CAP8_ADE40
ID CAP8_ADE40 Reviewed; 233 AA.
AC P11821;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 72.
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 Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=28284;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugan;
RX PubMed=8263936; DOI=10.1006/jmbi.1993.1687;
RA Davison A.J., Telford E.A., Watson M.S., McBride K., Mautner V.;
RT "The DNA sequence of adenovirus type 40.";
RL J. Mol. Biol. 234:1308-1316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RX PubMed=3279700; DOI=10.1016/0042-6822(88)90227-9;
RA Vos H.L., der Lee F.M., Reemst A.M.C.B., van Loon A.E., Sussenbach J.S.;
RT "The genes encoding the DNA binding protein and the 23K protease of
RT adenovirus types 40 and 41.";
RL Virology 163:1-10(1988).
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; L19443; AAC13972.1; -; Genomic_DNA.
DR EMBL; M19316; AAA52198.1; -; Genomic_DNA.
DR RefSeq; NP_040868.1; NC_001454.1.
DR SMR; P11821; -.
DR DNASU; 2715920; -.
DR GeneID; 2715920; -.
DR Proteomes; UP000151954; 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..233
FT /note="Pre-hexon-linking protein VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421399"
FT PEPTIDE 1..111
FT /note="Hexon-linking protein-N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421400"
FT PROPEP 112..163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036499"
FT PEPTIDE 164..233
FT /note="Hexon-linking protein-C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036500"
FT SITE 111..112
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT SITE 163..164
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"
FT MOD_RES 180
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
SQ SEQUENCE 233 AA; 25327 MW; D135E37D3CA6DE5C CRC64;
MSKDIPTPYM WSYQPQMGLA AGASQDYSSR MNWLSAGPHM IGRVNGIRAT RNQILLEQAA
LTSTPRRQLN PPSWPAAQVY QENPAPTTVL LPRDAEAEVQ MTNSGAQLAG GARHVRFRDR
PSPYSSGSIK RLIIRGRGIQ LNDEVVSSST GPRPDGVFQL GGAGRSSFTP RQAYLTLQSS
SSQPRSGGIG TLQFVEEFVP SVYFNPFSGA PGLYPDDFIP NYDAVSESVD GYD
