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P04133

- CAPSH_ADE05

UniProt

P04133 - CAPSH_ADE05

Protein

Hexon protein

Gene

L3

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 100 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein By similarity. Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei777 – 7771Involved in interaction with pre-protein VIBy similarity

    GO - Molecular functioni

    1. structural molecule activity Source: InterPro

    GO - Biological processi

    1. microtubule-dependent intracellular transport of viral material towards nucleus Source: UniProtKB-KW
    2. viral entry into host cell Source: UniProtKB-KW

    Keywords - Biological processi

    Cytoplasmic inwards viral transport, Host-virus interaction, Microtubular inwards viral transport, Virus entry into host cell

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hexon protein
    Short name:
    CP-H
    Alternative name(s):
    Protein II
    Gene namesi
    ORF Names:L3
    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

    Virion By similarity. Host nucleus By similarity
    Note: Forms the capsid icosahedric shell. Present in 720 copies per virion, assembled in 240 trimers By similarity.By similarity

    GO - Cellular componenti

    1. host cell nucleus Source: UniProtKB-SubCell
    2. intracellular Source: GOC
    3. T=25 icosahedral viral capsid Source: UniProtKB-KW
    4. viral capsid Source: CACAO

    Keywords - Cellular componenti

    Capsid protein, Host nucleus, T=25 icosahedral capsid protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed; by hostBy similarity
    Chaini2 – 952951Hexon proteinPRO_0000221816Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine; by hostBy similarity
    Modified residuei175 – 1751Phosphoserine; by hostBy similarity
    Modified residuei940 – 9401Phosphotyrosine; by hostBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Expressioni

    Inductioni

    Expressed in the late phase of the viral replicative cycle.

    Keywords - Developmental stagei

    Late protein

    Interactioni

    Subunit structurei

    Homotrimer By similarity. Interacts with the capsid vertex protein; this interaction binds the peripentonal hexons to the neighboring penton base. Interacts with the hexon-linking protein; this interaction tethers the hexons surrounding the penton to those situated in the central plate of the facet. Interacts with the hexon-interlacing protein; this interaction lashes the hexons together. Interacts with host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved in intracellular microtubule-dependent transport of incoming viral capsid. Interacts with the shutoff protein; this interaction allows folding and formation of hexons trimers By similarity. Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly.By similarity2 Publications

    Protein-protein interaction databases

    IntActiP04133. 2 interactions.
    MINTiMINT-6597435.

    Structurei

    Secondary structure

    1
    952
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 124
    Beta strandi15 – 173
    Helixi20 – 234
    Helixi26 – 3510
    Turni36 – 383
    Helixi42 – 443
    Beta strandi54 – 574
    Beta strandi64 – 685
    Beta strandi71 – 755
    Beta strandi77 – 8812
    Helixi96 – 983
    Beta strandi100 – 1089
    Beta strandi116 – 1183
    Beta strandi132 – 1354
    Beta strandi167 – 1693
    Beta strandi183 – 1875
    Beta strandi189 – 1913
    Beta strandi192 – 1954
    Turni198 – 2003
    Beta strandi209 – 2124
    Beta strandi217 – 2248
    Beta strandi226 – 2283
    Turni243 – 2453
    Turni254 – 2563
    Beta strandi263 – 2675
    Beta strandi283 – 2897
    Beta strandi298 – 3025
    Beta strandi306 – 3094
    Helixi312 – 3165
    Beta strandi318 – 3214
    Beta strandi327 – 3293
    Helixi331 – 3333
    Helixi342 – 3443
    Beta strandi347 – 3504
    Turni351 – 3533
    Helixi366 – 37712
    Helixi385 – 3873
    Helixi396 – 3994
    Beta strandi400 – 4023
    Beta strandi415 – 4173
    Beta strandi424 – 4263
    Beta strandi434 – 4363
    Beta strandi444 – 4463
    Beta strandi450 – 4523
    Helixi464 – 47613
    Helixi478 – 4803
    Helixi483 – 4853
    Helixi501 – 5066
    Helixi511 – 5144
    Turni516 – 5216
    Helixi527 – 5304
    Beta strandi536 – 5405
    Helixi541 – 55010
    Beta strandi552 – 56312
    Turni567 – 5715
    Beta strandi576 – 58611
    Helixi589 – 5924
    Beta strandi593 – 5975
    Turni601 – 6055
    Beta strandi607 – 61812
    Helixi624 – 63411
    Helixi637 – 6393
    Beta strandi641 – 6444
    Beta strandi649 – 6568
    Beta strandi662 – 6709
    Beta strandi677 – 6848
    Helixi685 – 6873
    Beta strandi692 – 6943
    Helixi706 – 7094
    Helixi715 – 7173
    Beta strandi718 – 7258
    Turni726 – 7283
    Beta strandi729 – 7324
    Beta strandi737 – 7393
    Beta strandi742 – 7443
    Helixi749 – 7546
    Beta strandi759 – 7624
    Helixi763 – 77412
    Beta strandi777 – 7793
    Helixi786 – 7883
    Helixi794 – 7974
    Beta strandi798 – 8069
    Turni808 – 8103
    Turni819 – 8213
    Turni826 – 8283
    Beta strandi831 – 8355
    Beta strandi858 – 8669
    Beta strandi871 – 8766
    Beta strandi882 – 8854
    Helixi888 – 8903
    Helixi892 – 8965
    Beta strandi899 – 9079
    Beta strandi914 – 9218
    Beta strandi923 – 9297
    Turni932 – 9343
    Beta strandi937 – 9459

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P30X-ray2.50A2-952[»]
    1VSZX-ray3.50A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
    2BVIelectron microscopy10.00F/G/H/I/J/K/L/M/N/O/P/Q2-952[»]
    3IYNelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L1-952[»]
    3TG7X-ray1.57A2-952[»]
    ProteinModelPortaliP04133.
    SMRiP04133. Positions 6-947.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04133.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi134 – 15926Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the adenoviridae hexon protein family.Curated

    Family and domain databases

    Gene3Di2.70.9.10. 2 hits.
    3.90.249.10. 3 hits.
    InterProiIPR016108. Adenovirus_Pll_hexon_C.
    IPR016107. Adenovirus_Pll_hexon_N.
    IPR016110. Adenovirus_Pll_hexon_sub3.
    IPR016111. Hexon_subdom4.
    IPR016112. VP_dsDNA_II.
    [Graphical view]
    PfamiPF01065. Adeno_hexon. 1 hit.
    PF03678. Adeno_hexon_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF49749. SSF49749. 2 hits.

    Sequencei

    Sequence statusi: Complete.

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

    P04133-1 [UniParc]FASTAAdd to Basket

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    MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV    50
    APTHDVTTDR SQRLTLRFIP VDREDTAYSY KARFTLAVGD NRVLDMASTY 100
    FDIRGVLDRG PTFKPYSGTA YNALAPKGAP NPCEWDEAAT ALEINLEEED 150
    DDNEDEVDEQ AEQQKTHVFG QAPYSGINIT KEGIQIGVEG QTPKYADKTF 200
    QPEPQIGESQ WYETEINHAA GRVLKKTTPM KPCYGSYAKP TNENGGQGIL 250
    VKQQNGKLES QVEMQFFSTT EATAGNGDNL TPKVVLYSED VDIETPDTHI 300
    SYMPTIKEGN SRELMGQQSM PNRPNYIAFR DNFIGLMYYN STGNMGVLAG 350
    QASQLNAVVD LQDRNTELSY QLLLDSIGDR TRYFSMWNQA VDSYDPDVRI 400
    IENHGTEDEL PNYCFPLGGV INTETLTKVK PKTGQENGWE KDATEFSDKN 450
    EIRVGNNFAM EINLNANLWR NFLYSNIALY LPDKLKYSPS NVKISDNPNT 500
    YDYMNKRVVA PGLVDCYINL GARWSLDYMD NVNPFNHHRN AGLRYRSMLL 550
    GNGRYVPFHI QVPQKFFAIK NLLLLPGSYT YEWNFRKDVN MVLQSSLGND 600
    LRVDGASIKF DSICLYATFF PMAHNTASTL EAMLRNDTND QSFNDYLSAA 650
    NMLYPIPANA TNVPISIPSR NWAAFRGWAF TRLKTKETPS LGSGYDPYYT 700
    YSGSIPYLDG TFYLNHTFKK VAITFDSSVS WPGNDRLLTP NEFEIKRSVD 750
    GEGYNVAQCN MTKDWFLVQM LANYNIGYQG FYIPESYKDR MYSFFRNFQP 800
    MSRQVVDDTK YKDYQQVGIL HQHNNSGFVG YLAPTMREGQ AYPANFPYPL 850
    IGKTAVDSIT QKKFLCDRTL WRIPFSSNFM SMGALTDLGQ NLLYANSAHA 900
    LDMTFEVDPM DEPTLLYVLF EVFDVVRVHR PHRGVIETVY LRTPFSAGNA 950
    TT 952
    Length:952
    Mass (Da):108,007
    Last modified:January 23, 2007 - v3
    Checksum:i822CCDE26E970C5A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti273 – 2731T → A no nucleotide entry (PubMed:23142869)Curated
    Sequence conflicti930 – 9301R → Q no nucleotide entry (PubMed:23142869)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73260 Genomic DNA. No translation available.
    X02997 Genomic DNA. Translation: CAA26753.1.
    PIRiA03849. HXAD5.
    RefSeqiAP_000211.1. AC_000008.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73260 Genomic DNA. No translation available.
    X02997 Genomic DNA. Translation: CAA26753.1 .
    PIRi A03849. HXAD5.
    RefSeqi AP_000211.1. AC_000008.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P30 X-ray 2.50 A 2-952 [» ]
    1VSZ X-ray 3.50 A/B/C/D/E/F/G/H/I/J/K/L 1-952 [» ]
    2BVI electron microscopy 10.00 F/G/H/I/J/K/L/M/N/O/P/Q 2-952 [» ]
    3IYN electron microscopy - A/B/C/D/E/F/G/H/I/J/K/L 1-952 [» ]
    3TG7 X-ray 1.57 A 2-952 [» ]
    ProteinModelPortali P04133.
    SMRi P04133. Positions 6-947.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P04133. 2 interactions.
    MINTi MINT-6597435.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P04133.

    Family and domain databases

    Gene3Di 2.70.9.10. 2 hits.
    3.90.249.10. 3 hits.
    InterProi IPR016108. Adenovirus_Pll_hexon_C.
    IPR016107. Adenovirus_Pll_hexon_N.
    IPR016110. Adenovirus_Pll_hexon_sub3.
    IPR016111. Hexon_subdom4.
    IPR016112. VP_dsDNA_II.
    [Graphical view ]
    Pfami PF01065. Adeno_hexon. 1 hit.
    PF03678. Adeno_hexon_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49749. SSF49749. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Adenovirus hexon. Sequence comparison of subgroup C serotypes 2 and 5."
      Kinloch R., MacKay N., Mautner V.
      J. Biol. Chem. 259:6431-6436(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
    3. "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].
    4. "Switch from capsid protein import to adenovirus assembly by cleavage of nuclear transport signals."
      Wodrich H., Guan T., Cingolani G., Von Seggern D., Nemerow G., Gerace L.
      EMBO J. 22:6245-6255(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRE-PROTEIN VI.
      Strain: Ad5 ts147 mutant and Human adenovirus C serotype 5.
    5. "Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit."
      Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.
      Cell Host Microbe 6:523-535(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HUMAN DYNEINS DYNC1LI1 AND DYNC1I2.

    Entry informationi

    Entry nameiCAPSH_ADE05
    AccessioniPrimary (citable) accession number: P04133
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 100 of the entry and version 3 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