ATP5E_HUMAN
ID ATP5E_HUMAN Reviewed; 51 AA.
AC P56381; B2RDD0; E1P5H6; Q53XU6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=ATP synthase subunit epsilon, mitochondrial {ECO:0000305};
DE Short=ATPase subunit epsilon;
DE AltName: Full=ATP synthase F1 subunit epsilon {ECO:0000312|HGNC:HGNC:838};
GN Name=ATP5F1E {ECO:0000312|HGNC:HGNC:838};
GN Synonyms=ATP5E {ECO:0000312|HGNC:HGNC:838};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10727396; DOI=10.1042/bj3470017;
RA Tu Q., Yu L., Zhang P., Zhang M., Zhang H., Jiang J., Chen C., Zhao S.;
RT "Cloning, characterization and mapping of the human ATP5E gene,
RT identification of pseudogene ATP5EP1, and definition of the ATP5E motif.";
RL Biochem. J. 347:17-21(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Skin;
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [10]
RP VARIANT MC5DN3 CYS-12.
RX PubMed=20566710; DOI=10.1093/hmg/ddq254;
RA Mayr J.A., Havlickova V., Zimmermann F., Magler I., Kaplanova V.,
RA Jesina P., Pecinova A., Nuskova H., Koch J., Sperl W., Houstek J.;
RT "Mitochondrial ATP synthase deficiency due to a mutation in the ATP5E gene
RT for the F1 epsilon subunit.";
RL Hum. Mol. Genet. 19:3430-3439(2010).
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(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 (By similarity). {ECO:0000250}.
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 ATP5MJ (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P56381; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-3904845, EBI-11522760;
CC P56381; P30049: ATP5F1D; NbExp=4; IntAct=EBI-3904845, EBI-1049505;
CC -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DISEASE: Mitochondrial complex V deficiency, nuclear type 3 (MC5DN3)
CC [MIM:614053]: A mitochondrial disorder with heterogeneous clinical
CC manifestations including dysmorphic features, psychomotor retardation,
CC hypotonia, growth retardation, cardiomyopathy, enlarged liver,
CC hypoplastic kidneys and elevated lactate levels in urine, plasma and
CC cerebrospinal fluid. {ECO:0000269|PubMed:20566710}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the eukaryotic ATPase epsilon family.
CC {ECO:0000305}.
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DR EMBL; AF052955; AAF72736.1; -; mRNA.
DR EMBL; AF077045; AAD27778.1; -; mRNA.
DR EMBL; AK315493; BAG37877.1; -; mRNA.
DR EMBL; BT007293; AAP35957.1; -; mRNA.
DR EMBL; AL109840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75445.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75446.1; -; Genomic_DNA.
DR EMBL; BC001690; AAH01690.1; -; mRNA.
DR EMBL; BC003671; AAH03671.1; -; mRNA.
DR EMBL; BC105811; AAI05812.1; -; mRNA.
DR CCDS; CCDS13476.1; -.
DR RefSeq; NP_008817.1; NM_006886.3.
DR AlphaFoldDB; P56381; -.
DR BioGRID; 106999; 52.
DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex.
DR CORUM; P56381; -.
DR IntAct; P56381; 17.
DR STRING; 9606.ENSP00000243997; -.
DR GlyGen; P56381; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P56381; -.
DR PhosphoSitePlus; P56381; -.
DR BioMuta; ATP5E; -.
DR EPD; P56381; -.
DR jPOST; P56381; -.
DR MassIVE; P56381; -.
DR MaxQB; P56381; -.
DR PaxDb; P56381; -.
DR PeptideAtlas; P56381; -.
DR PRIDE; P56381; -.
DR ProteomicsDB; 56917; -.
DR TopDownProteomics; P56381; -.
DR Antibodypedia; 29273; 154 antibodies from 21 providers.
DR DNASU; 514; -.
DR Ensembl; ENST00000243997.8; ENSP00000243997.3; ENSG00000124172.10.
DR Ensembl; ENST00000395659.1; ENSP00000379019.1; ENSG00000124172.10.
DR Ensembl; ENST00000395663.1; ENSP00000379023.1; ENSG00000124172.10.
DR GeneID; 514; -.
DR KEGG; hsa:514; -.
DR MANE-Select; ENST00000243997.8; ENSP00000243997.3; NM_006886.4; NP_008817.1.
DR UCSC; uc002yal.4; human.
DR CTD; 514; -.
DR DisGeNET; 514; -.
DR GeneCards; ATP5F1E; -.
DR HGNC; HGNC:838; ATP5F1E.
DR HPA; ENSG00000124172; Low tissue specificity.
DR MalaCards; ATP5F1E; -.
DR MIM; 606153; gene.
DR MIM; 614053; phenotype.
DR neXtProt; NX_P56381; -.
DR OpenTargets; ENSG00000124172; -.
DR Orphanet; 254913; Isolated ATP synthase deficiency.
DR PharmGKB; PA25128; -.
DR VEuPathDB; HostDB:ENSG00000124172; -.
DR eggNOG; KOG3495; Eukaryota.
DR GeneTree; ENSGT00390000015470; -.
DR HOGENOM; CLU_187039_4_0_1; -.
DR InParanoid; P56381; -.
DR OMA; HIRITKW; -.
DR OrthoDB; 1628103at2759; -.
DR PhylomeDB; P56381; -.
DR TreeFam; TF300278; -.
DR BioCyc; MetaCyc:HS04727-MON; -.
DR PathwayCommons; P56381; -.
DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; P56381; -.
DR BioGRID-ORCS; 514; 322 hits in 604 CRISPR screens.
DR GeneWiki; ATP5E; -.
DR GenomeRNAi; 514; -.
DR Pharos; P56381; Tbio.
DR PRO; PR:P56381; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; P56381; protein.
DR Bgee; ENSG00000124172; Expressed in renal medulla and 212 other tissues.
DR Genevisible; P56381; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
DR GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1); IMP:CACAO.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IC:ComplexPortal.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IDA:UniProtKB.
DR CDD; cd12153; F1-ATPase_epsilon; 1.
DR Gene3D; 1.10.1620.20; -; 1.
DR InterPro; IPR006721; ATP_synth_F1_esu_mt.
DR InterPro; IPR036742; ATP_synth_F1_esu_sf_mt.
DR PANTHER; PTHR12448; PTHR12448; 1.
DR Pfam; PF04627; ATP-synt_Eps; 1.
DR SUPFAM; SSF48690; SSF48690; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP synthesis; CF(1); Disease variant; Hydrogen ion transport;
KW Hydrolase; Ion transport; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Primary mitochondrial disease;
KW Reference proteome; Transport.
FT CHAIN 1..51
FT /note="ATP synthase subunit epsilon, mitochondrial"
FT /id="PRO_0000071662"
FT MOD_RES 21
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 21
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 32
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 32
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 37
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 37
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56382"
FT VARIANT 12
FT /note="Y -> C (in MC5DN3; dbSNP:rs387906929)"
FT /evidence="ECO:0000269|PubMed:20566710"
FT /id="VAR_066211"
SQ SEQUENCE 51 AA; 5780 MW; C3E8FDA7C9191CA4 CRC64;
MVAYWRQAGL SYIRYSQICA KAVRDALKTE FKANAEKTSG SNVKIVKVKK E
