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   24-JAN-2024, entry version 172.
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       ATP5MPL (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   BioGRID; 201539; 1.
DR   IntAct; P00848; 1.
DR   STRING; 10090.ENSMUSP00000080996; -.
DR   GlyGen; P00848; 1 site, 1 O-linked glycan (1 site).
DR   jPOST; P00848; -.
DR   PaxDb; 10090-ENSMUSP00000080996; -.
DR   PeptideAtlas; P00848; -.
DR   ProteomicsDB; 265181; -.
DR   Pumba; P00848; -.
DR   Antibodypedia; 58052; 105 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000082408.1; ENSMUSP00000080996.1; ENSMUSG00000064357.1.
DR   GeneID; 17705; -.
DR   KEGG; mmu:17705; -.
DR   AGR; MGI:99927; -.
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; 463312at2759; -.
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 110 other cell types or tissues.
DR   ExpressionAtlas; P00848; baseline and differential.
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; 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   CDD; cd00310; ATP-synt_Fo_a_6; 1.
DR   Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 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   NCBIfam; TIGR01131; ATP_synt_6_or_A; 1.
DR   PANTHER; PTHR11410; ATP SYNTHASE SUBUNIT A; 1.
DR   PANTHER; PTHR11410:SF0; ATP SYNTHASE SUBUNIT A; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; F1F0 ATP synthase subunit 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
//