♦Structural polyprotein (p110) [Cleaved into: Capsid protein (Coat protein) (C)
♦ Spike glycoprotein E2 (E2 envelope glycoprotein)
♦ Spike glycoprotein E1 (E1 envelope glycoprotein)]

NC_001545.2 ;  M15240.2 

MASTTPITMEDLQKALEAQSRALRAELAAGASQPRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQRKDWSRAPPPPEERQEGRSQTPAPKPSRAP
PQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPE
PPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARA
GLQPRVDMAAPPTPPQPPRAHGQHYGHHHHQLPFLGHDGHHGGTLRVGQHHRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPA
TPTPLTTAANSITAATPATAPAPCHAGLNDSCGGFLSGCGPMRLRHGADTRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPEDGWTCRGVP
AHPGTRCPELVSPMGRATCSPASALWLATANALSLDHALAAFVLLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQTP
VPVRLAGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTFWAVNAYSSGGYAQLASYFNPGGSYYKQYHPTACE
VEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCDVTTEHPFCNTPHGQLEVQVPPDPGDMVEYIMNYTGNQQSRW
GLGSPNCHGPDWASPVCQRHSPDCSRLVGATPERPRLRLVDADDPLLRTAPGPGEVWVTPVIGSQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHP
PGPLGLKFKTVRPVTLPRALAPPRNVRVTGCYQCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTAALLNTPPPYQVSCGGESDRASARVIDPAAQ
SFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALPLAGLLACCAKCLYYLRGAIAPR

♦Capsid protein: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions. 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, but this interaction seems not to be important for its biological function. 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.
♦ 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.
♦ Spike glycoprotein E1: Class II viral fusion protein. 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. This E1 homotrimer is fusion active, and promotes release of viral nucleocapsid in cytoplasm after endosome and viral membrane fusion (By similarity). E1 cytoplasmic tail modulates virus release, and the tyrosines residues are critical for this function.

♦ Capsid protein: Virion . Host cytoplasm . Host mitochondrion . Note=The capsid protein is concentrated around Golgi region. .
♦ Spike glycoprotein E2: Virion membrane
♦ Single-pass type I membrane protein . Host Golgi apparatus membrane
♦ Single-pass type I membrane protein . 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 (By similarity). .
♦ Spike glycoprotein E1: Virion membrane
♦ Single-pass type I membrane protein . Host Golgi apparatus membrane
♦ Single-pass type I membrane protein . 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 (By similarity). .

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