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P42671

- CAPSH_ADEG1

UniProt

P42671 - CAPSH_ADEG1

Protein

Hexon protein

Gene
N/A
Organism
Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian adenovirus gal1 (strain Phelps))
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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. 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.By 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
    OrganismiFowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian adenovirus gal1 (strain Phelps))
    Taxonomic identifieri10553 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageAdenoviridaeAviadenovirusFowl aviadenovirus A
    Virus hostiGalliformes [TaxID: 8976]
    ProteomesiUP000001594: 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

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 942942Hexon proteinPRO_0000221826Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei931 – 9311Phosphotyrosine; by hostBy similarity

    Keywords - PTMi

    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. Interacts with pre-protein VI; this interaction probably allows nuclear import of hexon trimers and possibly pre-capsid assembly By similarity.By similarity

    Structurei

    Secondary structure

    1
    942
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi13 – 175
    Beta strandi20 – 234
    Turni26 – 283
    Helixi31 – 399
    Turni40 – 423
    Beta strandi47 – 504
    Beta strandi59 – 624
    Beta strandi69 – 735
    Beta strandi82 – 898
    Beta strandi106 – 1083
    Beta strandi121 – 1233
    Beta strandi153 – 1564
    Beta strandi188 – 1925
    Beta strandi201 – 2033
    Beta strandi205 – 2073
    Beta strandi209 – 2135
    Beta strandi217 – 2193
    Beta strandi235 – 2395
    Beta strandi252 – 2576
    Beta strandi277 – 2793
    Helixi295 – 2973
    Beta strandi299 – 3013
    Helixi306 – 3083
    Helixi331 – 34111
    Turni349 – 3524
    Helixi360 – 3634
    Turni383 – 3853
    Beta strandi396 – 3983
    Beta strandi404 – 4063
    Helixi431 – 44313
    Helixi445 – 4473
    Helixi450 – 4523
    Beta strandi453 – 4553
    Turni462 – 4643
    Helixi471 – 4744
    Helixi481 – 4833
    Beta strandi486 – 4894
    Helixi497 – 4993
    Helixi511 – 5166
    Beta strandi522 – 5243
    Beta strandi530 – 5323
    Turni537 – 5415
    Beta strandi551 – 5566
    Turni559 – 5613
    Beta strandi564 – 5674
    Turni572 – 5754
    Beta strandi584 – 5885
    Helixi594 – 60411
    Beta strandi619 – 6224
    Beta strandi632 – 6409
    Beta strandi647 – 6504
    Helixi676 – 6783
    Beta strandi690 – 6956
    Turni696 – 6983
    Beta strandi699 – 7024
    Beta strandi707 – 7093
    Beta strandi711 – 7144
    Beta strandi719 – 7224
    Turni735 – 74612
    Helixi758 – 7603
    Beta strandi762 – 7643
    Beta strandi766 – 7727
    Beta strandi780 – 7867
    Beta strandi797 – 8015
    Turni806 – 8083
    Beta strandi813 – 8153
    Beta strandi817 – 8204
    Beta strandi838 – 8425
    Beta strandi855 – 8573
    Beta strandi863 – 8719
    Turni878 – 8803
    Turni883 – 8864
    Beta strandi890 – 8978
    Beta strandi909 – 9124
    Beta strandi923 – 9253
    Beta strandi934 – 9363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2INYX-ray3.90A1-942[»]
    ProteinModelPortaliP42671.
    SMRiP42671. Positions 2-942.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP42671.

    Family & Domainsi

    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.

    P42671-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTALTPDLTT ATPRLQYFHI AGPGTREYLS EDLQQFISAT GSYFDLKNKF    50
    RQTVVAPTRN VTTEKAQRLQ IRFYPIQTDD TPNSYRVRYS VNVGDSWVLD 100
    MGATYFDIKG VLDRGPSFKP YGGTAYNPLA PREAIFNTWV ESTGPQTNVV 150
    GQMTNVYTNQ TRNDKTATLQ QVNSISGVVP NVNLGPGLSQ LASRADVDNI 200
    GVVGRFAKVD SAGVKQAYGA YVKPVKDDGS QSLNQTAYWL MDNGGTNYLG 250
    ALAVEDYTQT LSYPDTVLVT PPTAYQQVNS GTMRACRPNY IGFRDNFINL 300
    LYHDSGVCSG TLNSERSGMN VVVELQDRNT ELSYQYMLAD MMSRHHYFAL 350
    WNQAVDQYDH DVRVFNNDGY EEGVPTYAFL PDGHGAGEDN GPDLSNVKIY 400
    TNGQQDKGNV VAGTVSTQLN FGTIPSYEID IAAATRRNFI MSNIADYLPD 450
    KYKFSIRGFD PVTDNIDPTT YFYMNRRVPL TNVVDLFTNI GARWSVDQMD 500
    NVNPFNHHRN WGLKYRSQLL GNSRYCRFHI QVPQKYFAIK NLLLLPGTYT 550
    YEWVLRKDPN MILQSSLGND LRADGAQIVY TEVNLMANFM PMDHNTSNQL 600
    ELMLRNATND QTFADYLGAK NALYNVPAGS TLLTINIPAR TWEGMRGWSF 650
    TRLKASETPQ LGAQYDVGFK YSGSIPYSDG TFYLSHTFRS MSVLFDTSIN 700
    WPGNDRLLTP NLFEIKRPVA TDSEGFTMSQ CDMTKDWFLV QMATNYNYVY 750
    NGYRFWPDRH YFHYDFLRNF DPMSRQGPNF LDTTLYDLVS STPVVNDTGS 800
    QPSQDNVRNN SGFIAPRSWP VWTAQQGEAW PANWPYPLIG NDAISSNQTV 850
    NYKKFLCDNY LWTVPFSSDF MYMGELTDLG QNPMYTNNSH SMVINFELDP 900
    MDENTYVYML YGVFDTVRVN QPERNVLAMA YFRTPFATGN AV 942
    Length:942
    Mass (Da):106,709
    Last modified:November 1, 1997 - v2
    Checksum:i7F4CE8D3F17D051B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46933 Genomic DNA. Translation: AAC54912.1.
    L13161 Genomic DNA. Translation: AAA51401.1.
    RefSeqiNP_043886.1. NC_001720.1.

    Genome annotation databases

    GeneIDi1476562.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U46933 Genomic DNA. Translation: AAC54912.1 .
    L13161 Genomic DNA. Translation: AAA51401.1 .
    RefSeqi NP_043886.1. NC_001720.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2INY X-ray 3.90 A 1-942 [» ]
    ProteinModelPortali P42671.
    SMRi P42671. Positions 2-942.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1476562.

    Miscellaneous databases

    EvolutionaryTracei P42671.

    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. "The complete DNA sequence and genomic organization of the avian adenovirus CELO."
      Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.
      J. Virol. 70:2939-2949(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Organization of the avian adenovirus genome and the structure of its endopeptidase."
      Cai F., Weber J.M.
      Virology 196:358-362(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 913-942.

    Entry informationi

    Entry nameiCAPSH_ADEG1
    AccessioniPrimary (citable) accession number: P42671
    Secondary accession number(s): Q64758
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 75 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 By similarity.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference 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