ATP6_SHEEP
ID ATP6_SHEEP Reviewed; 226 AA.
AC O78752;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=ATP synthase subunit a;
DE AltName: Full=F-ATPase protein 6;
GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6;
OS Ovis aries (Sheep).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Merinolandschaf {ECO:0000312|Proteomes:UP000002356}; TISSUE=Liver;
RX PubMed=9767689; DOI=10.1007/pl00006401;
RA Hiendleder S., Lewalski H., Wassmuth R., Janke A.;
RT "The complete mitochondrial DNA sequence of the domestic sheep (Ovis aries)
RT and comparison with the other major ovine haplotype.";
RL J. Mol. Evol. 47:441-448(1998).
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; AF010406; AAD10101.1; -; Genomic_DNA.
DR PIR; T11055; T11055.
DR RefSeq; NP_008411.1; NC_001941.1.
DR PDB; 6TT7; EM; 3.50 A; N=1-226.
DR PDB; 6ZA9; EM; 3.76 A; N=1-226.
DR PDBsum; 6TT7; -.
DR PDBsum; 6ZA9; -.
DR AlphaFoldDB; O78752; -.
DR SMR; O78752; -.
DR STRING; 9940.ENSOARP00000000006; -.
DR Ensembl; ENSOART00000000022; ENSOARP00000000006; ENSOARG00000000022.
DR Ensembl; ENSOART00020000022; ENSOARP00020000006; ENSOARG00020000022.
DR GeneID; 808254; -.
DR KEGG; oas:808254; -.
DR CTD; 4508; -.
DR eggNOG; KOG4665; Eukaryota.
DR HOGENOM; CLU_041018_0_2_1; -.
DR OMA; FFDQFMS; -.
DR OrthoDB; 1095315at2759; -.
DR Proteomes; UP000002356; Mitochondrion.
DR Bgee; ENSOARG00000000022; Expressed in adrenal cortex and 55 other tissues.
DR ExpressionAtlas; O78752; baseline.
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:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; 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 3D-structure; ATP synthesis; CF(0); Hydrogen ion transport; Ion transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..226
FT /note="ATP synthase subunit a"
FT /id="PRO_0000082170"
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"
FT TURN 3..6
FT /evidence="ECO:0007829|PDB:6TT7"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:6TT7"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 26..30
FT /evidence="ECO:0007829|PDB:6TT7"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 41..57
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:6TT7"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 98..118
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:6TT7"
FT TURN 125..128
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 152..184
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 186..223
FT /evidence="ECO:0007829|PDB:6TT7"
SQ SEQUENCE 226 AA; 24798 MW; CFE7F8A9FF1D75E5 CRC64;
MNENLFASFI TPMMFGLPLV TLIVLFPSLL FPTSNRLVNN RLISLQQWML QLVSKQMMSI
HNTKGQTWAL MLMSLILFIG STNLLGLLPH SFTPTTQLSM NLGMAIPLWG GAVITGFRNK
TKASLAHFLP QGTPTPLIPM LVIIETISLF IQPVALAVRL TANITAGHLL IHLIGGATLA
LMSINTTTAL ITFIILILLT VLEFAVAMIQ AYVFTLLVSL YLHDNT
