A0A097IWC5 · A0A097IWC5_9ADEN

Function

function

Endosome lysis protein: Structural component of the virion that provides increased stability to the particle shell through its interaction with the core-capsid bridging protein and the hexon-linking protein VIII. Fibers shedding during virus entry into host cell allows the endosome lysis protein to be exposed as a membrane-lytic peptide. Exhibits pH-independent membrane fragmentation activity and probably mediates viral rapid escape from host endosome via organellar membrane lysis. It is not clear if it then remains partially associated with the capsid and involved in the intracellular microtubule-dependent transport of capsid to the nucleus, or if it is lost during endosomal penetration.
Pre-protein VI: During virus assembly, promotes hexon trimers nuclear import through nuclear pore complexes via an importin alpha/beta-dependent mechanism. By analogy to herpesviruses capsid assembly, might act as a chaperone to promote the formation of the icosahedral capsid.
Protease cofactor: Cofactor that activates the viral protease. Binds to viral protease in a 1:1 ratio.

Miscellaneous

All late proteins expressed from the major late promoter are produced by alternative splicing and alternative polyadenylation of the same gene giving rise to non-overlapping ORFs. A leader sequence is present in the N-terminus of all these mRNAs and is recognized by the viral shutoff protein to provide expression although conventional translation via ribosome scanning from the cap has been shut off in the host cell.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for site.

TypeIDPosition(s)Description
Site33-34Cleavage; by viral protease
Site222-223Cleavage; by viral protease

GO annotations

AspectTerm
Cellular Componenthost cell
Cellular Componenthost cell cytoplasm
Cellular Componenthost cell nucleus
Cellular Componentviral capsid
Cellular Componentviral procapsid
Biological Processlysis of host organelle involved in viral entry into host cell
Biological Processmicrotubule-dependent intracellular transport of viral material towards nucleus
Biological Processviral release from host cell

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Pre-protein VI
  • Short names
    pVI
  • Cleaved into 2 chains

Gene names

    • Name
      L3

Organism names

  • Taxonomic identifier
  • Strain
    • 23336
  • Taxonomic lineage
    Viruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus > Simian mastadenovirus H > simian adenovirus 54

Accessions

  • Primary accession
    A0A097IWC5

Proteomes

Subcellular Location

Pre-protein VI

Host nucleus
Host cytoplasm
Note: Shuttles between host cytoplasm and nucleus.

Endosome lysis protein

Virion
Note: Associates with the base of each peripentonal hexon on the capsid interior. Present in around 360 copies per virion.

Keywords

PTM/Processing

Features

Showing features for propeptide, chain, modified residue, disulfide bond.

TypeIDPosition(s)Description
PropeptidePRO_50118007351-33
ChainPRO_50232865671-234Pre-protein VI
Modified residue139Phosphothreonine; by host
ChainPRO_5023286569223-233Protease cofactor
Disulfide bond232Interchain (with Adenovirus protease)

Post-translational modification

Protease cofactor: Contains the major nuclear import and export signals. Proteolytically removed during virion maturation. The processing of the C-terminus turns the precursor into a mature viral structural protein and abrogates its ability to promote hexon import and act as a potential chaperone protein.
Ubiquitinated by Nedd4 following partial capsid disassembly; which might play a role in intracellular virus movement during entry.

Keywords

Expression

Induction

Expressed in the late phase of the viral replicative cycle.

Keywords

Interaction

Subunit

Endosome lysis protein

Interacts (via PPxY motif) with host NEDD4 ubiquitine ligase; this interaction might play a role in virus intracellular transport during entry. Part of a complex composed of the core-capsid bridging protein, the endosome lysis protein VI and the hexon-linking protein VIII; these interactions bridge the virus core to the capsid. Interacts with peripentonal hexons; this interaction stabilizes the capsid by gluing two peripentonal hexons together and joining them with an adjacent group-of-nine hexon.

Pre-protein VI

Interacts with hexon protein; this interaction allows nuclear import of hexon trimers and possibly pre-capsid assembly. Interacts (via C-terminal NLS) with importin alpha/beta.

Protease cofactor

Heterodimer with the viral protease; disulfide-linked. Interacts with the viral protease.

Family & Domains

Features

Showing features for region, motif, compositional bias.

TypeIDPosition(s)Description
Region34-54Amphipathic alpha-helix essential for membrane lytic activity
Region36-53Involved in endosomal membrane lysis
Region48-74Interaction with hexon protein
Motif67-76Nuclear export signal
Region105-145Disordered
Compositional bias106-145Basic and acidic residues
Motif144-147PPXY motif
Motif214-225Nuclear export signal
Region216-222Interaction with hexon protein
Region223-233Binds to importin alpha/beta, involved in hexon nuclear import
Motif228-231Nuclear localization signal

Domain

Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Minor capsid protein 6 contains one L domain: a PPXY motif which binds to the WW domains of HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4. In adenoviruses, this motif seems to play a role in microtubule-dependent intracellular trafficking toward the nucleus during virus entry into host cell and in suppression of DAXX-mediated repression of the immediate early E1A promoter.
N-terminal amphipathic alpha-helix domain is essential for the membrane lytic activity.

Sequence similarities

Belongs to the adenoviridae protein VI family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    234
  • Mass (Da)
    25,877
  • Last updated
    2015-01-07 v1
  • Checksum
    061AF2626982F6A6
MEDVNFSSLAPRHGTRPYLGTWNDIGTSQLNGGAFNWSSIWSGLKNFGSAVKTYGNRAWNSSTGQLLRDKLKEQNFQQKVVDGLAAGINGVVDIANQAVQREINNRLDPRPVEEKLPELEKEPQGEKRPRPDLEETLVTKTEEPPSYEEAVKNVPSVSLKPVTYPLTKPILSMATPVGDVPVTSVPIAPPVSRPAIRPVAVATPRYSRSNNWQSTLNSIVGLGVKTLKRRRCYY

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A097IWC4A0A097IWC4_9ADENL3936
A0A097IWB8A0A097IWB8_9ADENL3204

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias106-145Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KM190146
EMBL· GenBank· DDBJ
AIT70981.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp