ATP6_PONPY
ID ATP6_PONPY Reviewed; 226 AA.
AC Q95A26; P92719; P92720;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS Pongo pygmaeus (Bornean orangutan).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9600;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7530363; DOI=10.1073/pnas.92.2.532;
RA Horai S., Hayasaka K., Kondo R., Tsugane K., Takahata N.;
RT "Recent African origin of modern humans revealed by complete sequences of
RT hominoid mitochondrial DNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:532-536(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-4 AND ALA-178.
RC STRAIN=Isolate Anna, and Isolate Dennis;
RX PubMed=8875856; DOI=10.1007/bf02337514;
RA Xu X., Arnason U.;
RT "The mitochondrial DNA molecule of Sumatran orangutan and a molecular
RT proposal for two (Bornean and Sumatran) species of orangutan.";
RL J. Mol. Evol. 43:431-437(1996).
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. Component of an ATP synthase complex composed of
CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-
CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and
CC ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct
CC (By similarity). {ECO:0000250|UniProtKB:P00846,
CC ECO:0000250|UniProtKB:P00847}.
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; D38115; BAA85288.1; -; Genomic_DNA.
DR EMBL; X97714; CAA66300.1; -; Genomic_DNA.
DR EMBL; X97710; CAA66296.1; -; Genomic_DNA.
DR RefSeq; NP_008230.1; NC_001646.1.
DR AlphaFoldDB; Q95A26; -.
DR SMR; Q95A26; -.
DR GeneID; 807900; -.
DR CTD; 4508; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
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..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082160"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 4
FT /note="D -> N (in strain: Isolate Anna)"
FT /evidence="ECO:0000269|PubMed:8875856"
FT /id="VAR_019552"
FT VARIANT 178
FT /note="T -> A (in strain: Isolate Anna)"
FT /evidence="ECO:0000269|PubMed:8875856"
FT /id="VAR_019553"
SQ SEQUENCE 226 AA; 24933 MW; 040592741EEEEA42 CRC64;
MNEDLFTPFT TPTVLGLPAA ILVILFPPLL VPTSKHFINN RLITTQQWLI RLTLKQMMIT
HNTKGRTWSL MLTSLIIFIA STNLLGLFPY SFTPTTQLSM NLAMAIPLWA STVAMGLRFK
AKISLAHLLP QGTPTPLIPM LIIIETISLF IQPLALAVRL TANITAGHLL MHLIGSATLT
MLTINLPLTL ITLTILTLLT ILEIAVALIQ AYVFTLLVSL YLHDNS