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CAP8_ADECR
ID   CAP8_ADECR              Reviewed;         224 AA.
AC   P68949; Q89783;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   12-AUG-2020, entry version 40.
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   Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine adenovirus 1
OS   (strain RI261)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=69151;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9129661; DOI=10.1099/0022-1317-78-4-873;
RA   Morrison M.D., Onions D.E., Nicolson L.;
RT   "Complete DNA sequence of canine adenovirus type 1.";
RL   J. Gen. Virol. 78:873-878(1997).
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; Y07760; CAA69041.1; -; Genomic_DNA.
DR   RefSeq; AP_000065.1; AC_000003.1.
DR   RefSeq; NP_044203.1; NC_001734.1.
DR   SMR; P68949; -.
DR   GeneID; 1488937; -.
DR   KEGG; vg:1488937; -.
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; Virion.
FT   CHAIN           1..224
FT                   /note="Pre-hexon-linking protein VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000421412"
FT   PEPTIDE         1..111
FT                   /note="Hexon-linking protein-N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000421413"
FT   PROPEP          112..154
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000036505"
FT   PEPTIDE         155..224
FT                   /note="Hexon-linking protein-C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000036506"
FT   SITE            111..112
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT   SITE            154..155
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT   MOD_RES         64
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
SQ   SEQUENCE   224 AA;  24533 MW;  AB6CB5A6A537F72B CRC64;
     MSKEIPTPYI WSYQPQTGHA AGASQDYSTQ MNWFSAGPSM ISHVYGIRDL RNKVLMTQAQ
     ITKTPRTIMD PPIWPASMLV QKHATPKTIA LPRNHTLEQA MVNCGAQLAG GRQPSPSHID
     IKDTMLAGTG IQLGEDIPSV SWIRPDGIFQ LGGGSRSSFS PTQAFLTLQQ ASSTPRTGGV
     GSYQFVREFV PEVYLNPFSG PPDTFPDQFI PNYDIVTNSV DGYD
 
 
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