ATP5H_MOUSE
ID ATP5H_MOUSE Reviewed; 161 AA.
AC Q9DCX2; B1ASE1; Q542H1; Q7M0I0; Q91YK9;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=ATP synthase subunit d, mitochondrial {ECO:0000305};
DE Short=ATPase subunit d;
DE AltName: Full=ATP synthase peripheral stalk subunit d {ECO:0000305};
GN Name=Atp5pd {ECO:0000250|UniProtKB:O75947}; Synonyms=Atp5h;
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 [MRNA].
RC TISSUE=Kidney;
RA Chen H., Huang C.-H.;
RT "The mouse ATP synthase subunit D interacts with the C-terminal domain of
RT Rh type C glycoprotein (Rhcg).";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP PROTEIN SEQUENCE OF 10-25; 33-73; 86-111; 124-144 AND 149-161, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 150-161.
RA Kato H.;
RT "Analysis of proteins isolated by two dimensional electrophoresis of mouse
RT neuroblastoma cells.";
RL Kawasaki Igakkaishi 22:245-259(1996).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y.,
RA Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT "Substrate and functional diversity of lysine acetylation revealed by a
RT proteomics survey.";
RL Mol. Cell 23:607-618(2006).
RN [8]
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 [9]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-85; LYS-95; LYS-144 AND
RP LYS-149, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-48; LYS-63; LYS-72;
RP LYS-78; LYS-85; LYS-95; LYS-117; LYS-144 AND LYS-149, AND IDENTIFICATION BY
RP 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 synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. Part of the complex
CC F(0) domain and the peripheric stalk, which acts as a stator to hold
CC the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC relative to the rotary elements.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(0) seems to have nine
CC subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP
CC synthase complex composed of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME,
CC ATP5PF, ATP5MF, MT-ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C,
CC ATP5PO, ATP5MG, ATP5MK and ATP5MJ (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- SIMILARITY: Belongs to the ATPase d subunit family. {ECO:0000305}.
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DR EMBL; AF354051; AAL83962.1; -; mRNA.
DR EMBL; AK002376; BAB22053.1; -; mRNA.
DR EMBL; AK088617; BAC40456.1; -; mRNA.
DR EMBL; AL627096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016547; AAH16547.1; -; mRNA.
DR EMBL; BC081431; AAH81431.1; -; mRNA.
DR CCDS; CCDS25633.1; -.
DR PIR; PN0046; PN0046.
DR RefSeq; NP_082138.1; NM_027862.1.
DR RefSeq; XP_006534317.1; XM_006534254.1.
DR AlphaFoldDB; Q9DCX2; -.
DR SMR; Q9DCX2; -.
DR BioGRID; 214850; 67.
DR IntAct; Q9DCX2; 7.
DR MINT; Q9DCX2; -.
DR STRING; 10090.ENSMUSP00000102147; -.
DR iPTMnet; Q9DCX2; -.
DR PhosphoSitePlus; Q9DCX2; -.
DR SwissPalm; Q9DCX2; -.
DR REPRODUCTION-2DPAGE; Q9DCX2; -.
DR CPTAC; non-CPTAC-3637; -.
DR EPD; Q9DCX2; -.
DR jPOST; Q9DCX2; -.
DR MaxQB; Q9DCX2; -.
DR PaxDb; Q9DCX2; -.
DR PeptideAtlas; Q9DCX2; -.
DR PRIDE; Q9DCX2; -.
DR ProteomicsDB; 265167; -.
DR TopDownProteomics; Q9DCX2; -.
DR Antibodypedia; 32083; 268 antibodies from 32 providers.
DR DNASU; 71679; -.
DR Ensembl; ENSMUST00000043931; ENSMUSP00000046256; ENSMUSG00000034566.
DR Ensembl; ENSMUST00000073791; ENSMUSP00000086072; ENSMUSG00000034566.
DR Ensembl; ENSMUST00000106537; ENSMUSP00000102147; ENSMUSG00000034566.
DR Ensembl; ENSMUST00000180072; ENSMUSP00000137071; ENSMUSG00000034566.
DR GeneID; 71679; -.
DR KEGG; mmu:71679; -.
DR UCSC; uc007mhm.1; mouse.
DR CTD; 71679; -.
DR MGI; MGI:1918929; Atp5h.
DR VEuPathDB; HostDB:ENSMUSG00000034566; -.
DR eggNOG; KOG3366; Eukaryota.
DR GeneTree; ENSGT00390000003582; -.
DR HOGENOM; CLU_130600_0_0_1; -.
DR InParanoid; Q9DCX2; -.
DR OMA; VSKGRWA; -.
DR OrthoDB; 1299717at2759; -.
DR PhylomeDB; Q9DCX2; -.
DR TreeFam; TF314031; -.
DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-MMU-8949613; Cristae formation.
DR BioGRID-ORCS; 71679; 15 hits in 57 CRISPR screens.
DR ChiTaRS; Atp5h; mouse.
DR PRO; PR:Q9DCX2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DCX2; protein.
DR Bgee; ENSMUSG00000034566; Expressed in heart and 100 other tissues.
DR ExpressionAtlas; Q9DCX2; baseline and differential.
DR Genevisible; Q9DCX2; MM.
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:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); ISO:MGI.
DR GO; GO:0000274; C:mitochondrial proton-transporting ATP synthase, stator stalk; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
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 Gene3D; 6.10.280.70; -; 1.
DR InterPro; IPR008689; ATP_synth_F0_dsu_mt.
DR InterPro; IPR036228; ATP_synth_F0_dsu_sf_mt.
DR PANTHER; PTHR12700; PTHR12700; 1.
DR Pfam; PF05873; Mt_ATP-synt_D; 1.
DR PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
DR SUPFAM; SSF161065; SSF161065; 1.
PE 1: Evidence at protein level;
KW Acetylation; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P13620"
FT CHAIN 2..161
FT /note="ATP synthase subunit d, mitochondrial"
FT /id="PRO_0000071674"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P13620"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 48
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 63
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 78
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 78
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 85
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 85
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 95
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 95
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:16916647,
FT ECO:0007744|PubMed:23576753"
FT MOD_RES 144
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 144
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 149
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 149
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 90
FT /note="V -> L (in Ref. 4; AAH16547)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..161
FT /note="ENL -> LMC (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 18749 MW; 380F3C6671D6DB4D CRC64;
MAGRKLALKT IDWVSFVEVM PQNQKAIGNA LKSWNETFHA RLASLSEKPP AIDWAYYRAN
VAKPGLVDDF EKKYNALKIP VPEDKYTALV DQEEKEDVKS CAEFVSGSQL RIQEYEKQLE
KMRNIIPFDQ MTIDDLNEIF PETKLDKKKY PYWPHQPIEN L
