PR:P14092; -.
DR Proteomes; UP000000539; Mitochondrion.
DR Bgee; ENSGALG00000041091; Expressed in cerebellum and 13 other tissues.
DR ExpressionAtlas; P14092; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IEA:Ensembl.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IEA:Ensembl.
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_0000082106"
FT TRANSMEM 12..32
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 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 227 AA; 24797 MW; E3BC5E98A884385D CRC64;
MNLSFFDQFS SPCLLGIPLI LPSLLLPALL LPSPGNRWIN NRLSTIQLWF THLITKQLMT
PLNKAGHKWA LLLTSLILML LSINLLGLLP YTFTPTTQLS MNMALALPLW LATLLTGLRN
QPSASLGHLL PEGTPTPLIP ALIMIETTSL LIRPLALGVR LTANLTAGHL LIQLISTATI
ALLPMMPSIS ALTALILFLL TILEVAVAMI QAYVFVLLLS LYLQENI
