A0A3Q9HJK2 · A0A3Q9HJK2_9ADEN

  • Protein
    Pre-hexon-linking protein IIIa
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    3/5

Function

function

Structural component of the virion that acts as a cement protein on the capsid exterior which mediates the interactions between the hexons, including the peripentonal hexons, and reaches all the way to the penton vertices. Two hexon linking proteins IIIa, one from each facet, stabilize the unique edge interface between a pair of facets. As the virus enters the host cell, hexon linking proteins IIIa are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in the serotype specificity of the packaging of viral DNA via its interaction with packaging protein 3.

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.

Features

Showing features for site.

158550100150200250300350400450500550
TypeIDPosition(s)Description
Site570-571Cleavage; by viral protease

GO annotations

AspectTerm
Cellular Componenthost cell nucleus
Cellular Componentviral capsid, decoration

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Pre-hexon-linking protein IIIa
  • Alternative names
    • Capsid vertex-specific component IIIa
      (CVSC
      )
    • Protein IIIa
    • pIIIa
  • Cleaved into 1 chains

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • 10C2
  • Taxonomic lineage
    Viruses > Varidnaviria > Bamfordvirae > Preplasmiviricota > Tectiliviricetes > Rowavirales > Adenoviridae > Mastadenovirus

Accessions

  • Primary accession
    A0A3Q9HJK2

Proteomes

Subcellular Location

Virion
Host nucleus
Note: Surrounds the border of each facet on the capsid exterior. Present in around 60 copies per virion.

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, propeptide.

TypeIDPosition(s)Description
ChainPRO_50233966141-570Hexon-linking protein IIIa
ChainPRO_50233966151-585Pre-hexon-linking protein IIIa
Modified residue225Phosphoserine; by host
Modified residue274Phosphothreonine; by host
Modified residue310Phosphoserine; by host
Modified residue444Phosphoserine; by host
Modified residue449Phosphoserine; by host
Modified residue450Phosphoserine; by host
Modified residue452Phosphoserine; by host
Modified residue469Phosphoserine; by host
Modified residue473Phosphoserine; by host
Modified residue490Phosphotyrosine; by host
Modified residue494Phosphoserine; by host
Modified residue515Phosphoserine; by host
PropeptidePRO_5018798665571-585

Post-translational modification

Cleaved near the C-terminus by the viral protease during virion maturation to form the mature protein.

Keywords

Expression

Induction

Expressed in the late phase of the viral replicative cycle.

Keywords

Interaction

Subunit

Interacts with hexon proteins; this interaction tethers the peripentonal hexons to hexons situated in the facet. Interacts with the penton protein (via N-terminus). Interacts with packaging protein 3; this interaction is required to promote correct genome packaging.

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-24Disordered
Region1-106Peripentonal hexon-tethering domain
Compositional bias10-24Polar residues
Region138-251Binding to hexon-linking protein
Region439-483Disordered
Compositional bias466-481Polar residues
Compositional bias528-556Basic and acidic residues
Region528-570Disordered

Sequence similarities

Belongs to the adenoviridae hexon-linking protein IIIa family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    585
  • Mass (Da)
    65,298
  • Last updated
    2019-04-10 v1
  • Checksum
    0301022ACCB21F6E
MMQDATDPAVRAALQSQPSGLNSTDDWRQVMDRIMSLTARNPDAFRQQPQANRLSAILEAVVPARANPTHEKVLAIVNALAENRAIRPDEAGLVYDALLQRVARYNSGNVQTNLDRLVGDVREAVAQRERAQQQGNLGSMVALNAFLSTQPANVPRGQEDYTNFVSALRLMVTETPQSEVYQSGPDYFFQTSRQGLQTVNLSQAFKNLQGLWGVRAPTGDRATVSSLLTPNSRLLLLLIAPFTDSGSVSRDTYLGHLLTLYREAIGQAHVDEHTFQEITSVSRALGQEDTGSLEATLNYLLTNRRQKIPSLHSLNSEEERILRYVQQSVSLNLMRDGVTPSVALDMTARNMEPGMYASNRPFINRLMDYLHRAAAVNPEYFTNAILNPHWLPPPGFYTGGFEVPECNDGFLWDDIDDSVFSPQPQTLLELQQREQAQAALRKESFRRPSSLSDLGAAAPRSDASSPFPSLIGSLTSTRTTRPRLLGEEEYLNNSLLQPQREKNLPPAFPNNGIESLVDKMSRWKTYAQEHRDVPGPRPPTRRQRHDRQRGLVWEDDDSADDSSVLDLGGSGNPFAHLRPRLGRMF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias10-24Polar residues
Compositional bias466-481Polar residues
Compositional bias528-556Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MH121079
EMBL· GenBank· DDBJ
AZR66535.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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