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P12537

- CAP3_ADE05

UniProt

P12537 - CAP3_ADE05

Protein

Pre-capsid vertex protein

Gene

L1

Organism
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 2 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Structural component of the virion that is likely to participate in vertex stabilization and genome packaging. Stabilizes vertices by tethering the penton bases to neighboring peripentonal hexons. Lashes peripentonal hexons to the neighboring hexons thanks to its interaction with hexon-linking protein. As the virus enters the host cell, capsid vertex proteins are shed concomitant with virion acidification in the endosome. During virus assembly, seems to play a role in packaging of viral DNA via its interaction with packaging protein 3.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei15 – 162Cleavage; by viral proteaseBy similarity

    GO - Biological processi

    1. viral release from host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Viral genome packaging, Virus exit from host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pre-capsid vertex protein
    Alternative name(s):
    Capsid vertex-specific component IIIa
    Short name:
    CVSC
    Protein IIIa
    pIIIa
    Cleaved into the following chain:
    Gene namesi
    ORF Names:L1
    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

    Chain Capsid vertex protein : Virion
    Note: Located inside the virion, arranged in a ring underneath the penton base and peripentonal hexons. Present in around 60 copies per virion.

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell
    2. viral capsid Source: CACAO

    Keywords - Cellular componenti

    Capsid protein, Host nucleus, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 585585Pre-capsid vertex proteinPRO_0000221835Add
    BLAST
    Propeptidei1 – 1515By similarityPRO_0000421129Add
    BLAST
    Chaini16 – 585570Capsid vertex proteinBy similarityPRO_0000421130Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei225 – 2251Phosphoserine; by hostBy similarity
    Modified residuei274 – 2741Phosphothreonine; by hostBy similarity
    Modified residuei310 – 3101Phosphoserine; by hostBy similarity
    Modified residuei444 – 4441Phosphoserine; by hostBy similarity
    Modified residuei449 – 4491Phosphoserine; by hostBy similarity
    Modified residuei450 – 4501Phosphoserine; by hostBy similarity
    Modified residuei452 – 4521Phosphoserine; by hostBy similarity
    Modified residuei469 – 4691Phosphoserine; by hostBy similarity
    Modified residuei473 – 4731Phosphoserine; by hostBy similarity
    Modified residuei490 – 4901Phosphotyrosine; by hostBy similarity
    Modified residuei494 – 4941Phosphoserine; by hostBy similarity
    Modified residuei515 – 5151Phosphoserine; by hostBy similarity

    Post-translational modificationi

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

    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 penton and hexon proteins; this interaction binds the penton base to neighboring peripentonal hexons. Interacts with hexon-linking protein; this interaction tethers the peripentonal hexons to hexons situated in the facet. Interacts with packaging protein 3; this interaction is required to promote correct genome packaging. Interacts with adjacent capsid vertex proteins (self-interaction).2 Publications

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3IYNelectron microscopy-N1-585[»]
    ProteinModelPortaliP12537.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12537.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 106106Peripentonal hexon-tethering domainBy similarityAdd
    BLAST
    Regioni138 – 251114Binding to hexon-linking proteinBy similarityAdd
    BLAST

    Sequence similaritiesi

    Family and domain databases

    InterProiIPR003479. Hex_IIIa.
    [Graphical view]
    PfamiPF02455. Hex_IIIa. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P12537-1 [UniParc]FASTAAdd to Basket

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    MMQDATDPAV RAALQSQPSG LNSTDDWRQV MDRIMSLTAR NPDAFRQQPQ    50
    ANRLSAILEA VVPARANPTH EKVLAIVNAL AENRAIRPDE AGLVYDALLQ 100
    RVARYNSGNV QTNLDRLVGD VREAVAQRER AQQQGNLGSM VALNAFLSTQ 150
    PANVPRGQED YTNFVSALRL MVTETPQSEV YQSGPDYFFQ TSRQGLQTVN 200
    LSQAFKNLQG LWGVRAPTGD RATVSSLLTP NSRLLLLLIA PFTDSGSVSR 250
    DTYLGHLLTL YREAIGQAHV DEHTFQEITS VSRALGQEDT GSLEATLNYL 300
    LTNRRQKIPS LHSLNSEEER ILRYVQQSVS LNLMRDGVTP SVALDMTARN 350
    MEPGMYASNR PFINRLMDYL HRAAAVNPEY FTNAILNPHW LPPPGFYTGG 400
    FEVPEGNDGF LWDDIDDSVF SPQPQTLLEL QQREQAEAAL RKESFRRPSS 450
    LSDLGAAAPR SDASSPFPSL IGSLTSTRTT RPRLLGEEEY LNNSLLQPQR 500
    EKNLPPAFPN NGIESLVDKM SRWKTYAQEH RDVPGPRPPT RRQRHDRQRG 550
    LVWEDDDSAD DSSVLDLGGS GNPFAHLRPR LGRMF 585
    Length:585
    Mass (Da):65,253
    Last modified:March 1, 1992 - v2
    Checksum:i430113688C473F1D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73260 Genomic DNA. Translation: AAA96407.1.
    M22141 Genomic DNA. Translation: AAA42518.1.
    PIRiB39449. SXADH5.
    RefSeqiAP_000205.1. AC_000008.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73260 Genomic DNA. Translation: AAA96407.1 .
    M22141 Genomic DNA. Translation: AAA42518.1 .
    PIRi B39449. SXADH5.
    RefSeqi AP_000205.1. AC_000008.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3IYN electron microscopy - N 1-585 [» ]
    ProteinModelPortali P12537.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P12537.

    Family and domain databases

    InterProi IPR003479. Hex_IIIa.
    [Graphical view ]
    Pfami PF02455. Hex_IIIa. 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. "Determination of the nucleotide sequence for the penton-base gene of human adenovirus type 5."
      Neumann R., Chroboczek J., Jacrot B.
      Gene 69:153-157(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 469-585.
    4. "Localization of the N-terminus of minor coat protein IIIa in the adenovirus capsid."
      San Martin C., Glasgow J.N., Borovjagin A., Beatty M.S., Kashentseva E.A., Curiel D.T., Marabini R., Dmitriev I.P.
      J. Mol. Biol. 383:923-934(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Adenovirus structural protein IIIa is involved in the serotype specificity of viral DNA packaging."
      Ma H.C., Hearing P.
      J. Virol. 85:7849-7855(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PACKAGING PROTEIN 3.
      Strain: Human adenovirus D serotype 17.
    6. "Latest insights on adenovirus structure and assembly."
      San Martin C.
      Viruses 4:847-877(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    7. "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, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HEXON-LINKING PROTEIN; PENTON PROTEIN AND HEXON PROTEIN.

    Entry informationi

    Entry nameiCAP3_ADE05
    AccessioniPrimary (citable) accession number: P12537
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 51 of the entry and version 2 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.

    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