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Primary Information | |
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| BoMiProt ID | Bomi4140 |
| Protein Name | ATP synthase subunit delta, mitochondrial/ATP synthase F1 subunit delta/F-ATPase delta subunit |
| Organism | Bos taurus |
| Uniprot ID | P05630 |
| Milk Fraction | Whey |
| Ref Sequence ID | NP_788843.1 |
| Aminoacid Length | 168 |
| Molecular Weight | 17612 |
| FASTA Sequence | Download |
| Gene Name | ATP5F1D |
| Gene ID | 338081 |
| Protein Existence Status | Reviewed |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | laryngeal cartilage |
| Protein Function | F1Fo-ATP synthase δ subunit is required for lethal C. albicans infection. |
| Biochemical Properties | F1Fo-ATP synthase consists of two major domains, a globular F1 catalytic domain (the α3β3 domain) and a membrane-bound Fo proton-translocating domain (the ab2c8-12 domain), which are linked by a central stalk containing the γ, ε and δ subunits. The δ and ε subunits interact with a Rossmann fold in the γ subunit, forming a foot that interacts with the c-ring and couples the transmembrane proton motive force to catalyse in the α3β3 domain, in which the δ subunit plays a key role in the mechanical coupling of the F1 domain to the Fo domain. |
| PTMs | N6-acetylation at Lysine |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | na |
| SCOP | Class : All alpha proteins Fold : Long alpha-hairpin Superfamily : Epsilon subunit of F1F0-ATP synthase C-terminal domain Family : Epsilon subunit of F1F0-ATP synthase C-terminal domain Domain Name : 2V7Q H:102-145 |
| CATH | Matched CATH superfamily 1.20.5.440 3.10.450.640 2.60.15.10 |
| Predicted Disorder Regions | (1-28) |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| PDB ID | 1E79, 1H8E, 2CK3, 2JDI, 2V7Q, 2W6H, 2W6I, 2W6J, 2WSS, 2XND, 4ASU, 4YXW, 5ARA, 5ARE, 5ARH, 5ARI, 5FIJ,5FIK, 5FIL, 6YY0, 6Z1R, 6Z1U, 6ZG7, 6ZG8, 6ZIK, 6ZPO, 6ZQM, 6ZQN, 7AJB, 7AJC, 7AJD, 7AJE, 7AJF, 7AJG, 7AJH, 7AJI, 7AJJ, |
| Bibliography | 1.Li S, Zhao Y, Zhang Y, Zhang Y, Zhang Z, Tang C, Weng L, Chen X, Zhang G, Zhang H. The δ subunit of F1Fo-ATP synthase is required for pathogenicity of Candida albicans. Nat Commun. 2021 Oct 15;12(1):6041. doi: 10.1038/s41467-021-26313-9. PMID: 34654833; PMCID: PMC8519961. 2. Song J, Pfanner N, Becker T. Assembling the mitochondrial ATP synthase. Proc. Natl Acad. Sci. USA. 2018;115:2850–2852. doi: 10.1073/pnas.1801697115. 3.Duvezin-Caubet S, Caron M, Giraud MF, Velours J, di Rago JP. The two rotor components of yeast mitochondrial ATP synthase are mechanically coupled by subunit delta. Proc. Natl Acad. Sci. USA. 2003;100:13235–13240. doi: 10.1073/pnas.2135169100. 4.Gibbons C, Montgomery MG, Leslie AG, Walker JE. The structure of the central stalk in bovine F(1)-ATPase at 2.4 A resolution. Nat. Struct. Biol. 2000;7:1055–1061. doi: 10.1038/80981. 5.Fillingame RH. Getting to the bottom of the F1-ATPase. Nat. Struct. Biol. 2000;7:1002–1004. doi: 10.1038/80902. 6.Duvezin-Caubet S, et al. A “petite obligate” mutant of Saccharomyces cerevisiae: functional mtDNA is lethal in cells lacking the delta subunit of mitochondrial F1-ATPase. J. Biol. Chem. 2006;281:16305–16313. doi: 10.1074/jbc.M513805200. |