CAP8_ADECC
ID CAP8_ADECC Reviewed; 224 AA.
AC P68948; Q89783;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 12-AUG-2020, entry version 39.
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 CLL) (CAdV-1) (Canine adenovirus 1
OS (strain CLL)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Canine mastadenovirus A.
OX NCBI_TaxID=69150;
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Campbell J.B., Zhao Y.;
RT "DNA sequence and genomic organization of canine adenovirus type 1.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE OF 154-224.
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-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; U55001; AAB05448.1; -; Genomic_DNA.
DR EMBL; U09195; AAA18163.1; -; Unassigned_RNA.
DR RefSeq; AP_000065.1; AC_000003.1.
DR SMR; P68948; -.
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_0000421409"
FT PEPTIDE 1..111
FT /note="Hexon-linking protein-N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421410"
FT PROPEP 112..154
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036503"
FT PEPTIDE 155..224
FT /note="Hexon-linking protein-C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036504"
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
