CAP8_ADE12
ID CAP8_ADE12 Reviewed; 233 AA.
AC P36713;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 02-JUN-2021, entry version 66.
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 A serotype 12 (HAdV-12) (Human adenovirus 12).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus A.
OX NCBI_TaxID=28282;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8254750; DOI=10.1128/jvi.68.1.379-389.1994;
RA Sprengel J., Schmitz B., Heuss-Neitzel D., Zock C., Doerfler W.;
RT "Nucleotide sequence of human adenovirus type 12 DNA: comparative
RT functional analysis.";
RL J. Virol. 68:379-389(1994).
RN [2]
RP PROTEIN SEQUENCE OF 139-155 AND 164-178.
RC STRAIN=Huie;
RX PubMed=8438575; DOI=10.1006/viro.1993.1131;
RA Freimuth P., Anderson C.W.;
RT "Human adenovirus serotype 12 virion precursors pMu and pVI are cleaved at
RT amino-terminal and carboxy-terminal sites that conform to the adenovirus 2
RT endoproteinase cleavage consensus sequence.";
RL Virology 193:348-355(1993).
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; X73487; CAA51895.1; -; Genomic_DNA.
DR PIR; S33946; S33946.
DR RefSeq; NP_040928.1; NC_001460.1.
DR SMR; P36713; -.
DR DNASU; 1460842; -.
DR GeneID; 1460842; -.
DR Proteomes; UP000004993; 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; Virion.
FT CHAIN 1..233
FT /note="Pre-hexon-linking protein VIII"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421397"
FT PEPTIDE 1..111
FT /note="Hexon-linking protein-N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000421398"
FT PROPEP 112..163
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT /id="PRO_0000036497"
FT PEPTIDE 164..233
FT /note="Hexon-linking protein-C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000305"
FT /id="PRO_0000036498"
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; 25254 MW; 63111557E3D83CAF CRC64;
MSKDIPTPYM WSFQPQMGLA AGAAQDYSSK MNWLSAGPHM ISRVNGVRAR RNQILLEQAA
LTATPRNQLN PPSWPAALIY QENPPPTTVL LPRDAQAEVH MTNAGAQLAG GARHSFRYKG
RTEPYPSPAI KRVLIRGKGI QLNDEVTSPL GVRPDGVFQL GGSGRSSFTA RQAYLTLQSS
SSAPRSGGIG TLQFVEEFTP SVYFNPFSGS PGHYPDAFIP NFDAVSESVD GYD
