ID   CAP8_ADE05              Reviewed;         227 AA.
AC   P24936;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   24-JAN-2024, entry version 83.
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 5 (HAdV-5) (Human adenovirus 5).
OC   Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC   Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus C.
OX   NCBI_TaxID=28285;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA   Chroboczek J., Bieber F., Jacrot B.;
RT   "The sequence of the genome of adenovirus type 5 and its comparison with
RT   the genome of adenovirus type 2.";
RL   Virology 186:280-285(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=23142869; DOI=10.1038/nmeth.2227;
RA   Evans V.C., Barker G., Heesom K.J., Fan J., Bessant C., Matthews D.A.;
RT   "De novo derivation of proteomes from transcriptomes for transcript and
RT   protein identification.";
RL   Nat. Methods 9:1207-1211(2012).
RN   [3]
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).
RN   [4]
RP   STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE VIRAL PARTICLE, AND
RP   PROTEOLYTIC CLEAVAGE BY VIRAL PROTEASE.
RX   PubMed=17005667; DOI=10.1128/jvi.01652-06;
RA   Saban S.D., Silvestry M., Nemerow G.R., Stewart P.L.;
RT   "Visualization of alpha-helices in a 6-angstrom resolution cryoelectron
RT   microscopy structure of adenovirus allows refinement of capsid protein
RT   assignments.";
RL   J. Virol. 80:12049-12059(2006).
RN   [5]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.6 ANGSTROMS) OF THE VIRAL PARTICLE,
RP   PROTEOLYTIC CLEAVAGE BY VIRAL PROTEASE, AND INTERACTION WITH THE HEXON
RP   PROTEIN.
RX   PubMed=20798312; DOI=10.1126/science.1187433;
RA   Liu H., Jin L., Koh S.B., Atanasov I., Schein S., Wu L., Zhou Z.H.;
RT   "Atomic structure of human adenovirus by cryo-EM reveals interactions among
RT   protein networks.";
RL   Science 329:1038-1043(2010).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=20798318; DOI=10.1126/science.1187292;
RA   Reddy V.S., Natchiar S.K., Stewart P.L., Nemerow G.R.;
RT   "Crystal structure of human adenovirus at 3.5 A resolution.";
RL   Science 329:1071-1075(2010).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS), IDENTIFICATION IN A COMPLEX WITH
RP   ENDOSOME LYSIS PROTEIN VI AND HEXON-LINKING PROTEIN VIII, INTERACTION WITH
RP   THE HEXON PROTEIN, PROTEOLYTIC CLEAVAGE BY VIRAL PROTEASE, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=25071205; DOI=10.1073/pnas.1408462111;
RA   Reddy V.S., Nemerow G.R.;
RT   "Structures and organization of adenovirus cement proteins provide insights
RT   into the role of capsid maturation in virus entry and infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:11715-11720(2014).
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, ECO:0000269|PubMed:25071205}.
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, ECO:0000269|PubMed:25071205}.
CC   -!- SUBUNIT: Interacts with the peripentonal hexons as well as the hexons
CC       in the facets (PubMed:20798312, PubMed:25071205). Part of a complex
CC       composed of the core-capsid bridging protein, the endosome lysis
CC       protein VI and the hexon-linking protein VIII; these interactions
CC       bridge the virus core to the capsid (PubMed:25071205).
CC       {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:20798312,
CC       ECO:0000269|PubMed:25071205}.
CC   -!- SUBCELLULAR LOCATION: [Hexon-linking protein-C]: Virion
CC       {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}.
CC       Note=Located on the inner side of the capsid shell. Present in 120
CC       copies per virion. {ECO:0000255|HAMAP-Rule:MF_04049,
CC       ECO:0000269|PubMed:25071205}.
CC   -!- SUBCELLULAR LOCATION: [Pre-hexon-linking protein VIII]: Host nucleus
CC       {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: [Hexon-linking protein-N]: Virion
CC       {ECO:0000255|HAMAP-Rule:MF_04049, ECO:0000269|PubMed:25071205}.
CC       Note=Located on the inner side of the capsid shell. Present in 120
CC       copies per virion. {ECO:0000255|HAMAP-Rule:MF_04049,
CC       ECO:0000269|PubMed:25071205}.
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, ECO:0000269|PubMed:17005667,
CC       ECO:0000269|PubMed:20798312, ECO:0000269|PubMed:25071205}.
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}.
CC   -!- CAUTION: An interaction between hexon-linking protein IIIa and hexon-
CC       linking protein VIII as been described in PubMed:20798312. However, the
CC       subcellular location of hexon-linking protein IIIa was incorrectly
CC       assigned to the capsid interior. {ECO:0000305}.
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DR   EMBL; M73260; AAA96413.1; -; Genomic_DNA.
DR   PIR; E39449; SXAD85.
DR   RefSeq; AP_000217.1; AC_000008.1.
DR   PDB; 6B1T; EM; 3.20 A; O/P=1-227.
DR   PDB; 6CGV; X-ray; 3.80 A; U/V=1-227.
DR   PDB; 7S78; EM; 3.72 A; U/V=1-227.
DR   PDBsum; 6B1T; -.
DR   PDBsum; 6CGV; -.
DR   PDBsum; 7S78; -.
DR   EMDB; EMD-24881; -.
DR   EMDB; EMD-7034; -.
DR   SMR; P24936; -.
DR   IntAct; P24936; 1.
DR   EvolutionaryTrace; P24936; -.
DR   Proteomes; UP000004992; 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   Gene3D; 6.10.250.1460; -; 1.
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   3D-structure; Capsid protein; Host nucleus; Late protein; Phosphoprotein;
KW   Virion.
FT   CHAIN           1..227
FT                   /note="Pre-hexon-linking protein VIII"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000421131"
FT   PEPTIDE         1..111
FT                   /note="Hexon-linking protein-N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000036495"
FT   PROPEP          112..157
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000421132"
FT   PEPTIDE         158..227
FT                   /note="Hexon-linking protein-C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT                   /id="PRO_0000036496"
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   MOD_RES         118
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT   MOD_RES         174
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04049"
FT   CONFLICT        160
FT                   /note="P -> S (in Ref. 2; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
FT   HELIX           40..43
FT                   /evidence="ECO:0007829|PDB:6CGV"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:6CGV"
FT   HELIX           51..57
FT                   /evidence="ECO:0007829|PDB:6CGV"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:6CGV"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:6CGV"
SQ   SEQUENCE   227 AA;  24687 MW;  C1CACF31E6F5E5D5 CRC64;
     MSKEIPTPYM WSYQPQMGLA AGAAQDYSTR INYMSAGPHM ISRVNGIRAH RNRILLEQAA
     ITTTPRNNLN PRSWPAALVY QESPAPTTVV LPRDAQAEVQ MTNSGAQLAG GFRHRVRSPG
     QGITHLTIRG RGIQLNDESV SSSLGLRPDG TFQIGGAGRP SFTPRQAILT LQTSSSEPRS
     GGIGTLQFIE EFVPSVYFNP FSGPPGHYPD QFIPNFDAVK DSADGYD
//