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Protein

Pre-hexon-linking protein

Gene

L4

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hexon-linking protein: Structural component of the virion that lashes peripentonal hexons to the hexons situated in the facets thanks to its interaction with the capsid vertex protein. Also binds together hexons of different facets.1 Publication

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

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-hexon-linking protein
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]
ProteomesiUP000004992: Genome

Subcellular locationi

Peptide Hexon-linking protein-N : Virion
Note: Located on the inner side of the capsid shell. Present in around 120 copies per virion.
Peptide Hexon-linking protein-C : Virion
Note: Located on the inner side of the capsid shell. Present in around 120 copies per virion.

GO - Cellular componenti

  1. host cell nucleus Source: UniProtKB-SubCell
  2. viral capsid Source: UniProtKB-KW
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 proteinPRO_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 causing the middle segment to be shed from the capsid.Curated

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 capsid vertex protein; this interaction allows tethering of the hexons surrounding the penton base to those situated in the central plate of the facet. Interacts with hexon protein; this interaction lashes hexons together, each copy of hexon-linking protein being bound to 4 hexon trimers.1 Publication

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-ray3.50R/S/X/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-ray3.50R/S/X/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...

Publicationsi

  1. "The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2."
    Chroboczek J., Bieber F., Jacrot B.
    Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "De novo derivation of proteomes from transcriptomes for transcript and protein identification."
    Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.
    Nat. Methods 9:1207-1211(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Latest insights on adenovirus structure and assembly."
    San Martin C.
    Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  4. "Visualization of alpha-helices in a 6-angstrom resolution cryoelectron microscopy structure of adenovirus allows refinement of capsid protein assignments."
    Saban S.D., Silvestry M., Nemerow G.R., Stewart P.L.
    J. Virol. 80:12049-12059(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE VIRAL PARTICLE, PROTEOLYTIC PROCESSING.
  5. "Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks."
    Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.
    Science 329:1038-1043(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE, PROTEOLYTIC PROCESSING, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CAPSID VERTEX PROTEIN AND HEXON PROTEIN.
  6. "Crystal structure of human adenovirus at 3.5 A resolution."
    Reddy V.S., Natchiar S.K., Stewart P.L., Nemerow G.R.
    Science 329:1071-1075(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).

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: March 4, 2015
This is version 52 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

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

External Data

Dasty 3

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 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.