CAPSH_ADEG1
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 23-FEB-2022, entry version 107.
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; 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; 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
