ATP8_MOUSE
ID ATP8_MOUSE Reviewed; 67 AA.
AC P03930;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=ATP synthase protein 8;
DE AltName: Full=A6L;
DE AltName: Full=F-ATPase subunit 8;
GN Name=Mtatp8; Synonyms=Atp8, mt-Atp8;
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 [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 [3]
RP PROTEIN SEQUENCE OF 58-67, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [5]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-57, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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; J01420; AAB48648.1; -; Genomic_DNA.
DR EMBL; V00711; CAA24084.1; -; Genomic_DNA.
DR EMBL; AY172335; AAN85126.1; -; Genomic_DNA.
DR PIR; A01064; PWMS8.
DR RefSeq; NP_904332.1; NC_005089.1.
DR AlphaFoldDB; P03930; -.
DR SMR; P03930; -.
DR BioGRID; 201540; 16.
DR STRING; 10090.ENSMUSP00000080995; -.
DR iPTMnet; P03930; -.
DR PhosphoSitePlus; P03930; -.
DR EPD; P03930; -.
DR jPOST; P03930; -.
DR PaxDb; P03930; -.
DR PeptideAtlas; P03930; -.
DR PRIDE; P03930; -.
DR ProteomicsDB; 277132; -.
DR Antibodypedia; 64403; 42 antibodies from 13 providers.
DR Ensembl; ENSMUST00000082407; ENSMUSP00000080995; ENSMUSG00000064356.
DR GeneID; 17706; -.
DR KEGG; mmu:17706; -.
DR CTD; 4509; -.
DR MGI; MGI:99926; mt-Atp8.
DR VEuPathDB; HostDB:ENSMUSG00000064356; -.
DR eggNOG; ENOG502T21P; Eukaryota.
DR GeneTree; ENSGT00390000008771; -.
DR HOGENOM; CLU_2811757_0_0_1; -.
DR InParanoid; P03930; -.
DR OMA; LDTSTWF; -.
DR OrthoDB; 1621322at2759; -.
DR PhylomeDB; P03930; -.
DR TreeFam; TF343854; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR ChiTaRS; mt-Atp8; mouse.
DR PRO; PR:P03930; -.
DR Proteomes; UP000000589; Mitochondrion.
DR RNAct; P03930; protein.
DR Bgee; ENSMUSG00000064356; Expressed in striatum and 62 other tissues.
DR ExpressionAtlas; P03930; baseline and differential.
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:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:MGI.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:MGI.
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 Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..67
FT /note="ATP synthase protein 8"
FT /id="PRO_0000195551"
FT TRANSMEM 8..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 54
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 54
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 57
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
SQ SEQUENCE 67 AA; 7766 MW; 49C9BB34FF275349 CRC64;
MPQLDTSTWF ITIISSMITL FILFQLKVSS QTFPLAPSPK SLTTMKVKTP WELKWTKIYL
PHSLPQQ
