ATP6_MOUSE
ID ATP6_MOUSE Reviewed; 226 AA.
AC P00848;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=Mtatp6; Synonyms=Atp6, Atpase6, mt-Atp6;
OS Mus musculus (Mouse).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7;
RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.;
RT "Sequence and gene organization of mouse mitochondrial DNA.";
RL Cell 26:167-180(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Sato M., Matsuki Y., Oguma T., Tadakuma T.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12954771; DOI=10.1093/nar/gkg739;
RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S.,
RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., Bai Y.,
RA Enriquez J.A.;
RT "Revisiting the mouse mitochondrial DNA sequence.";
RL Nucleic Acids Res. 31:5349-5355(2003).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; J01420; AAB48649.1; -; Genomic_DNA.
DR EMBL; V00711; CAA24085.1; -; Genomic_DNA.
DR EMBL; AF093677; AAC63375.1; -; mRNA.
DR EMBL; AY172335; AAN85127.1; -; Genomic_DNA.
DR PIR; A01051; PWMS6.
DR RefSeq; NP_904333.1; NC_005089.1.
DR AlphaFoldDB; P00848; -.
DR SMR; P00848; -.
DR IntAct; P00848; 1.
DR STRING; 10090.ENSMUSP00000080996; -.
DR jPOST; P00848; -.
DR PaxDb; P00848; -.
DR PeptideAtlas; P00848; -.
DR PRIDE; P00848; -.
DR ProteomicsDB; 265181; -.
DR Antibodypedia; 58052; 71 antibodies from 21 providers.
DR Ensembl; ENSMUST00000082408; ENSMUSP00000080996; ENSMUSG00000064357.
DR GeneID; 17705; -.
DR KEGG; mmu:17705; -.
DR CTD; 4508; -.
DR MGI; MGI:99927; mt-Atp6.
DR VEuPathDB; HostDB:ENSMUSG00000064357; -.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P00848; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR PhylomeDB; P00848; -.
DR TreeFam; TF343395; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR ChiTaRS; mt-Atp6; mouse.
DR PRO; PR:P00848; -.
DR Proteomes; UP000000589; Mitochondrion.
DR RNAct; P00848; protein.
DR Bgee; ENSMUSG00000064357; Expressed in epiblast (generic) and 107 other tissues.
DR ExpressionAtlas; P00848; 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; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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; ISO:MGI.
DR GO; GO:0007568; P:aging; 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; ISO:MGI.
DR GO; GO:0055093; P:response to hyperoxia; 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 1: Evidence at protein level;
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..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082139"
FT TRANSMEM 6..26
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"
SQ SEQUENCE 226 AA; 25096 MW; 9941E80F027C4DA7 CRC64;
MNENLFASFI TPTMMGFPIV VAIIMFPSIL FPSSKRLINN RLHSFQHWLV KLIIKQMMLI
HTPKGRTWTL MIVSLIMFIG STNLLGLLPH TFTPTTQLSM NLSMAIPLWA GAVITGFRHK
LKSSLAHFLP QGTPISLIPM LIIIETISLF IQPMALAVRL TANITAGHLL MHLIGGATLV
LMNISPPTAT ITFIILLLLT ILEFAVALIQ AYVFTLLVSL YLHDNT
