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Primary Information | |
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| BoMiProt ID | Bomi10543 |
| Protein Name | V-type proton ATPase subunit C 1/Vacuolar proton pump subunit C 1 |
| Organism | Bos taurus |
| Uniprot ID | P21282 |
| Milk Fraction | Exosomes |
| Ref Sequence ID | NP_788849.1 |
| Aminoacid Length | 382 |
| Molecular Weight | 43986 |
| FASTA Sequence | Download |
| Gene Name | ATP6V1C1 |
| Gene ID | 338089 |
| Protein Existence Status | Reviewed |
Secondary Information | |
| Presence in other biological fluids/tissue/cells | occipital lobe |
| Protein Function | Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons.Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity |
| Biochemical Properties | Mammalian V-ATPase is a rotary machine made up of two domains: the ATP-hydrolytic V1 domain and the proton-translocation Vo domain. The V1 domain consists of three catalytic AB heterodimers that form a heterohexamer with threefold rotational pseudosymmetry, three peripheral stalks each consisting of the subunits EG, one central rotor including subunits D and F, and the regulatory subunits C and H.The composition of the mammalian V1 domain is similar to that of the yeast domain, which is a well-characterized model for V-ATPase studies. The c-ring of yeast’s Vo domain contains eight subunit c, one subunit c’, and one subunit c”. |
| PTMs | N-acetylation at Thr |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | na |
| SCOP | Class : Alpha and beta proteins (a+b) Fold : Vacuolar ATP synthase subunit C Superfamily : Vacuolar ATP synthase subunit C Family : Vacuolar ATP synthase subunit C Domain Name : 6XBW G:2-379 |
| CATH | Matched CATH superfamily n/a |
| Predicted Disorder Regions | NA |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| PDB ID | 6XBW, 6XBY, 7KHR, |
| Bibliography | 1.Wang R, Long T, Hassan A, Wang J, Sun Y, Xie XS, Li X. Cryo-EM structures of intact V-ATPase from bovine brain. Nat Commun. 2020 Aug 6;11(1):3921. doi: 10.1038/s41467-020-17762-9. PMID: 32764564; PMCID: PMC7414150. 2.Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase.Zhao J, Benlekbir S, Rubinstein JL.Nature. 2015 May 14; 521(7551):241-5. 3. |