ID ATPO_HUMAN Reviewed; 213 AA. AC P48047; B2R4E2; Q5U042; Q6IBI2; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 219. DE RecName: Full=ATP synthase subunit O, mitochondrial {ECO:0000305}; DE AltName: Full=ATP synthase peripheral stalk subunit OSCP {ECO:0000305}; DE AltName: Full=Oligomycin sensitivity conferral protein; DE Short=OSCP; DE Flags: Precursor; GN Name=ATP5PO {ECO:0000312|HGNC:HGNC:850}; Synonyms=ATP5O, ATPO; 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]. RC TISSUE=Brain, and Muscle; RX PubMed=7490082; DOI=10.1006/geno.1995.1176; RA Chen H.M., Morris M.A., Rossier C., Blouin J.-L., Antonarakis S.E.; RT "Cloning of the cDNA for the human ATP synthase OSCP subunit (ATP5O) by RT exon trapping and mapping to chromosome 21q22.1-q22.2."; RL Genomics 28:470-476(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98. 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-98. RC TISSUE=Heart; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. 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=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 [8] RP PROTEIN SEQUENCE OF 24-40. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-162; LYS-172 AND LYS-192, AND RP IDENTIFICATION BY MASS 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP ACETYLATION AT LYS-162, DEACETYLATION BY SIRT3, AND MUTAGENESIS OF LYS-162. RA Vassilopoulos A., Pennington D.J., Andresson T., Rees D., Fearnley I., RA Ham A., Yan Y., Flynn C.R., Jones K., Kim H.S., Deng C., Walker J., RA Gius D.; RT "SIRT3 deacetylates ATP synthase F1 complex proteins in response to RT nutrient and exercise-induced stress."; RL Antioxid. Redox Signal. 0:0-0(2013). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] 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 [14] RP INVOLVEMENT IN MC5DN7, AND VARIANT MC5DN7 12-GLN--VAL-213 DEL. RX PubMed=34954817; DOI=10.1002/ana.26293; RA Zech M., Kopajtich R., Steinbruecker K., Bris C., Gueguen N., RA Feichtinger R.G., Achleitner M.T., Duzkale N., Perivier M., Koch J., RA Engelhardt H., Freisinger P., Wagner M., Brunet T., Berutti R., Smirnov D., RA Navaratnarajah T., Rodenburg R.J.T., Pais L.S., Austin-Tse C., O'Leary M., RA Boesch S., Jech R., Bakhtiari S., Jin S.C., Wilbert F., Kruer M.C., RA Wortmann S.B., Eckenweiler M., Mayr J.A., Distelmaier F., Steinfeld R., RA Winkelmann J., Prokisch H.; RT "Variants in Mitochondrial ATP Synthase Cause Variable Neurologic RT Phenotypes."; RL Ann. Neurol. 91:225-237(2022). 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 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(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main CC subunits: a, b and c. Component of an ATP synthase complex composed of CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT- CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and CC ATP5MJ (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC P48047; PRO_0000000092 [P05067]: APP; NbExp=2; IntAct=EBI-355815, EBI-821758; CC P48047; P25705: ATP5F1A; NbExp=5; IntAct=EBI-355815, EBI-351437; CC P48047; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-355815, EBI-10171416; CC P48047; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-355815, EBI-739624; CC P48047; Q08379: GOLGA2; NbExp=3; IntAct=EBI-355815, EBI-618309; CC P48047; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-355815, EBI-2549423; CC P48047; P42858: HTT; NbExp=6; IntAct=EBI-355815, EBI-466029; CC P48047; A1A4E9: KRT13; NbExp=3; IntAct=EBI-355815, EBI-10171552; CC P48047; P19012: KRT15; NbExp=3; IntAct=EBI-355815, EBI-739566; CC P48047; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-355815, EBI-2548751; CC P48047; O14777: NDC80; NbExp=3; IntAct=EBI-355815, EBI-715849; CC P48047; P49902: NT5C2; NbExp=3; IntAct=EBI-355815, EBI-742084; CC P48047; Q8ND90: PNMA1; NbExp=4; IntAct=EBI-355815, EBI-302345; CC P48047; Q08752: PPID; NbExp=3; IntAct=EBI-355815, EBI-716596; CC P48047; Q9BXU3: TEX13A; NbExp=3; IntAct=EBI-355815, EBI-10301068; CC P48047; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-355815, EBI-1105213; CC P48047; Q15654: TRIP6; NbExp=3; IntAct=EBI-355815, EBI-742327; CC P48047; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-355815, EBI-739895; CC P48047; O43829: ZBTB14; NbExp=3; IntAct=EBI-355815, EBI-10176632; CC P48047; P36508: ZNF76; NbExp=3; IntAct=EBI-355815, EBI-7254550; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner CC membrane {ECO:0000250}. CC -!- PTM: Acetylation at Lys-162 decreases ATP production. Deacetylated by CC SIRT3. {ECO:0000269|Ref.11}. CC -!- DISEASE: Mitochondrial complex V deficiency, nuclear type 7 (MC5DN7) CC [MIM:620359]: An autosomal recessive, severe, mitochondrial disorder CC apparent soon after birth. It is characterized by multisystemic CC features that include hypotonia, developmental delay, progressive CC epileptic encephalopathy, progressive cerebral atrophy, white matter CC abnormalities on brain imaging, and hypertrophic cardiomyopathy in some CC patients. Death in infancy or early childhood may occur. CC {ECO:0000269|PubMed:34954817}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ATPase delta chain 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; X83218; CAA58219.1; -; mRNA. DR EMBL; BT019836; AAV38639.1; -; mRNA. DR EMBL; CR456822; CAG33103.1; -; mRNA. DR EMBL; AK222962; BAD96682.1; -; mRNA. DR EMBL; AK311796; BAG34739.1; -; mRNA. DR EMBL; CH471079; EAX09802.1; -; Genomic_DNA. DR EMBL; BC021233; AAH21233.1; -; mRNA. DR EMBL; BC022865; AAH22865.1; -; mRNA. DR CCDS; CCDS13634.1; -. DR RefSeq; NP_001688.1; NM_001697.2. DR PDB; 8H9E; EM; 2.53 A; O=24-213. DR PDB; 8H9I; EM; 2.77 A; O=24-213. DR PDB; 8H9L; EM; 2.61 A; O=24-213. DR PDB; 8H9P; EM; 3.02 A; O=24-213. DR PDB; 8H9S; EM; 2.53 A; O=24-213. DR PDB; 8H9T; EM; 2.77 A; O=24-213. DR PDB; 8H9U; EM; 2.61 A; O=24-213. DR PDB; 8H9V; EM; 3.02 A; O=24-213. DR PDBsum; 8H9E; -. DR PDBsum; 8H9I; -. DR PDBsum; 8H9L; -. DR PDBsum; 8H9P; -. DR PDBsum; 8H9S; -. DR PDBsum; 8H9T; -. DR PDBsum; 8H9U; -. DR PDBsum; 8H9V; -. DR AlphaFoldDB; P48047; -. DR EMDB; EMD-34564; -. DR EMDB; EMD-34568; -. DR EMDB; EMD-34572; -. DR EMDB; EMD-34576; -. DR EMDB; EMD-34580; -. DR EMDB; EMD-34581; -. DR EMDB; EMD-34582; -. DR EMDB; EMD-34583; -. DR SMR; P48047; -. DR BioGRID; 107021; 325. DR ComplexPortal; CPX-6151; Mitochondrial proton-transporting ATP synthase complex. DR CORUM; P48047; -. DR IntAct; P48047; 143. DR MINT; P48047; -. DR STRING; 9606.ENSP00000290299; -. DR DrugBank; DB11638; Artenimol. DR TCDB; 3.A.2.1.15; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily. DR GlyGen; P48047; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P48047; -. DR MetOSite; P48047; -. DR PhosphoSitePlus; P48047; -. DR SwissPalm; P48047; -. DR BioMuta; ATP5O; -. DR DMDM; 1352049; -. DR OGP; P48047; -. DR EPD; P48047; -. DR jPOST; P48047; -. DR MassIVE; P48047; -. DR MaxQB; P48047; -. DR PaxDb; 9606-ENSP00000290299; -. DR PeptideAtlas; P48047; -. DR ProteomicsDB; 55837; -. DR Pumba; P48047; -. DR TopDownProteomics; P48047; -. DR Antibodypedia; 35000; 248 antibodies from 31 providers. DR DNASU; 539; -. DR Ensembl; ENST00000290299.7; ENSP00000290299.2; ENSG00000241837.7. DR GeneID; 539; -. DR KEGG; hsa:539; -. DR MANE-Select; ENST00000290299.7; ENSP00000290299.2; NM_001697.3; NP_001688.1. DR UCSC; uc002ytl.4; human. DR AGR; HGNC:850; -. DR CTD; 539; -. DR DisGeNET; 539; -. DR GeneCards; ATP5PO; -. DR HGNC; HGNC:850; ATP5PO. DR HPA; ENSG00000241837; Tissue enhanced (tongue). DR MalaCards; ATP5PO; -. DR MIM; 600828; gene. DR MIM; 620359; phenotype. DR neXtProt; NX_P48047; -. DR OpenTargets; ENSG00000241837; -. DR PharmGKB; PA25144; -. DR VEuPathDB; HostDB:ENSG00000241837; -. DR eggNOG; KOG1662; Eukaryota. DR GeneTree; ENSGT00390000015060; -. DR HOGENOM; CLU_085114_0_0_1; -. DR InParanoid; P48047; -. DR OMA; YSIEGLY; -. DR OrthoDB; 312519at2759; -. DR PhylomeDB; P48047; -. DR TreeFam; TF106241; -. DR BioCyc; MetaCyc:HS08368-MONOMER; -. DR PathwayCommons; P48047; -. DR Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-HSA-8949613; Cristae formation. DR SignaLink; P48047; -. DR SIGNOR; P48047; -. DR BioGRID-ORCS; 539; 364 hits in 1129 CRISPR screens. DR ChiTaRS; ATP5PO; human. DR GeneWiki; ATP5O; -. DR GenomeRNAi; 539; -. DR Pharos; P48047; Tbio. DR PRO; PR:P48047; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P48047; Protein. DR Bgee; ENSG00000241837; Expressed in heart left ventricle and 104 other cell types or tissues. DR ExpressionAtlas; P48047; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB. 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:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0006754; P:ATP biosynthetic process; NAS:UniProtKB. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; NAS:ComplexPortal. DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IMP:UniProtKB. DR GO; GO:1902600; P:proton transmembrane transport; NAS:UniProtKB. DR Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1. DR HAMAP; MF_01416; ATP_synth_delta_bact; 1. DR InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf. DR InterPro; IPR020781; ATPase_OSCP/d_CS. DR InterPro; IPR000711; ATPase_OSCP/dsu. DR NCBIfam; TIGR01145; ATP_synt_delta; 1. DR PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1. DR PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1. DR Pfam; PF00213; OSCP; 1. DR PRINTS; PR00125; ATPASEDELTA. DR SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1. DR PROSITE; PS00389; ATPASE_DELTA; 1. DR UCD-2DPAGE; P48047; -. DR Genevisible; P48047; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ATP synthesis; Direct protein sequencing; KW Disease variant; Hydrogen ion transport; Ion transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Primary mitochondrial disease; KW Reference proteome; Transit peptide; Transport. FT TRANSIT 1..23 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 24..213 FT /note="ATP synthase subunit O, mitochondrial" FT /id="PRO_0000002646" FT MOD_RES 54 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 60 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 70 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 73 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 90 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 158 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 158 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 162 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|Ref.11, ECO:0007744|PubMed:19608861" FT MOD_RES 162 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 172 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 176 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT MOD_RES 192 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 199 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DB20" FT VARIANT 12..213 FT /note="Missing (in MC5DN7)" FT /evidence="ECO:0000269|PubMed:34954817" FT /id="VAR_088523" FT VARIANT 98 FT /note="K -> R (in dbSNP:rs4842)" FT /evidence="ECO:0000269|Ref.2, ECO:0000269|Ref.5" FT /id="VAR_011930" FT MUTAGEN 162 FT /note="K->R: Increased ATP levels." FT /evidence="ECO:0000269|Ref.11" FT HELIX 36..50 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 55..68 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 72..77 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 85..97 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 103..113 FT /evidence="ECO:0007829|PDB:8H9V" FT TURN 114..116 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 121..135 FT /evidence="ECO:0007829|PDB:8H9V" FT STRAND 138..147 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 151..163 FT /evidence="ECO:0007829|PDB:8H9V" FT STRAND 170..173 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 179..181 FT /evidence="ECO:0007829|PDB:8H9V" FT STRAND 183..189 FT /evidence="ECO:0007829|PDB:8H9V" FT STRAND 192..195 FT /evidence="ECO:0007829|PDB:8H9V" FT HELIX 198..209 FT /evidence="ECO:0007829|PDB:8H9V" SQ SEQUENCE 213 AA; 23277 MW; 311F53576A31FC93 CRC64; MAAPAVSGLS RQVRCFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KQNKLEQVEK ELLRVAQILK EPKVAASVLN PYVKRSIKVK SLNDITAKER FSPLTTNLIN LLAENGRLSN TQGVVSAFST MMSVHRGEVP CTVTSASPLE EATLSELKTV LKSFLSQGQV LKLEAKTDPS ILGGMIVRIG EKYVDMSVKT KIQKLGRAMR EIV //