AC   MF_04051;
DC   Protein; auto
TR   HAMAP; MF_04051; -; 1; level=0
XX
Names: ADV_CAPSH
XX
ID   CAPSH
DE   RecName: Full=Hexon protein;
DE            Short=CP-H;
DE   AltName: Full=Protein II;
GN   Name=L3;
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CC   -!- FUNCTION: Major capsid protein that self-associates to form 240 hexon
CC       trimers, each in the shape of a hexagon, building most of the pseudo
CC       T=25 capsid. Assembled into trimeric units with the help of the
CC       chaperone shutoff protein. Transported by pre-protein VI to the nucleus
CC       where it associates with other structural proteins to form an empty
CC       capsid. Might be involved, through its interaction with host dyneins,
CC       in the intracellular microtubule-dependent transport of incoming viral
CC       capsid to the nucleus.
CC   -!- SUBUNIT: Homotrimer. Interacts with the capsid vertex protein; this
CC       interaction binds the peripentonal hexons to the neighboring penton
CC       base. Interacts with the hexon-linking protein; this interaction
CC       tethers the hexons surrounding the penton to those situated in the
CC       central plate of the facet. Interacts with the hexon-interlacing
CC       protein; this interaction lashes the hexons together. Interacts with
CC       host dyneins DYNC1LI1 and DYNC1I2; this interaction might be involved
CC       in intracellular microtubule-dependent transport of incoming viral
CC       capsid. Interacts with the shutoff protein; this interaction allows
CC       folding and formation of hexons trimers. Interacts with pre-protein VI;
CC       this interaction probably allows nuclear import of hexon trimers and
CC       possibly pre-capsid assembly.
CC   -!- SUBCELLULAR LOCATION: Virion. Host nucleus. Note=Forms the capsid
CC       icosahedric shell. Present in 720 copies per virion, assembled in 240
CC       trimers.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- MISCELLANEOUS: All late proteins expressed from the major late promoter
CC       are produced by alternative splicing and alternative polyadenylation of
CC       the same gene giving rise to non-overlapping ORFs. A leader sequence is
CC       present in the N-terminus of all these mRNAs and is recognized by the
CC       viral shutoff protein to provide expression although conventional
CC       translation via ribosome scanning from the cap has been shut off in the
CC       host cell.
CC   -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
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DR   Pfam; PF01065; Adeno_hexon; 1; trigger=no
DR   Pfam; PF03678; Adeno_hexon_C; 1; trigger=no
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case <FTTag:Acet>
KW   Acetylation
end case
KW   Capsid protein
KW   Cytoplasmic inwards viral transport
KW   Host nucleus
KW   Host-virus interaction
KW   Late protein
KW   Microtubular inwards viral transport
KW   Phosphoprotein
KW   T=25 icosahedral capsid protein
KW   Virion
KW   Virus entry into host cell
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GO   GO:0042025; C:host cell nucleus
GO   GO:0039623; C:T=25 icosahedral viral capsid
GO   GO:0019028; C:viral capsid
GO   GO:0005198; F:structural molecule activity
GO   GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus
GO   GO:0046718; P:viral entry into host cell
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FT   From: CAPSH_ADE05 (P04133)
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT   Group: 1; Condition: M
case <FTGroup:1>
FT   CHAIN           2..Cter
FT                   /note="Hexon protein"
end case
case not <FTGroup:1>
FT   CHAIN           Nter..Cter
FT                   /note="Hexon protein"
end case
FT   SITE            777
FT                   /note="Involved in interaction with pre-protein VI"
FT   Condition: G
FT   MOD_RES         2
FT                   /note="N-acetylalanine; by host"
FT   Tag: Acet; Condition: A
FT   MOD_RES         175
FT                   /note="Phosphoserine; by host"
FT   Condition: S
FT   MOD_RES         940
FT                   /note="Phosphotyrosine; by host"
FT   Condition: Y
XX
Size: 905-968;
Related: None;
Template: P04133;
Scope:
 Viruses; Adenoviridae
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
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# Revision 1.4 2019/11/20
//