ATP8_BOVIN
ID ATP8_BOVIN Reviewed; 66 AA.
AC P03929;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 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 PARTIAL PROTEIN SEQUENCE.
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 PROTEIN SEQUENCE OF 1-5, AND FORMYLATION AT MET-1.
RC TISSUE=Heart;
RX PubMed=1827992; DOI=10.1021/bi00236a007;
RA Walker J.E., Lutter R., Dupuis A., Runswick M.J.;
RT "Identification of the subunits of F1F0-ATPase from bovine heart
RT mitochondria.";
RL Biochemistry 30:5369-5378(1991).
RN [5]
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).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE ATP SYNTHASE
RP COMPLEX.
RX PubMed=25851905; DOI=10.1074/jbc.m115.645283;
RA Lee J., Ding S., Walpole T.B., Holding A.N., Montgomery M.G.,
RA Fearnley I.M., Walker J.E.;
RT "Organization of Subunits in the Membrane Domain of the Bovine F-ATPase
RT Revealed by Covalent Cross-linking.";
RL J. Biol. Chem. 290:13308-13320(2015).
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. Interacts with PRICKLE3 (By similarity).
CC {ECO:0000250|UniProtKB:P03928, ECO:0000269|PubMed:17570365,
CC ECO:0000269|PubMed:25851905}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V00654; CAA24001.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08333.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08346.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12793.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12806.1; -; Genomic_DNA.
DR PIR; A01063; PWBO8.
DR RefSeq; YP_209209.1; NC_006853.1.
DR PDB; 6ZBB; EM; 3.61 A; 8=1-66.
DR PDB; 6ZIQ; EM; 4.33 A; 8=1-66.
DR PDB; 6ZIT; EM; 3.49 A; 8=1-66.
DR PDB; 6ZIU; EM; 6.02 A; 8=1-66.
DR PDB; 6ZPO; EM; 4.00 A; 8=1-66.
DR PDB; 6ZQM; EM; 3.29 A; 8=1-66.
DR PDB; 6ZQN; EM; 4.00 A; 8=1-66.
DR PDB; 7AJB; EM; 9.20 A; 8/A8=1-66.
DR PDB; 7AJC; EM; 11.90 A; 8/A8=1-66.
DR PDB; 7AJD; EM; 9.00 A; 8/A8=1-66.
DR PDB; 7AJE; EM; 9.40 A; 8/A8=1-66.
DR PDB; 7AJF; EM; 8.45 A; 8/A8=1-66.
DR PDB; 7AJG; EM; 10.70 A; 8/A8=1-66.
DR PDB; 7AJH; EM; 9.70 A; 8/A8=1-66.
DR PDB; 7AJI; EM; 11.40 A; 8/A8=1-66.
DR PDB; 7AJJ; EM; 13.10 A; 8/A8=1-66.
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; P03929; -.
DR SMR; P03929; -.
DR CORUM; P03929; -.
DR IntAct; P03929; 2.
DR MINT; P03929; -.
DR STRING; 9913.ENSBTAP00000053143; -.
DR PaxDb; P03929; -.
DR PeptideAtlas; P03929; -.
DR Ensembl; ENSBTAT00000060553; ENSBTAP00000053143; ENSBTAG00000043564.
DR GeneID; 3283881; -.
DR KEGG; bta:3283881; -.
DR CTD; 4509; -.
DR VEuPathDB; HostDB:ENSBTAG00000043564; -.
DR eggNOG; ENOG502T21P; Eukaryota.
DR GeneTree; ENSGT00390000008771; -.
DR HOGENOM; CLU_2811757_0_0_1; -.
DR InParanoid; P03929; -.
DR OMA; LDTSTWF; -.
DR OrthoDB; 1621322at2759; -.
DR TreeFam; TF343854; -.
DR Reactome; R-BTA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-BTA-8949613; Cristae formation.
DR Proteomes; UP000009136; Mitochondrion.
DR Bgee; ENSBTAG00000043564; Expressed in thymus 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:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
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 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); Direct protein sequencing;
KW Formylation; Hydrogen ion transport; Ion transport; Membrane;
KW Mitochondrion; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..66
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195495"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:1827992,
FT ECO:0000269|PubMed:2875870"
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 TURN 2..4
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6ZIT"
FT HELIX 9..28
FT /evidence="ECO:0007829|PDB:6ZIT"
SQ SEQUENCE 66 AA; 7937 MW; 0DED46ADEF5D8BDE CRC64;
MPQLDTSTWL TMILSMFLTL FIIFQLKVSK HNFYHNPELT PTKMLKQNTP WETKWTKIYL
PLLLPL
