ATP6_BOVIN
ID ATP6_BOVIN Reviewed; 226 AA.
AC P00847; Q8SFX8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS Bos taurus (Bovine).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-15, AND FORMYLATION AT MET-1.
RX PubMed=2875870; DOI=10.1002/j.1460-2075.1986.tb04456.x;
RA Fearnley I.M., Walker J.E.;
RT "Two overlapping genes in bovine mitochondrial DNA encode membrane
RT components of ATP synthase.";
RL EMBO J. 5:2003-2008(1986).
RN [4]
RP IDENTIFICATION IN THE ATP SYNTHASE COMPLEX.
RX PubMed=17570365; DOI=10.1016/j.febslet.2007.05.079;
RA Chen R., Runswick M.J., Carroll J., Fearnley I.M., Walker J.E.;
RT "Association of two proteolipids of unknown function with ATP synthase from
RT bovine heart mitochondria.";
RL FEBS Lett. 581:3145-3148(2007).
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 (PubMed:17570365). Interacts with DNAJC30; interaction is direct
CC (By similarity). {ECO:0000250|UniProtKB:P00846,
CC ECO:0000269|PubMed:17570365}.
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; V00654; CAA24002.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08334.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08347.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12794.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12807.1; -; Genomic_DNA.
DR PIR; A01050; PWBO6.
DR RefSeq; YP_209210.1; NC_006853.1.
DR PDB; 5ARA; EM; 6.70 A; W=10-226.
DR PDB; 5ARE; EM; 7.40 A; W=10-226.
DR PDB; 5ARH; EM; 7.20 A; W=10-226.
DR PDB; 5ARI; EM; 7.40 A; W=10-226.
DR PDB; 5FIJ; EM; 7.40 A; W=10-226.
DR PDB; 5FIK; EM; 6.40 A; W=10-226.
DR PDB; 5FIL; EM; 7.10 A; W=10-226.
DR PDB; 6ZBB; EM; 3.61 A; a=1-226.
DR PDB; 6ZIQ; EM; 4.33 A; a=1-226.
DR PDB; 6ZIT; EM; 3.49 A; a=1-226.
DR PDB; 6ZIU; EM; 6.02 A; a=1-226.
DR PDB; 6ZPO; EM; 4.00 A; a=1-226.
DR PDB; 6ZQM; EM; 3.29 A; a=1-226.
DR PDB; 6ZQN; EM; 4.00 A; a=1-226.
DR PDB; 7AJB; EM; 9.20 A; Aa/a=1-226.
DR PDB; 7AJC; EM; 11.90 A; Aa/a=1-226.
DR PDB; 7AJD; EM; 9.00 A; Aa/a=1-226.
DR PDB; 7AJE; EM; 9.40 A; Aa/a=1-226.
DR PDB; 7AJF; EM; 8.45 A; Aa/a=1-226.
DR PDB; 7AJG; EM; 10.70 A; Aa/a=1-226.
DR PDB; 7AJH; EM; 9.70 A; Aa/a=1-226.
DR PDB; 7AJI; EM; 11.40 A; Aa/a=1-226.
DR PDB; 7AJJ; EM; 13.10 A; Aa/a=1-226.
DR PDBsum; 5ARA; -.
DR PDBsum; 5ARE; -.
DR PDBsum; 5ARH; -.
DR PDBsum; 5ARI; -.
DR PDBsum; 5FIJ; -.
DR PDBsum; 5FIK; -.
DR PDBsum; 5FIL; -.
DR PDBsum; 6ZBB; -.
DR PDBsum; 6ZIQ; -.
DR PDBsum; 6ZIT; -.
DR PDBsum; 6ZIU; -.
DR PDBsum; 6ZPO; -.
DR PDBsum; 6ZQM; -.
DR PDBsum; 6ZQN; -.
DR PDBsum; 7AJB; -.
DR PDBsum; 7AJC; -.
DR PDBsum; 7AJD; -.
DR PDBsum; 7AJE; -.
DR PDBsum; 7AJF; -.
DR PDBsum; 7AJG; -.
DR PDBsum; 7AJH; -.
DR PDBsum; 7AJI; -.
DR PDBsum; 7AJJ; -.
DR AlphaFoldDB; P00847; -.
DR SMR; P00847; -.
DR CORUM; P00847; -.
DR IntAct; P00847; 1.
DR MINT; P00847; -.
DR STRING; 9913.ENSBTAP00000053155; -.
DR PaxDb; P00847; -.
DR PRIDE; P00847; -.
DR Ensembl; ENSBTAT00000060539; ENSBTAP00000053155; ENSBTAG00000043584.
DR GeneID; 3283882; -.
DR KEGG; bta:3283882; -.
DR CTD; 4508; -.
DR VEuPathDB; HostDB:ENSBTAG00000043584; -.
DR eggNOG; KOG4665; Eukaryota.
DR GeneTree; ENSGT00390000005568; -.
DR HOGENOM; CLU_041018_0_2_1; -.
DR InParanoid; P00847; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR TreeFam; TF343395; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR Proteomes; UP000009136; Mitochondrion.
DR Bgee; ENSBTAG00000043584; Expressed in ureter and 103 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA: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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; CF(0); Direct protein sequencing; Formylation;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082094"
FT TRANSMEM 9..29
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 MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:2875870"
FT VARIANT 59
FT /note="S -> N (in strain: 65)"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:6ZIT"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 63..86
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 98..119
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 121..127
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 138..181
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 186..224
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 226 AA; 24788 MW; ABAD892CB253F126 CRC64;
MNENLFTSFI TPVILGLPLV TLIVLFPSLL FPTSNRLVSN RFVTLQQWML QLVSKQMMSI
HNSKGQTWTL MLMSLILFIG STNLLGLLPH SFTPTTQLSM NLGMAIPLWA GAVITGFRNK
TKASLAHFLP QGTPTPLIPM LVIIETISLF IQPMALAVRL TANITAGHLL IHLIGGATLA
LMSISTTTAL ITFTILILLT ILEFAVAMIQ AYVFTLLVSL YLHDNT
