ID   CAPSH_ADEG1             Reviewed;         942 AA.
AC   P42671; Q64758;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   22-FEB-2023, entry version 109.
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   Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS   adenovirus gal1 (strain Phelps)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX   NCBI_TaxID=10553;
OH   NCBI_TaxID=8976; Galliformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA   Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT   "The complete DNA sequence and genomic organization of the avian adenovirus
RT   CELO.";
RL   J. Virol. 70:2939-2949(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 913-942.
RX   PubMed=8395124; DOI=10.1006/viro.1993.1489;
RA   Cai F., Weber J.M.;
RT   "Organization of the avian adenovirus genome and the structure of its
RT   endopeptidase.";
RL   Virology 196:358-362(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. {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; U46933; AAC54912.1; -; Genomic_DNA.
DR   EMBL; L13161; AAA51401.1; -; Genomic_DNA.
DR   RefSeq; NP_043886.1; NC_001720.1.
DR   PDB; 2INY; X-ray; 3.90 A; A=1-942.
DR   PDBsum; 2INY; -.
DR   SMR; P42671; -.
DR   GeneID; 1476562; -.
DR   KEGG; vg:1476562; -.
DR   EvolutionaryTrace; P42671; -.
DR   Proteomes; UP000001594; Genome.
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; 2.70.9.10; Adenovirus Type 2 Hexon, domain 4; 2.
DR   Gene3D; 3.90.39.10; Hexon Major Viral Coat Protein, domain 2; 1.
DR   Gene3D; 3.90.249.10; Hexon Major Viral Coat Protein, domain 3; 2.
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; Group II dsDNA viruses VP; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Cytoplasmic inwards viral transport;
KW   Host nucleus; Host-virus interaction; Late protein;
KW   Microtubular inwards viral transport; Phosphoprotein; Reference proteome;
KW   T=25 icosahedral capsid protein; Virion; Virus entry into host cell.
FT   CHAIN           1..942
FT                   /note="Hexon protein"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
FT                   /id="PRO_0000221826"
FT   MOD_RES         931
FT                   /note="Phosphotyrosine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04051"
SQ   SEQUENCE   942 AA;  106709 MW;  7F4CE8D3F17D051B CRC64;
     MTALTPDLTT ATPRLQYFHI AGPGTREYLS EDLQQFISAT GSYFDLKNKF RQTVVAPTRN
     VTTEKAQRLQ IRFYPIQTDD TPNSYRVRYS VNVGDSWVLD MGATYFDIKG VLDRGPSFKP
     YGGTAYNPLA PREAIFNTWV ESTGPQTNVV GQMTNVYTNQ TRNDKTATLQ QVNSISGVVP
     NVNLGPGLSQ LASRADVDNI GVVGRFAKVD SAGVKQAYGA YVKPVKDDGS QSLNQTAYWL
     MDNGGTNYLG ALAVEDYTQT LSYPDTVLVT PPTAYQQVNS GTMRACRPNY IGFRDNFINL
     LYHDSGVCSG TLNSERSGMN VVVELQDRNT ELSYQYMLAD MMSRHHYFAL WNQAVDQYDH
     DVRVFNNDGY EEGVPTYAFL PDGHGAGEDN GPDLSNVKIY TNGQQDKGNV VAGTVSTQLN
     FGTIPSYEID IAAATRRNFI MSNIADYLPD KYKFSIRGFD PVTDNIDPTT YFYMNRRVPL
     TNVVDLFTNI GARWSVDQMD NVNPFNHHRN WGLKYRSQLL GNSRYCRFHI QVPQKYFAIK
     NLLLLPGTYT YEWVLRKDPN MILQSSLGND LRADGAQIVY TEVNLMANFM PMDHNTSNQL
     ELMLRNATND QTFADYLGAK NALYNVPAGS TLLTINIPAR TWEGMRGWSF TRLKASETPQ
     LGAQYDVGFK YSGSIPYSDG TFYLSHTFRS MSVLFDTSIN WPGNDRLLTP NLFEIKRPVA
     TDSEGFTMSQ CDMTKDWFLV QMATNYNYVY NGYRFWPDRH YFHYDFLRNF DPMSRQGPNF
     LDTTLYDLVS STPVVNDTGS QPSQDNVRNN SGFIAPRSWP VWTAQQGEAW PANWPYPLIG
     NDAISSNQTV NYKKFLCDNY LWTVPFSSDF MYMGELTDLG QNPMYTNNSH SMVINFELDP
     MDENTYVYML YGVFDTVRVN QPERNVLAMA YFRTPFATGN AV
//