| IED ID | IndEnz0002013045 |
| Enzyme Type ID | protease013045 |
| Protein Name |
Structural polyprotein p110 Cleaved into: Capsid protein Coat protein C ; Spike glycoprotein E2 E2 envelope glycoprotein ; Spike glycoprotein E1 E1 envelope glycoprotein |
| Gene Name | |
| Organism | Rubella virus (strain Therien) (RUBV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Alsuviricetes Hepelivirales Matonaviridae Rubivirus Rubivirus rubellae Rubella virus (RUBV) Rubella virus (strain Therien) (RUBV) |
| Enzyme Sequence | MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRRDWSRAPPPPEERQETRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLATVAVGTARAGLQPRADMAAPPTLPQPPCAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHYRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVPAHPGARCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPAAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNYTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRTLAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDLGAVPPGKFVTAALLNTPPPYQVSCGGESDRATARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR |
| Enzyme Length | 1063 |
| Uniprot Accession Number | P07566 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes. Phosphorylation negatively regulates RNA-binding activity, possibly delaying virion assembly during the viral replication phase. Capsid protein dimerizes and becomes disulfide-linked in the virion. Modulates genomic RNA replication. Modulates subgenomic RNA synthesis by interacting with human C1QBP/SF2P32. Induces both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of rubella virus infected cells. Induces apoptosis when expressed in transfected cells. {ECO:0000250|UniProtKB:P08563}.; FUNCTION: [Spike glycoprotein E2]: Responsible for viral attachment to target host cell, by binding to the cell receptor. Its transport to the plasma membrane depends on interaction with E1 protein. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement. {ECO:0000250|UniProtKB:P08563}.; FUNCTION: [Spike glycoprotein E1]: Class II viral fusion protein (By similarity). Fusion activity is inactive as long as E1 is bound to E2 in mature virion. After virus attachment to target cell and clathrin-mediated endocytosis, acidification of the endosome would induce dissociation of E1/E2 heterodimer and concomitant trimerization of the E1 subunits (PubMed:15557740). This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion. The cytoplasmic tail of spike glycoprotein E1 modulates virus release. The surface glycoproteins display an irregular helical organization and a pseudo-tetrameric inner nucleocapsid arrangement (By similarity). {ECO:0000250|UniProtKB:P08563, ECO:0000269|PubMed:15557740}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (3); Compositional bias (1); Disulfide bond (9); Glycosylation (9); Metal binding (4); Modified residue (1); Natural variant (10); Region (4); Site (2); Topological domain (4); Transmembrane (2) |
| Keywords | 3D-structure;Calcium;Capsid protein;Clathrin-mediated endocytosis of virus by host;Disulfide bond;Fusion of virus membrane with host endosomal membrane;Fusion of virus membrane with host membrane;Glycoprotein;Host Golgi apparatus;Host cytoplasm;Host membrane;Host mitochondrion;Host-virus interaction;Lipoprotein;Membrane;Metal-binding;Palmitate;Phosphoprotein;RNA-binding;Reference proteome;T=4 icosahedral capsid protein;Transmembrane;Transmembrane helix;Viral attachment to host cell;Viral envelope protein;Viral penetration into host cytoplasm;Virion;Virus endocytosis by host;Virus entry into host cell |
| Interact With | Q07021; Q9MZE0 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion {ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is concentrated around Golgi region (By similarity). In the virion, it is probably associated to the viral membrane (By similarity). {ECO:0000250|UniProtKB:P08563}.; SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. {ECO:0000250|UniProtKB:P08563}.; SUBCELLULAR LOCATION: [Spike glycoprotein E1]: Virion membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Host Golgi apparatus membrane {ECO:0000250|UniProtKB:P08563}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P08563}. Note=E1 and E2 form heterodimer in the endoplasmic reticulum before they are transported to and retained in the Golgi complex, where virus assembly occurs. E1 possesses an endoplasmic reticulum retention signal, and unassembled E2 and E1 subunits are retained in the endoplasmic reticulum. Presumably, assembly of E2 and E1 would mask the signal, thereby allowing transport of the heterodimer to the Golgi complex. {ECO:0000250|UniProtKB:P08563}. |
| Modified Residue | MOD_RES 46; /note=Phosphoserine; by host; /evidence=ECO:0000250|UniProtKB:P08563 |
| Post Translational Modification | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidase. Another signal peptide at E2 C-terminus directs E1 to the ER, with a similar mechanism. {ECO:0000250|UniProtKB:P08563}.; PTM: [Spike glycoprotein E1]: Contains three N-linked oligosaccharides. {ECO:0000250|UniProtKB:P08563}.; PTM: Capsid is phosphorylated on Ser-46 by host. This phosphorylation negatively regulates capsid protein RNA-binding activity (By similarity). Dephosphorylated by human PP1A (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P08563}. |
| Signal Peptide | |
| Structure 3D | Electron microscopy (2) |
| Cross Reference PDB | 5KHE; 5KHF; |
| Mapped Pubmed ID | 28575072; |
| Motif | |
| Gene Encoded By | |
| Mass | 114,679 |
| Kinetics | |
| Metal Binding | METAL 670; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P08563; METAL 671; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08563; METAL 718; /note=Calcium; /evidence=ECO:0000250|UniProtKB:P08563; METAL 719; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P08563 |
| Rhea ID | |
| Cross Reference Brenda |