ATP6_TROHI
ID ATP6_TROHI Reviewed; 212 AA.
AC O03570; O03358;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
DE Flags: Fragment;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS Tropidurus hispidus (Venezuelan lizard) (Peters' lava lizard).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Iguanidae; Tropidurinae; Tropidurus.
OX NCBI_TaxID=44142;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9108063; DOI=10.1073/pnas.94.8.3828;
RA Vitt L.J., Caldwell J.P., Zani P.A., Titus T.A.;
RT "The role of habitat shift in the evolution of lizard morphology: evidence
RT from tropical Tropidurus.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3828-3832(1997).
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; U83494; AAB84365.1; -; Genomic_DNA.
DR EMBL; U83496; AAB84367.1; -; Genomic_DNA.
DR EMBL; U83497; AAB84368.1; -; Genomic_DNA.
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..>212
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082179"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 3
FT /note="M -> T"
FT VARIANT 187
FT /note="V -> M"
FT VARIANT 211
FT /note="Y -> I"
FT NON_TER 1
FT NON_TER 212
SQ SEQUENCE 212 AA; 23225 MW; 54BD321B90909A3A CRC64;
PQMMGIPLIL IAIFLPTLLI YTSPTRLSTN RMTTLQLWLT NTITKQLFLP VNTPGHKWAA
MLMTLMIXLL SMNLLGLLPY TFTPTTQLSM NMALAIPLWL ATVLTGLRNQ PTASLGHLLP
EGTPTPLIPL LIIIETVSLF IRPLALGVRL TANLTAGHLL IQLISTAAFV LLPMMTLTAL
STFIVLVLLT GLEIAVAMIQ AYVFTLLLTL YL
