| Description | The membrane (M) protein is the most abundant structural protein and defines the shape of the viral envelope. It is also regarded as the central organiser of coronavirus assembly, interacting with all other major coronaviral structural proteins. M proteins play a critical role in protein-protein interactions (as well as protein-RNA interactions) since virus-like particle (VLP) formation in many CoVs requires only the M and envelope (E) proteins for efficient virion assembly [ ]. Interaction of spike (S) with M is necessary for retention of S in the ER-Golgi intermediate compartment (ERGIC)/Golgi complex and its incorporation into new virions, but dispensable for the assembly process. Binding of M to nucleocapsid (N) proteins stabilises the nucleocapsid (N protein-RNA complex), as well as the internal core of virions, and, ultimately, promotes completion of viral assembly. Together, M and E protein make up the viral envelope and their interaction is sufficient for the production and release of virus-like particles (VLPs) [, , ].This entry contains the Membrane (M) protein of Severe acute respiratory syndrome coronavirus (SARS-CoV), SARS-CoV-2 (also known as 2019 novel CoV (2019-nCoV) or COVID-19 virus), and related proteins from betacoronaviruses in the sarbecovirus subgenera (B lineage). M protein from SARS-CoV-2 has high sequence identity to its SARS-CoV homologue and is predicted to have a small glycosylated amino-terminal ectodomain, a triple-membrane spanning domain, and a carboxyl-terminal endodomain. The C-terminal portion of coronaviral M proteins binds to the N protein within the cell membrane of the ER or Golgi complex, stabilizing the nucleocapsid and the core of the virion [ ]. | Name | M matrix/glycoprotein, SARS-CoV-like |
| Short Name | M_SARS-like-CoV | Type | Family |
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