ID   CAPSH_ADEB3             Reviewed;         911 AA.
AC   P03278;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 101.
DE   RecName: Full=Hexon protein {ECO:0000255|HAMAP-Rule:MF_04051};
DE            Short=CP-H {ECO:0000255|HAMAP-Rule:MF_04051};
DE   AltName: Full=Protein II {ECO:0000255|HAMAP-Rule:MF_04051};
GN   Name=L3 {ECO:0000255|HAMAP-Rule:MF_04051};
OS   Bovine adenovirus B serotype 3 (BAdV-3) (Mastadenovirus bos3).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Bovine mastadenovirus B.
OX   NCBI_TaxID=10510;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6694264; DOI=10.1128/jvi.49.2.604-608.1984;
RA   Hu S.-L., Hays W.W., Potts D.E.;
RT   "Sequence homology between bovine and human adenoviruses.";
RL   J. Virol. 49:604-608(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 877-911.
RX   PubMed=2216745; DOI=10.1093/nar/18.18.5568;
RA   Cai F., Bourbonniere M., Tang D., Hu S.L., Weber J.M.;
RT   "Nucleotide and deduced amino acid sequence of the bovine adenovirus type 3
RT   proteinase.";
RL   Nucleic Acids Res. 18:5568-5568(1990).
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. {ECO:0000255|HAMAP-Rule:MF_04051}.
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. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04051}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04051}. Note=Forms the capsid
CC       icosahedric shell. Present in 720 copies per virion, assembled in 240
CC       trimers. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC       {ECO:0000255|HAMAP-Rule:MF_04051}.
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. {ECO:0000255|HAMAP-Rule:MF_04051}.
CC   -!- SIMILARITY: Belongs to the adenoviridae hexon protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04051, ECO:0000305}.
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DR   EMBL; K01264; AAA42509.1; -; Genomic_DNA.
DR   EMBL; X53990; CAA37936.1; -; Genomic_DNA.
DR   PIR; A03850; HXADB3.
DR   PDB; 3ZIF; EM; 4.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-911.
DR   PDBsum; 3ZIF; -.
DR   SMR; P03278; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039623; C:T=25 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.249.10; -; 2.
DR   Gene3D; 3.90.39.10; -; 1.
DR   HAMAP; MF_04051; ADV_CAPSH; 1.
DR   InterPro; IPR016108; Adenovirus_Pll_hexon_C.
DR   InterPro; IPR016107; Adenovirus_Pll_hexon_N.
DR   InterPro; IPR044942; Adenovirus_Pll_hexon_sub2.
DR   InterPro; IPR016110; Adenovirus_Pll_hexon_sub3.
DR   InterPro; IPR037542; ADV_hexon.
DR   InterPro; IPR016112; VP_dsDNA_II.
DR   Pfam; PF01065; Adeno_hexon; 1.
DR   Pfam; PF03678; Adeno_hexon_C; 1.
DR   SUPFAM; SSF49749; SSF49749; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Capsid protein;
KW   Cytoplasmic inwards viral transport; Host nucleus; Host-virus interaction;
KW   Late protein; Microtubular inwards viral transport; Phosphoprotein;
KW   T=25 icosahedral capsid protein; Virion; Virus entry into host cell.
FT   INIT_MET        1
FT                   /note="Removed; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT   CHAIN           2..911
FT                   /note="Hexon protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT                   /id="PRO_0000221827"
FT   SITE            737
FT                   /note="Involved in interaction with pre-protein VI"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT   MOD_RES         2
FT                   /note="N-acetylalanine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT   MOD_RES         899
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ   SEQUENCE   911 AA;  103052 MW;  20F3DED4333BB8AB CRC64;
     MATPSMLPQW SYMHIAGQDA SEYLSPGLVQ FAQATESYFN IGNKFRNPTV APTHDVTTER
     SQRLQLRFVP VDREDTQYSY KTRFQLAVGD NRVLDMASTY FDIRGTLDRG ASFKPYSGTA
     YNSFAPKSAP NNTQFRQANN GHPAQTIAQA SYVATIGGAN NDLQMGVDER QLPVYANTTY
     QPEPQLGIEG WTAGSMAVID QAGGRVLRNP TQTPCYGSYA KPTNEHGGIT KANTQVEKKY
     YRTGDNGNPE TVFYTEEADV LTPDTHLVHA VPAADRAKVE GLSQHAAPNR PNFIGFRDCF
     VGLMYYNSGG NLGVLAGQSS QLNAVVDLQD RNTELSYQML LANTTDRSRY FSMWNQAMDS
     YDPEVRVIDN VGVEDEMPNY CFPLSGVQIG NRSHEVQRNQ QQWQNVANSD NNYIGKGNLP
     AMEINLAANL WRSFLYSNVA LYLPDNLKFT PHNIQLPPNT NTYEYMNGRI PVSGLIDTYV
     NIGTRWSPDV MDNVNPFNHH RNSGLRYRSQ LLGNGRFCDF HIQVPQKFFA IRNLLLLPGT
     YTYEWSFRKD VNMILQSTLG NDLRVDGATV NITSVNLYAS FFPMSHNTAS TLEAMLRNDT
     NDQSFNDYLS AANMLYPIPP NATQLPIPSR NWAAFRGWSL TRLKQRETPA LGSPFDPYFT
     YSGTIPYLDG TFYLSHTFRK VAIQFDSSVT WPGNDRLLTP NEFEIKISVD GEGYNVAQSN
     MTKDWFLVQM LANYNIGYQG YHLPPDYKDR TFSFLHNFIP MCRQVPNPAT EGYFGLGIVN
     HRTTPAYWFR FCRAPREGHP YPQLALPPHW DPRHALRDPE RKFLCDRTLW RIPFSSNFMS
     MGSLTDLGQN LLYANAAHAL DMTFEMDPIN EPTLLYVLFE VFDVARVHQP HRGVIEVVYL
     RTPFSAGNAT T