ATP8_SHEEP
ID ATP8_SHEEP Reviewed; 66 AA.
AC O78751; O99388;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ATP synthase protein 8;
DE AltName: Full=A6L;
DE AltName: Full=F-ATPase subunit 8;
GN Name=MT-ATP8; Synonyms=ATP8, ATPASE8, MTATP8;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Peripheral blood;
RX PubMed=9734874; DOI=10.2527/1998.7682207x;
RA Tartaglia M., Saulle E.;
RT "Rapid communication: nucleotide sequence of porcine and ovine tRNA(Lys)
RT and ATPase8 mitochondrial genes.";
RL J. Anim. Sci. 76:2207-2208(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. Part of the complex
CC F(0) domain. Minor subunit located with subunit a in the membrane (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. Component of an ATP synthase
CC complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF,
CC ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO,
CC ATP5MG, ATP5MK and ATP5MJ (By similarity). Interacts with PRICKLE3 (By
CC similarity). {ECO:0000250|UniProtKB:P03928}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
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DR EMBL; AF010406; AAD10100.1; -; Genomic_DNA.
DR EMBL; AF039171; AAD05067.1; -; Genomic_DNA.
DR PIR; T11054; T11054.
DR RefSeq; NP_008410.1; NC_001941.1.
DR PDB; 6TT7; EM; 3.50 A; Q=1-66.
DR PDB; 6ZA9; EM; 3.76 A; Q=1-66.
DR PDBsum; 6TT7; -.
DR PDBsum; 6ZA9; -.
DR AlphaFoldDB; O78751; -.
DR SMR; O78751; -.
DR STRING; 9940.ENSOARP00000000005; -.
DR Ensembl; ENSOART00000000021; ENSOARP00000000005; ENSOARG00000000021.
DR GeneID; 808253; -.
DR KEGG; oas:808253; -.
DR CTD; 4509; -.
DR eggNOG; ENOG502T21P; Eukaryota.
DR HOGENOM; CLU_2811757_0_0_1; -.
DR OMA; LDTSTWF; -.
DR OrthoDB; 1621322at2759; -.
DR Proteomes; UP000002356; Mitochondrion.
DR Bgee; ENSOARG00000000021; Expressed in cerebellum and 53 other tissues.
DR ExpressionAtlas; O78751; 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:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
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 InterPro; IPR039017; ATP8_mammal.
DR InterPro; IPR001421; ATP8_metazoa.
DR PANTHER; PTHR13722; PTHR13722; 1.
DR Pfam; PF00895; ATP-synt_8; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP synthesis; CF(0); Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..66
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195587"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 54
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P03930"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P03930"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P03930"
FT CONFLICT 23
FT /note="I -> V (in Ref. 2; AAD05067)"
FT /evidence="ECO:0000305"
FT CONFLICT 35..36
FT /note="HN -> YS (in Ref. 2; AAD05067)"
FT /evidence="ECO:0000305"
FT CONFLICT 44
FT /note="T -> M (in Ref. 2; AAD05067)"
FT /evidence="ECO:0000305"
FT HELIX 2..4
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:6TT7"
FT HELIX 22..29
FT /evidence="ECO:0007829|PDB:6TT7"
SQ SEQUENCE 66 AA; 7910 MW; 5BCCC68AF6498B93 CRC64;
MPQLDTSTWL TMILSMFLVL FIIFQLKISK HNFYHNPELM TTKTPKQNTP WETKWTKIYL
PLSLPL
