CAP8_ADE02
ID CAP8_ADE02 Reviewed; 227 AA.
AC P03280;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-DEC-2020, 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 C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=478297; DOI=10.1016/0378-1119(79)90081-7;
RA Galibert F., Herisse J., Courtois G.;
RT "Nucleotide sequence of the EcoRI-F fragment of adenovirus 2 genome.";
RL Gene 6:1-22(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 54-227.
RX PubMed=6253880; DOI=10.1093/nar/8.10.2173;
RA Herisse J., Courtois G., Galibert F.;
RT "Nucleotide sequence of the EcoRI D fragment of adenovirus 2 genome.";
RL Nucleic Acids Res. 8:2173-2192(1980).
RN [3]
RP PROTEIN SEQUENCE OF 54-66; 116-127 AND 166-179, AND PHOSPHORYLATION AT
RP THR-64; SER-118 AND SER-174.
RX PubMed=22939182; DOI=10.1016/j.virol.2012.08.012;
RA Bergstrom Lind S., Artemenko K.A., Elfineh L., Zhao Y., Bergquist J.,
RA Pettersson U.;
RT "The phosphoproteome of the adenovirus type 2 virion.";
RL Virology 433:253-261(2012).
RN [4]
RP REVIEW.
RX PubMed=22754652; DOI=10.3390/v4050847;
RA San Martin C.;
RT "Latest insights on adenovirus structure and assembly.";
RL Viruses 4:847-877(2012).
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; J01917; AAA92220.1; -; Genomic_DNA.
DR PIR; A91583; SXAD82.
DR RefSeq; AP_000181.1; AC_000007.1.
DR RefSeq; NP_040530.1; NC_001405.1.
DR SMR; P03280; -.
DR iPTMnet; P03280; -.
DR GeneID; 2653005; -.
DR Proteomes; UP000008167; 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 1: Evidence at protein level;
KW Capsid protein; Direct protein sequencing; Host nucleus; Late protein;
KW Phosphoprotein; Reference proteome; Virion.
FT CHAIN 1..227
FT /note="Pre-hexon-linking protein VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421075"
FT PEPTIDE 1..111
FT /note="Hexon-linking protein-N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036491"
FT PROPEP 112..157
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421076"
FT PEPTIDE 158..227
FT /note="Hexon-linking protein-C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036492"
FT SITE 111..112
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT SITE 157..158
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 ECO:0000269|PubMed:22939182"
FT MOD_RES 118
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049,
FT ECO:0000269|PubMed:22939182"
FT MOD_RES 174
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049,
FT ECO:0000269|PubMed:22939182"
SQ SEQUENCE 227 AA; 24704 MW; 4C40FEA0278E64BF CRC64;
MSKEIPTPYM WSYQPQMGLA AGAAQDYSTR INYMSAGPHM ISRVNGIRAH RNRILLEQAA
ITTTPRNNLN PRSWPAALVY QESPAPTTVV LPRDAQAEVQ MTNSGAQLAG GFRHRVRSPG
QGITHLKIRG RGIQLNDESV SSSLGLRPDG TFQIGGAGRS SFTPRQAILT LQTSSSEPRS
GGIGTLQFIE EFVPSVYFNP FSGPPGHYPD QFIPNFDAVK DSADGYD
