A0A5J6AAY5 · A0A5J6AAY5_RUBV

Function

function

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.
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. 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.
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.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componenthost cell Golgi membrane
Cellular Componenthost cell mitochondrion
Cellular Componentmembrane
Cellular ComponentT=4 icosahedral viral capsid
Cellular Componentviral envelope
Cellular Componentviral nucleocapsid
Cellular Componentvirion membrane
Molecular Functionmetal ion binding
Molecular FunctionRNA binding
Biological Processclathrin-dependent endocytosis of virus by host cell
Biological Processfusion of virus membrane with host endosome membrane
Biological Processvirion attachment to host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Structural polyprotein
  • Alternative names
    • p110

Organism names

  • Taxonomic identifier
  • Strain
    • RVi/California.USA/43.16[1a]
  • Taxonomic lineage
    Viruses > Riboviria > Orthornavirae > Kitrinoviricota > Alsuviricetes > Hepelivirales > Matonaviridae > Rubivirus > Rubivirus rubellae

Accessions

  • Primary accession
    A0A5J6AAY5

Subcellular Location

Host Golgi apparatus membrane
; Single-pass type I membrane protein
Host cytoplasm
Host mitochondrion
Virion membrane
; Single-pass type I membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane1032-1056Helical

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Heterodimer with spike glycoprotein E1.
Heterodimer with spike glycoprotein E2.
Homodimer; further assembles into homooligomer. Interacts with human C1QBP. Interacts (via N-terminus) with protease/methyltransferase p150.

Family & Domains

Features

Showing features for compositional bias, region, domain.

Type
IDPosition(s)Description
Compositional bias1-15Polar residues
Region1-131Disordered
Compositional bias37-62Basic and acidic residues
Domain301-567Rubella membrane glycoprotein E2

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,063
  • Mass (Da)
    114,898
  • Last updated
    2019-12-11 v1
  • Checksum
    E074EED4F006E583
MASTTPITMEDLQKALETQSRALRAELAAGASQSRRPRPPRQRDSSTTGDDSGRDSGGPRRRRGNRGRGQGRDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACATSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGHWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDRAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPTLPLPPRAHRQHYGHHHRQLPFLGHDGHHGGTLRVGQHHRNASDVLPGHWLQGGWGCYNLSDWHQGTHVCHTKHMDFWCVEHDRPPPATPTPLTTAANSTTAATPATALAPCHAGLNDSCGGFLSGCGPMRLRHGTDIRCGRLICGLSTTAQYPPTRFGCAMRWGLPPWELVVLTARPDDGWTCRGVPAHPGTRCPELVSPMGRATCSPASALWLATANALSLDHALAAFALLVPWVLIFMVCRRACRRRGAAAALTAVVLQGYNPPAYGEEAFTYLCTAPGCATQAPVPVRLVGVRFESKIVDGGCFAPWDLEATGACICEIPTDVSCEGLGAWVPTAPCARIWNGTQRACTLWAINAYSSGGYAQLASYFNPGGSYYKQYHPTACEVEPAFGHSDAACWGFPTDTVMSVFALASYVQHPHKTVRVKFHTETRTVWQLSVAGVSCNVTTEHPFCNTPHGQLEVQVPPDPGDLVEYIMNHTGNQQSRWGLGSPNCHGPDWASPVCQRHSPDCSRVVGATPERPRLRLVDVDDPLLRTAPGPGEVWVTPVMGAQARKCGLHIRAGPYGHATVEMPEWIHAHTTSDPWHPPGPLGLKFKTVRPVALPRVLAPPRNVRVTGCYRCGTPALVEGLAPGGGNCHLTVNGEDVGAFPPGKFVTTALLNTPPPYQVSCGGESDRASARVIDPAAQSFTGVVYGTHTTAVSETRQTWAEWAAAHWWQLTLGAICALLLAGLLACCAKCLYYLRGAIAPR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Compositional bias37-62Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MK787188
EMBL· GenBank· DDBJ
QBZ96522.1
EMBL· GenBank· DDBJ
Genomic RNA

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