CAP6_ADEG1
ID CAP6_ADEG1 Reviewed; 223 AA.
AC Q64757;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 23-FEB-2022, entry version 86.
DE RecName: Full=Pre-protein VI {ECO:0000255|HAMAP-Rule:MF_04048};
DE Short=pVI {ECO:0000255|HAMAP-Rule:MF_04048};
DE Contains:
DE RecName: Full=Endosome lysis protein {ECO:0000255|HAMAP-Rule:MF_04048};
DE Contains:
DE RecName: Full=Protease cofactor {ECO:0000255|HAMAP-Rule:MF_04048};
DE AltName: Full=pVI-C {ECO:0000255|HAMAP-Rule:MF_04048};
DE Flags: Precursor;
GN Name=L3 {ECO:0000255|HAMAP-Rule:MF_04048};
OS Fowl adenovirus A serotype 1 (strain CELO / Phelps) (FAdV-1) (Avian
OS adenovirus gal1 (strain Phelps)).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus A.
OX NCBI_TaxID=10553;
OH NCBI_TaxID=8976; Galliformes.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8627769; DOI=10.1128/jvi.70.5.2939-2949.1996;
RA Chiocca S., Kurzbauer R., Schaffner G., Baker A., Mautner V., Cotten M.;
RT "The complete DNA sequence and genomic organization of the avian adenovirus
RT CELO.";
RL J. Virol. 70:2939-2949(1996).
CC -!- FUNCTION: [Pre-protein VI]: During virus assembly, promotes hexon
CC trimers nuclear import through nuclear pore complexes via an importin
CC alpha/beta-dependent mechanism. By analogy to herpesviruses capsid
CC assembly, might act as a chaperone to promote the formation of the
CC icosahedral capsid. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- FUNCTION: [Endosome lysis protein]: Structural component of the virion
CC that provides increased stability to the particle shell through its
CC interaction with the core-capsid bridging protein and the hexon-linking
CC protein VIII. Fibers shedding during virus entry into host cell allows
CC the endosome lysis protein to be exposed as a membrane-lytic peptide.
CC Exhibits pH-independent membrane fragmentation activity and probably
CC mediates viral rapid escape from host endosome via organellar membrane
CC lysis. It is not clear if it then remains partially associated with the
CC capsid and involved in the intracellular microtubule-dependent
CC transport of capsid to the nucleus, or if it is lost during endosomal
CC penetration. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- FUNCTION: [Protease cofactor]: Cofactor that activates the viral
CC protease. Binds to viral protease in a 1:1 ratio. {ECO:0000255|HAMAP-
CC Rule:MF_04048}.
CC -!- SUBUNIT: [Pre-protein VI]: Interacts with hexon protein; this
CC interaction allows nuclear import of hexon trimers and possibly pre-
CC capsid assembly. Interacts (via C-terminal NLS) with importin
CC alpha/beta. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- SUBUNIT: [Endosome lysis protein]: Interacts (via PPxY motif) with host
CC NEDD4 ubiquitine ligase; this interaction might play a role in virus
CC intracellular transport during entry. Part of a complex composed of the
CC core-capsid bridging protein, the endosome lysis protein VI and the
CC hexon-linking protein VIII; these interactions bridge the virus core to
CC the capsid. Interacts with peripentonal hexons; this interaction
CC stabilizes the capsid by gluing two peripentonal hexons together and
CC joining them with an adjacent group-of-nine hexon. {ECO:0000255|HAMAP-
CC Rule:MF_04048}.
CC -!- SUBUNIT: [Protease cofactor]: Heterodimer with the viral protease;
CC disulfide-linked. Interacts with the viral protease.
CC {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- SUBCELLULAR LOCATION: [Pre-protein VI]: Host nucleus
CC {ECO:0000255|HAMAP-Rule:MF_04048}. Host cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_04048}. Note=Shuttles between host cytoplasm and nucleus.
CC {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- SUBCELLULAR LOCATION: [Endosome lysis protein]: Virion
CC {ECO:0000255|HAMAP-Rule:MF_04048}. Note=Associates with the base of
CC each peripentonal hexon on the capsid interior. Present in around 360
CC copies per virion. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- DOMAIN: N-terminal amphipathic alpha-helix domain is essential for the
CC membrane lytic activity. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle release. They can occur individually or in
CC close proximity within structural proteins. They interacts with sorting
CC cellular proteins of the multivesicular body (MVB) pathway. Most of
CC these proteins are class E vacuolar protein sorting factors belonging
CC to ESCRT-I, ESCRT-II or ESCRT-III complexes. Minor capsid protein 6
CC contains one L domain: a PPXY motif which binds to the WW domains of
CC HECT (homologous to E6-AP C-terminus) E3 ubiquitin ligases, like NEDD4.
CC In adenoviruses, this motif seems to play a role in microtubule-
CC dependent intracellular trafficking toward the nucleus during virus
CC entry into host cell and in suppression of DAXX-mediated repression of
CC the immediate early E1A promoter. {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- PTM: Ubiquitinated by Nedd4 following partial capsid disassembly; which
CC might play a role in intracellular virus movement during entry.
CC {ECO:0000255|HAMAP-Rule:MF_04048}.
CC -!- PTM: [Protease cofactor]: Contains the major nuclear import and export
CC signals. Proteolytically removed during virion maturation. The
CC processing of the C-terminus turns the precursor into a mature viral
CC structural protein and abrogates its ability to promote hexon import
CC and act as a potential chaperone protein. {ECO:0000255|HAMAP-
CC Rule:MF_04048}.
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_04048}.
CC -!- SIMILARITY: Belongs to the adenoviridae protein VI family.
CC {ECO:0000255|HAMAP-Rule:MF_04048}.
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DR EMBL; U46933; AAC54911.1; -; Genomic_DNA.
DR RefSeq; NP_043885.1; NC_001720.1.
DR GeneID; 1476562; -.
DR Proteomes; UP000001594; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0046729; C:viral procapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0039664; P:lysis of host organelle involved in viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04048; ADV_CAP6; 1.
DR InterPro; IPR004243; McpVI.
DR Pfam; PF02993; MCPVI; 1.
PE 3: Inferred from homology;
KW Capsid protein; Cytoplasmic inwards viral transport; Disulfide bond;
KW Host cytoplasm; Host nucleus; Host-virus interaction; Late protein;
KW Microtubular inwards viral transport; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Viral capsid assembly;
KW Viral penetration into host cytoplasm;
KW Viral penetration via lysis of host organellar membrane;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT CHAIN 1..223
FT /note="Pre-protein VI"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT /id="PRO_0000421432"
FT PROPEP 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT /id="PRO_0000036566"
FT CHAIN 29..212
FT /note="Endosome lysis protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT /id="PRO_0000036567"
FT PEPTIDE 213..223
FT /note="Protease cofactor"
FT /id="PRO_0000036568"
FT CHAIN 213..223
FT /note="Protease cofactor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT /id="PRO_0000439555"
FT REGION 29..53
FT /note="Amphipathic alpha-helix essential for membrane lytic
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT REGION 31..52
FT /note="Involved in endosomal membrane lysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT REGION 47..73
FT /note="Interaction with hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT REGION 136..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..212
FT /note="Interaction with hexon protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT REGION 213..223
FT /note="Binds to importin alpha/beta, involved in hexon
FT nuclear import"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT MOTIF 66..75
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT MOTIF 204..215
FT /note="Nuclear export signal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT COMPBIAS 139..155
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 28..29
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT SITE 212..213
FT /note="Cleavage; by viral protease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
FT DISULFID 222
FT /note="Interchain (with Adenovirus protease)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04048"
SQ SEQUENCE 223 AA; 23891 MW; C816C6DCD8A3BDA1 CRC64;
MDYAALSPHL GGWALRDHHI GDSSLRGGAI NWGNLGSRIT SALNSTGRWL YNTGNRFVHS
NTFNQIKQGI QDSGVIRNVA NLAGETLGAL TDIGRLKLQQ DLEKLRRKAL GEEGPATQAE
LQALIQALQA QVAAGEPPAA PAAPAPAPPL VPTTRPIPEM VTEVKPPVTS SAPAVPVDVP
TTLEMRPPPP KRRRKRARPG QWRARLDSLS GTGVATATRR MCY
