ID   CAP8_ADECG              Reviewed;          71 AA.
AC   P22231;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   12-AUG-2020, entry version 52.
DE   RecName: Full=Pre-hexon-linking protein VIII;
DE   AltName: Full=Pre-protein VIII;
DE            Short=pVIII;
DE   Contains:
DE     RecName: Full=Hexon-linking protein-C;
DE     AltName: Full=7.6 kDa protein VIII;
DE     AltName: Full=Protein VIII-C;
DE   Flags: Fragment;
GN   ORFNames=L4;
OS   Canine adenovirus serotype 1 (strain Glaxo) (CAdV-1) (Canine adenovirus 1
OS   (strain Glaxo)).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX   NCBI_TaxID=10513;
OH   NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1828920; DOI=10.1016/0042-6822(91)90142-x;
RA   Dragulev B.P., Sira S., Abouhaidar M.G., Campbell J.B.;
RT   "Sequence analysis of putative E3 and fiber genomic regions of two strains
RT   of canine adenovirus type 1.";
RL   Virology 183:298-305(1991).
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:0000250|UniProtKB:P24936}.
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:0000250|UniProtKB:P24936}.
CC   -!- SUBCELLULAR LOCATION: [Pre-hexon-linking protein VIII]: Host nucleus
CC       {ECO:0000250|UniProtKB:P24936}.
CC   -!- SUBCELLULAR LOCATION: [Hexon-linking protein-C]: Virion
CC       {ECO:0000250|UniProtKB:P24936}. Note=Located on the inner side of the
CC       capsid shell. Present in 120 copies per virion.
CC       {ECO:0000250|UniProtKB:P24936}.
CC   -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC   -!- PTM: Cleaved by the viral protease during virion maturation. May cause
CC       the middle segment to be shed from the capsid.
CC       {ECO:0000250|UniProtKB:P24936}.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the adenoviridae hexon-linking protein family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M60937; AAA42533.1; -; Genomic_DNA.
DR   PIR; A40318; A40318.
DR   SMR; P22231; -.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0031423; F:hexon binding; IEA:InterPro.
DR   InterPro; IPR000646; Adeno_PVIII.
DR   Pfam; PF01310; Adeno_PVIII; 1.
PE   2: Evidence at transcript level;
KW   Capsid protein; Host nucleus; Late protein; Virion.
FT   CHAIN           <1..71
FT                   /note="Pre-hexon-linking protein VIII"
FT                   /id="PRO_0000421411"
FT   PEPTIDE         2..71
FT                   /note="Hexon-linking protein-C"
FT                   /id="PRO_0000221843"
FT   SITE            1..2
FT                   /note="Cleavage; by viral protease"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   71 AA;  7798 MW;  CC2B47D959328F77 CRC64;
     GSRSSFSPTQ AFLTLQQASS TPRTGGVGSY QFVREFVPEV YLNPFSGPPD TFPDQFIPNY
     DIVTNSVDGY D