PROSITE documentation PDOC52083Major vault protein (MVP) shoulder domain profile
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PURL: https://purl.expasy.org/prosite/documentation/PDOC52083
The vault is the biggest ribonucleoprotein organelle present in many eukaryotic cells, three times the size of a ribosome. Vaults have been identified in a wide variety of species, including mammals, birds, fish, echinoids and slime molds. Although several functions have been proposed for vaults since their discovery in 1986, including roles in multidrug resistance, cell signaling, and innate immunity, their cellular function remains unclear. Most vault particles are present in the cytoplasm, but a few of them localize to the nucleus. Mammalian vaults are composed of major vault protein (MVP), telomerase-associated protein 1 (TEP1), vault poly(ADP-ribose) polymerase (VPARP) and vault RNA vRNA. MVP is the main constituent of the vault organelle and is sufficient to give the vault its hollow barrel-like shape [1,2,3,4].
Each MVP monomer folds into 12 domains: nine structural repeat domains (see <PDOC51224>), a shoulder domain, a cap-helix domain and a cap-ring domain [1,2].
The MVP shoulder domain folds into a single α/β globular domain with a four-stranded antiparallel β sheet on one side and four α helices on the other side (see <PDB:2QZV>). The shoulder domain is structurally similar to the core domain of stomatin from Pyrococcus horikoshii (PhStoCD) and the flotillin-2 band-7 domain (FlotBD7). The core domain of stomatin is evolutionarily conserved and falls within the stomatin-prohibitin-flotillin-HflK-C (SPFH) domain family. The SPFH domain is known to be involved in lipid raft association. The structural similarities between the shoulder domain and SPFH domain family supports an interaction between MVP and lipid rafts-for example, when human lung epithelial cells are infected with Pseudomonas aeruginosa [1,2,4].
The profile we developed covers the entire MVP shoulder domain.
Last update:November 2025 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Tanaka H. Kato K. Yamashita E. Sumizawa T. Zhou Y. Yao M. Iwasaki K. Yoshimura M. Tsukihara T. |
| Title | The structure of rat liver vault at 3.5 angstrom resolution. | |
| Source | Science 323:384-388(2009). | |
| PubMed ID | 19150846 | |
| DOI | 10.1126/science.1164975 |
| 2 | Authors | Tanaka H. Tsukihara T. |
| Title | Structural studies of large nucleoprotein particles, vaults. | |
| Source | Proc. Jpn. Acad. Ser. B. Phys. Biol. Sci. 88:416-433(2012). | |
| PubMed ID | 23060231 | |
| DOI | 10.2183/pjab.88.416 |
| 3 | Authors | Kretz P.F. Wagner C. Mikhaleva A. Montillot C. Hugel S. Morella I. Kannan M. Fischer M.-C. Milhau M. Yalcin I. Brambilla R. Selloum M. Herault Y. Reymond A. Collins S.C. Yalcin B. |
| Title | Dissecting the autism-associated 16p11.2 locus identifies multiple drivers in neuroanatomical phenotypes and unveils a male-specific role for the major vault protein. | |
| Source | Genome Biol 24:261-261(2023). | |
| PubMed ID | 37968726 | |
| DOI | 10.1186/s13059-023-03092-8 |
| 4 | Authors | Loevestam S. Scheres S.H.W. |
| Title | Cryo-EM structure of the vault from human brain reveals symmetry mismatch at its caps. | |
| Source | Structure 33:1643-1648.e1(2025). | |
| PubMed ID | 40803316 | |
| DOI | 10.1016/j.str.2025.07.014 |
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