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P24936

- CAP8_ADE05

UniProt

P24936 - CAP8_ADE05

Protein

Pre-hexon-linking protein

Gene

L4

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    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

    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 – 434
    Helixi45 – 473
    Helixi51 – 577
    Beta strandi58 – 614
    Beta strandi67 – 704

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VSZX-ray3.50R/S1-227[»]
    3IYNelectron microscopy-O/P1-227[»]
    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

    MSKEIPTPYM WSYQPQMGLA AGAAQDYSTR INYMSAGPHM ISRVNGIRAH    50
    RNRILLEQAA ITTTPRNNLN PRSWPAALVY QESPAPTTVV LPRDAQAEVQ 100
    MTNSGAQLAG GFRHRVRSPG QGITHLTIRG RGIQLNDESV SSSLGLRPDG 150
    TFQIGGAGRP SFTPRQAILT LQTSSSEPRS GGIGTLQFIE EFVPSVYFNP 200
    FSGPPGHYPD QFIPNFDAVK DSADGYD 227
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73260 Genomic DNA. Translation: AAA96413.1.
    PIRiE39449. SXAD85.
    RefSeqiAP_000217.1. AC_000008.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73260 Genomic DNA. Translation: AAA96413.1 .
    PIRi E39449. SXAD85.
    RefSeqi AP_000217.1. AC_000008.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VSZ X-ray 3.50 R/S 1-227 [» ]
    3IYN electron microscopy - O/P 1-227 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P24936.

    Family and domain databases

    InterProi IPR000646. Adeno_PVIII.
    [Graphical view ]
    Pfami PF01310. Adeno_PVIII. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 48 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