ATP6_MYTED
ID ATP6_MYTED Reviewed; 238 AA.
AC Q00224; Q68SR0;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=ATP6;
OS Mytilus edulis (Blue mussel).
OG Mitochondrion.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1386586; DOI=10.1093/genetics/131.2.397;
RA Hoffmann R.J., Boore J.L., Brown W.M.;
RT "A novel mitochondrial genome organization for the blue mussel, Mytilus
RT edulis.";
RL Genetics 131:397-412(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014161; DOI=10.1093/molbev/msh090;
RA Boore J.L., Medina M., Rosenberg L.A.;
RT "Complete sequences of the highly rearranged molluscan mitochondrial
RT genomes of the scaphopod Graptacme eborea and the bivalve Mytilus edulis.";
RL Mol. Biol. Evol. 21:1492-1503(2004).
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; AY484747; AAT98403.1; -; Genomic_DNA.
DR PIR; S28758; S28758.
DR RefSeq; YP_073344.1; NC_006161.1.
DR AlphaFoldDB; Q00224; -.
DR SMR; Q00224; -.
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; 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.
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..238
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082140"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 238 AA; 25773 MW; 0832F2A7D41757CF CRC64;
MLMDVFSSFD AHSYNLIWLS MPLWLLSSMV PMTVLFSDVH SKSGSTSSFR SLVLSFTYSM
IRLNGKGLKL SGFPLVMSGL FMMILMLNLS GNFPFFFPVS GQFVFGFSFA LSIWTCLVLS
SLLCSFEQGL MSLVPTGCPL ILVPFMVVVE LISGMLRPLT LVLRLTLNLG AGKVILTMCS
SELVVGWLNS SSLITGVGGI KGLLMGGGVF GAAEVAIACI QCYIFCVLLC LYTEDHSS