ATP6_PARLI
ID ATP6_PARLI Reviewed; 232 AA.
AC P12696;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=ATP6;
OS Paracentrotus lividus (Common sea urchin).
OG Mitochondrion.
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Paracentrotus.
OX NCBI_TaxID=7656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2544576; DOI=10.1016/s0021-9258(18)60413-2;
RA Cantatore P., Roberti M., Rainaldi G., Gadaleta M.N., Saccone C.;
RT "The complete nucleotide sequence, gene organization, and genetic code of
RT the mitochondrial genome of Paracentrotus lividus.";
RL J. Biol. Chem. 264:10965-10975(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-232.
RX PubMed=3596250; DOI=10.1016/0378-1119(87)90091-6;
RA Cantatore P., Roberti M., Morisco P., Rainaldi G., Gadaleta M.N.,
RA Saccone C.;
RT "A novel gene order in the Paracentrotus lividus mitochondrial genome.";
RL Gene 53:41-54(1987).
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; J04815; AAA68139.1; -; Genomic_DNA.
DR EMBL; M16522; AAA31993.2; -; Genomic_DNA.
DR PIR; G34284; G34284.
DR RefSeq; NP_008127.1; NC_001572.1.
DR AlphaFoldDB; P12696; -.
DR SMR; P12696; -.
DR GeneID; 807714; -.
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..232
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082150"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 232 AA; 25827 MW; DB0979ACAA45F87E CRC64;
MTMTITVSIF GQFFPETLLF IPMNLFSIVF ALSWIAFIYP TNWAPSRFQS IWASFRANVL
EMIFQNTSPN TAPWAGLITT VFIVILSANV LGLFPYAFTA TSHISLTYSL GFPIWMAVNI
LGFYLAFNSR LSHLVPQGTP SALIPLMVWI ETLSLFAQPI ALGLRLAANL TAGHLLIFLL
STAIWLLSSS LMVSSIPIFV IFVLLFILEI GVACIEAYVF TALVHFYLQQ NV