ID   ATPD_MOUSE              Reviewed;         168 AA.
AC   Q9D3D9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial {ECO:0000305};
DE   AltName: Full=ATP synthase F1 subunit delta {ECO:0000250|UniProtKB:P30049};
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Precursor;
GN   Name=Atp5f1d {ECO:0000250|UniProtKB:P30049}; Synonyms=Atp5d;
OS   Mus musculus (Mouse).
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 137-150 AND 157-165, AND IDENTIFICATION BY MASS
RP   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,
RC   Pancreas, 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-136 AND LYS-165, AND
RP   IDENTIFICATION BY MASS 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-136 AND LYS-165, AND
RP   IDENTIFICATION 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
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP turnover in
CC       the 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(1) domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the surrounding
CC       alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate
CC       catalytic sites on the beta subunits. {ECO:0000250|UniProtKB:P30049}.
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) seems to have
CC       nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an
CC       ATP synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD,
CC       ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D,
CC       ATP5F1C, ATP5PO, ATP5MG, ATP5MK and ATP5MPL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR   EMBL; AK018011; BAB31035.1; -; mRNA.
DR   EMBL; BC008273; AAH08273.1; -; mRNA.
DR   CCDS; CCDS24010.1; -.
DR   RefSeq; NP_079589.2; NM_025313.2.
DR   RefSeq; XP_017169541.1; XM_017314052.1.
DR   AlphaFoldDB; Q9D3D9; -.
DR   SMR; Q9D3D9; -.
DR   BioGRID; 211172; 56.
DR   IntAct; Q9D3D9; 3.
DR   STRING; 10090.ENSMUSP00000101006; -.
DR   GlyGen; Q9D3D9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9D3D9; -.
DR   PhosphoSitePlus; Q9D3D9; -.
DR   EPD; Q9D3D9; -.
DR   jPOST; Q9D3D9; -.
DR   MaxQB; Q9D3D9; -.
DR   PaxDb; 10090-ENSMUSP00000101006; -.
DR   PeptideAtlas; Q9D3D9; -.
DR   ProteomicsDB; 277092; -.
DR   Pumba; Q9D3D9; -.
DR   TopDownProteomics; Q9D3D9; -.
DR   Antibodypedia; 1258; 348 antibodies from 29 providers.
DR   DNASU; 66043; -.
DR   Ensembl; ENSMUST00000003156.15; ENSMUSP00000003156.9; ENSMUSG00000003072.16.
DR   Ensembl; ENSMUST00000105367.8; ENSMUSP00000101006.2; ENSMUSG00000003072.16.
DR   GeneID; 66043; -.
DR   KEGG; mmu:66043; -.
DR   UCSC; uc007gby.2; mouse.
DR   AGR; MGI:1913293; -.
DR   CTD; 513; -.
DR   MGI; MGI:1913293; Atp5f1d.
DR   VEuPathDB; HostDB:ENSMUSG00000003072; -.
DR   eggNOG; KOG1758; Eukaryota.
DR   GeneTree; ENSGT00390000017576; -.
DR   HOGENOM; CLU_084338_0_1_1; -.
DR   InParanoid; Q9D3D9; -.
DR   OMA; PHQTIYR; -.
DR   OrthoDB; 5394300at2759; -.
DR   PhylomeDB; Q9D3D9; -.
DR   TreeFam; TF313029; -.
DR   Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR   Reactome; R-MMU-8949613; Cristae formation.
DR   BioGRID-ORCS; 66043; 23 hits in 75 CRISPR screens.
DR   ChiTaRS; Atp5d; mouse.
DR   PRO; PR:Q9D3D9; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9D3D9; Protein.
DR   Bgee; ENSMUSG00000003072; Expressed in heart right ventricle and 261 other cell types or tissues.
DR   ExpressionAtlas; Q9D3D9; baseline and differential.
DR   GO; GO:0005740; C:mitochondrial envelope; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR   GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB.
DR   GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; ISO:MGI.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0015078; F:proton transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:Ensembl.
DR   GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR   GO; GO:0033615; P:mitochondrial proton-transporting ATP synthase complex assembly; ISS:UniProtKB.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR   GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; ISO:MGI.
DR   GO; GO:1902600; P:proton transmembrane transport; ISO:MGI.
DR   CDD; cd12152; F1-ATPase_delta; 1.
DR   Gene3D; 1.20.5.440; ATP synthase delta/epsilon subunit, C-terminal domain; 1.
DR   Gene3D; 2.60.15.10; F0F1 ATP synthase delta/epsilon subunit, N-terminal; 1.
DR   HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR   InterPro; IPR036794; ATP_F1_dsu/esu_C_sf.
DR   InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR   InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR   InterPro; IPR048937; ATPD_C_metazoa.
DR   InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR   NCBIfam; TIGR01216; ATP_synt_epsi; 1.
DR   PANTHER; PTHR13822; ATP SYNTHASE DELTA/EPSILON CHAIN; 1.
DR   PANTHER; PTHR13822:SF7; ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   Pfam; PF21335; ATPD_C_metazoa; 1.
DR   SUPFAM; SSF46604; Epsilon subunit of F1F0-ATP synthase C-terminal domain; 1.
DR   SUPFAM; SSF51344; Epsilon subunit of F1F0-ATP synthase N-terminal domain; 1.
DR   UCD-2DPAGE; Q9D3D9; -.
DR   Genevisible; Q9D3D9; MM.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW   Transport.
FT   TRANSIT         1..22
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..168
FT                   /note="ATP synthase subunit delta, mitochondrial"
FT                   /id="PRO_0000002662"
FT   MOD_RES         136
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         136
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         165
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         165
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
SQ   SEQUENCE   168 AA;  17600 MW;  EC3DF1B581B630E9 CRC64;
     MLPASLLRHP GLRRLMLQAR TYAEAAAAPA PAAGPGQMSF TFASPTQVFF DSANVKQVDV
     PTLTGAFGIL ASHVPTLQVL RPGLVVVHTE DGTTTKYFVS SGSVTVNADS SVQLLAEEAV
     TLDMLDLGAA RANLEKAQSE LSGAADEAAR AEIQIRIEAN EALVKALE
//