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Protein

Pre-hexon-linking protein VIII

Gene

L4

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hexon-linking protein-N: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together.1 Publication
Hexon-linking protein-C: Structural component of the virion that acts as a cement protein on the capsid interior and which glue the peripentonal hexons and group-of-nine hexons together.1 Publication

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-hexon-linking protein VIII
Alternative name(s):
Pre-protein VIII
Short name:
pVIII
Cleaved into the following 2 chains:
Alternative name(s):
12.1 kDa protein VIII
Protein VIII-N
Alternative name(s):
7.6 kDa protein VIII
Protein VIII-C
Gene namesi
ORF Names:L4
OrganismiHuman adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Taxonomic identifieri28285 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeMastadenovirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Proteomesi
  • UP000004992 Componenti: Genome

Subcellular locationi

Hexon-linking protein-N :
  • Virion 1 Publication

  • Note: Located on the inner side of the capsid shell. Present in 120 copies per virion.1 Publication
Hexon-linking protein-C :
  • Virion 1 Publication

  • Note: Located on the inner side of the capsid shell. Present in 120 copies per virion.1 Publication

GO - Cellular componenti

  • host cell nucleus Source: UniProtKB-SubCell
  • viral capsid Source: UniProtKB-KW
  • virion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Host nucleus, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Pre-hexon-linking protein VIIIPRO_0000421131Add
BLAST
Peptidei1 – 111111Hexon-linking protein-NSequence analysisPRO_0000036495Add
BLAST
Propeptidei112 – 15746Sequence analysisPRO_0000421132Add
BLAST
Peptidei158 – 22770Hexon-linking protein-CSequence analysisPRO_0000036496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphothreonine; by hostBy similarity
Modified residuei118 – 1181Phosphoserine; by hostBy similarity
Modified residuei174 – 1741Phosphoserine; by hostBy similarity

Post-translational modificationi

Cleaved by the viral protease during virion maturation. May cause the middle segment to be shed from the capsid.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei111 – 1122Cleavage; by viral proteaseSequence analysis
Sitei131 – 1322Cleavage; by viral proteaseSequence analysis
Sitei157 – 1582Cleavage; by viral proteaseSequence analysis

Keywords - PTMi

Phosphoprotein

Expressioni

Inductioni

Expressed in the late phase of the viral replicative cycle.

Keywords - Developmental stagei

Late protein

Interactioni

Subunit structurei

Interacts with the peripentonal hexons as well as the hexons in the facets (PubMed:20798312, PubMed:25071205). 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 (PubMed:25071205).2 Publications

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 434Combined sources
Helixi45 – 473Combined sources
Helixi51 – 577Combined sources
Beta strandi58 – 614Combined sources
Beta strandi67 – 704Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-O/P1-227[»]
4CWUX-ray3.80X/Y1-227[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24936.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR000646. Adeno_PVIII.
[Graphical view]
PfamiPF01310. Adeno_PVIII. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24936-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKEIPTPYM WSYQPQMGLA AGAAQDYSTR INYMSAGPHM ISRVNGIRAH
60 70 80 90 100
RNRILLEQAA ITTTPRNNLN PRSWPAALVY QESPAPTTVV LPRDAQAEVQ
110 120 130 140 150
MTNSGAQLAG GFRHRVRSPG QGITHLTIRG RGIQLNDESV SSSLGLRPDG
160 170 180 190 200
TFQIGGAGRP SFTPRQAILT LQTSSSEPRS GGIGTLQFIE EFVPSVYFNP
210 220
FSGPPGHYPD QFIPNFDAVK DSADGYD
Length:227
Mass (Da):24,687
Last modified:March 1, 1992 - v1
Checksum:iC1CACF31E6F5E5D5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti160 – 1601P → S no nucleotide entry (PubMed:23142869).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. Translation: AAA96413.1.
PIRiE39449. SXAD85.
RefSeqiAP_000217.1. AC_000008.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M73260 Genomic DNA. Translation: AAA96413.1.
PIRiE39449. SXAD85.
RefSeqiAP_000217.1. AC_000008.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYNelectron microscopy-O/P1-227[»]
4CWUX-ray3.80X/Y1-227[»]
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP24936.

Family and domain databases

InterProiIPR000646. Adeno_PVIII.
[Graphical view]
PfamiPF01310. Adeno_PVIII. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAP8_ADE05
AccessioniPrimary (citable) accession number: P24936
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: July 6, 2016
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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 (By similarity).By similarity

Caution

An interaction between hexon-linking protein IIIa and hexon-linking protein VIII as been described in PubMed:20798312. However, the subcellular location of hexon-linking protein IIIa was incorrectly assigned to the capsid interior.Curated

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.