ID   CAPSH_ADE01             Reviewed;         467 AA.
AC   Q04965;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   23-FEB-2022, entry version 89.
DE   RecName: Full=Hexon protein;
DE            Short=CP-H;
DE   AltName: Full=Protein II;
DE   Flags: Fragment;
GN   ORFNames=L3;
OS   Human adenovirus C serotype 1 (HAdV-1) (Human adenovirus 1).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus.
OX   NCBI_TaxID=10533;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8511397; DOI=10.1016/s0923-2516(06)80020-8;
RA   Pring-Akerblom P., Adrian T.;
RT   "The hexon genes of adenoviruses of subgenus C: comparison of the variable
RT   regions.";
RL   Res. Virol. 144:117-127(1993).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts with the capsid vertex
CC       protein; this interaction binds the peripentonal hexons to the
CC       neighboring penton base. Interacts with the hexon-linking protein; this
CC       interaction tethers the hexons surrounding the penton to those situated
CC       in the 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host nucleus {ECO:0000250}.
CC       Note=Forms the capsid icosahedric shell. Present in 720 copies per
CC       virion, assembled in 240 trimers (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC       {ECO:0000305}.
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DR   EMBL; X67709; CAA47946.1; -; Genomic_DNA.
DR   SMR; Q04965; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039623; C:T=25 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.39.10; -; 1.
DR   InterPro; IPR016107; Adenovirus_Pll_hexon_N.
DR   InterPro; IPR044942; Adenovirus_Pll_hexon_sub2.
DR   InterPro; IPR016112; VP_dsDNA_II.
DR   Pfam; PF01065; Adeno_hexon; 1.
DR   SUPFAM; SSF49749; SSF49749; 1.
PE   2: Evidence at transcript level;
KW   Capsid protein; Cytoplasmic inwards viral transport; Host nucleus;
KW   Host-virus interaction; Late protein; Microtubular inwards viral transport;
KW   T=25 icosahedral capsid protein; Virion; Virus entry into host cell.
FT   CHAIN           <1..>467
FT                   /note="Hexon protein"
FT                   /id="PRO_0000221812"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..44
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         467
SQ   SEQUENCE   467 AA;  52060 MW;  DC72E5BBFA6FB825 CRC64;
     AYNALAPKGA PNSCEWEQEE PTQEMAGELE DEEEAEEEEA EEEAEAPQAG QKVKKTHVYA
     QAPLAGEKIT ANGLQIVSDT QTEGNPVFAD PTYQPEPQVG ESQWNEAEAT AIGGRVLKKT
     TPMKPCYGSY ARPTNKNGGQ GILVANNQGA LESKVEMQFF APSGTAMNER NAVQPSIVLY
     SEDVNMETPD THISYKPSKT DENSKAMLGQ QAMPNRPNYI AFRDNFIGLM YYNSTGNMGV
     LAGQASQLNA VVDLQDRNTE LSYQLLLDSI GDRTRYFSMW NQAVDSYDPD VRIIENHGTE
     DELPNYCFPL GGIGVTDTYQ GIKSNGNGNP QNWTKNDDFA ARNEIGVGNN FALEINLNAN
     LWRNFLYSNI ALYLPDKLKY TPTNVEISPN PNSYDYMNKR VVAPGLVDCY INLGARWSLD
     YMENVNPFNH HRNAGLRYRS MLLGNGRYVP FHIQVPQKFF AIKNLLL