CAP8_ADEG1
ID CAP8_ADEG1 Reviewed; 245 AA.
AC Q89814;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 66.
DE RecName: Full=Pre-hexon-linking protein VIII {ECO:0000255|HAMAP-Rule:MF_04049};
DE AltName: Full=Pre-protein VIII {ECO:0000255|HAMAP-Rule:MF_04049};
DE Short=pVIII {ECO:0000255|HAMAP-Rule:MF_04049};
DE Contains:
DE RecName: Full=Hexon-linking protein-N {ECO:0000255|HAMAP-Rule:MF_04049};
DE AltName: Full=12.1 kDa protein VIII {ECO:0000255|HAMAP-Rule:MF_04049};
DE AltName: Full=Protein VIII-N {ECO:0000255|HAMAP-Rule:MF_04049};
DE Contains:
DE RecName: Full=Hexon-linking protein-C {ECO:0000255|HAMAP-Rule:MF_04049};
DE AltName: Full=7.6 kDa protein VIII {ECO:0000255|HAMAP-Rule:MF_04049};
DE AltName: Full=Protein VIII-C {ECO:0000255|HAMAP-Rule:MF_04049};
GN Name=L4 {ECO:0000255|HAMAP-Rule:MF_04049};
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 [GENOMIC DNA].
RX PubMed=7563058; DOI=10.1006/jmbi.1995.0504;
RA Hess M., Cuzange A., Ruigrok R.W., Chroboczek J., Jacrot B.;
RT "The avian adenovirus penton: two fibres and one base.";
RL J. Mol. Biol. 252:379-385(1995).
RN [2]
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).
CC -!- FUNCTION: [Hexon-linking protein-N]: Structural component of the virion
CC that acts as a cement protein on the capsid interior and which glue the
CC peripentonal hexons and group-of-nine hexons together.
CC {ECO:0000255|HAMAP-Rule:MF_04049}.
CC -!- FUNCTION: [Hexon-linking protein-C]: Structural component of the virion
CC that acts as a cement protein on the capsid interior and which glue the
CC peripentonal hexons and group-of-nine hexons together.
CC {ECO:0000255|HAMAP-Rule:MF_04049}.
CC -!- SUBUNIT: Interacts with the peripentonal hexons as well as the hexons
CC in the facets. Part of a complex composed of the core-capsid bridging
CC protein, the endosome lysis protein VI and the hexon-linking protein
CC VIII; these interactions bridge the virus core to the capsid.
CC {ECO:0000255|HAMAP-Rule:MF_04049}.
CC -!- SUBCELLULAR LOCATION: [Hexon-linking protein-C]: Virion
CC {ECO:0000255|HAMAP-Rule:MF_04049}. Note=Located on the inner side of
CC the capsid shell. Present in 120 copies per virion. {ECO:0000255|HAMAP-
CC Rule:MF_04049}.
CC -!- SUBCELLULAR LOCATION: [Pre-hexon-linking protein VIII]: Host nucleus
CC {ECO:0000255|HAMAP-Rule:MF_04049}.
CC -!- SUBCELLULAR LOCATION: [Hexon-linking protein-N]: Virion
CC {ECO:0000255|HAMAP-Rule:MF_04049}. Note=Located on the inner side of
CC the capsid shell. Present in 120 copies per virion. {ECO:0000255|HAMAP-
CC Rule:MF_04049}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04049}.
CC -!- PTM: Cleaved by the viral protease during virion maturation. May cause
CC the middle segment to be shed from the capsid. {ECO:0000255|HAMAP-
CC Rule:MF_04049}.
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_04049}.
CC -!- SIMILARITY: Belongs to the adenoviridae hexon-linking protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000305}.
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DR EMBL; X84724; CAA59205.1; -; Genomic_DNA.
DR EMBL; U46933; AAC54916.1; -; Genomic_DNA.
DR PIR; S54125; S54125.
DR RefSeq; NP_043890.1; NC_001720.1.
DR GeneID; 1476563; -.
DR Proteomes; UP000001594; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0031423; F:hexon binding; IEA:InterPro.
DR HAMAP; MF_04049; ADV_CAP8; 1.
DR InterPro; IPR000646; Adeno_PVIII.
DR Pfam; PF01310; Adeno_PVIII; 1.
PE 3: Inferred from homology;
KW Capsid protein; Host nucleus; Late protein; Phosphoprotein;
KW Reference proteome; Virion.
FT CHAIN 1..245
FT /note="Pre-hexon-linking protein VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421418"
FT PEPTIDE 1..115
FT /note="Hexon-linking protein-N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421419"
FT PROPEP 116..167
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036511"
FT PEPTIDE 168..245
FT /note="Hexon-linking protein-C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000439696"
FT SITE 115..116
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT SITE 167..168
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
SQ SEQUENCE 245 AA; 26877 MW; 7AD09EEF923088B8 CRC64;
MNLMNATPTE YVWKYNPVSG IPAGAQQNYG ATIDWVLPGG TGFAIATNDI RRQTLNPAVT
RAITARFEAE SDQQPYASPH ETNVIAANVL DSGYPKSGLY PLELSGNQRV QLAGGLMVGR
TEGRMQLAGG LTEGRVQLSG GFHGRPLVRG RSRRPPRWCG AELTGNGLPE QAEVTSDTYK
YFLRTQGPSQ VVEEPGVFSQ RQFMTTFLPS VVPHPFDSTN PGDFPAQYSA IYKGRTAFED
TFWDW
