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Pre-protein VI (pVI) [Cleaved into: Endosome lysis protein; Protease cofactor (pVI-C)]

 CAP6_ADECR              Reviewed;         238 AA.
Q96686;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
22-NOV-2017, entry version 77.
RecName: Full=Pre-protein VI {ECO:0000255|HAMAP-Rule:MF_04048};
Short=pVI {ECO:0000255|HAMAP-Rule:MF_04048};
Contains:
RecName: Full=Endosome lysis protein {ECO:0000255|HAMAP-Rule:MF_04048};
Contains:
RecName: Full=Protease cofactor {ECO:0000255|HAMAP-Rule:MF_04048};
AltName: Full=pVI-C {ECO:0000255|HAMAP-Rule:MF_04048};
Name=L3 {ECO:0000255|HAMAP-Rule:MF_04048};
Canine adenovirus serotype 1 (strain RI261) (CAdV-1) (Canine
adenovirus 1 (strain RI261)).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus;
Canine mastadenovirus A.
NCBI_TaxID=69151;
NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=9129661;
Morrison M.D., Onions D.E., Nicolson L.;
"Complete DNA sequence of canine adenovirus type 1.";
J. Gen. Virol. 78:873-878(1997).
-!- FUNCTION: Pre-protein VI: During virus assembly, promotes hexon
trimers nuclear import through nuclear pore complexes via an
importin alpha/beta-dependent mechanism. By analogy to
herpesviruses capsid assembly, might act as a chaperone to promote
the formation of the icosahedral capsid. {ECO:0000255|HAMAP-
Rule:MF_04048}.
-!- FUNCTION: Endosome lysis protein: Structural component of the
virion that provides increased stability to the particle shell
through its interaction with the core-capsid bridging protein and
the hexon-linking protein VIII. Fibers shedding during virus entry
into host cell allows the endosome lysis protein to be exposed as
a membrane-lytic peptide. Exhibits pH-independent membrane
fragmentation activity and probably mediates viral rapid escape
from host endosome via organellar membrane lysis. It is not clear
if it then remains partially associated with the capsid and
involved in the intracellular microtubule-dependent transport of
capsid to the nucleus, or if it is lost during endosomal
penetration. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- FUNCTION: Protease cofactor: Cofactor that activates the viral
protease. Binds to viral protease in a 1:1 ratio.
{ECO:0000255|HAMAP-Rule:MF_04048}.
-!- SUBUNIT: Pre-protein VI: Interacts with hexon protein; this
interaction allows nuclear import of hexon trimers and possibly
pre-capsid assembly. Pre-protein VI: Interacts (via C-terminal
NLS) with importin alpha/beta. Endosome lysis protein: Interacts
(via PPxY motif) with host NEDD4 ubiquitine ligase; this
interaction might play a role in virus intracellular transport
during entry. Endosome lysis protein: Part of a complex composed
of the core-capsid bridging protein, the endosome lysis protein VI
and the hexon-linking protein VIII; these interactions bridge the
virus core to the capsid. Endosome lysis protein: Interacts with
peripentonal hexons; this interaction stabilizes the capsid by
gluing two peripentonal hexons together and joining them with an
adjacent group-of-nine hexon. Protease cofactor: Heterodimer with
the viral protease; disulfide-linked. Interacts with the viral
protease. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- SUBCELLULAR LOCATION: Pre-protein VI: Host nucleus
{ECO:0000255|HAMAP-Rule:MF_04048}. Host cytoplasm
{ECO:0000255|HAMAP-Rule:MF_04048}. Note=Shuttles between host
cytoplasm and nucleus. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- SUBCELLULAR LOCATION: Endosome lysis protein: Virion
{ECO:0000255|HAMAP-Rule:MF_04048}. Note=Associates with the base
of each peripentonal hexon on the capsid interior. Present in
around 360 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- INDUCTION: Expressed in the late phase of the viral replicative
cycle. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- DOMAIN: N-terminal amphipathic alpha-helix domain is essential for
the membrane lytic activity. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
essential for viral particle release. They can occur individually
or in close proximity within structural proteins. They interacts
with sorting cellular proteins of the multivesicular body (MVB)
pathway. Most of these proteins are class E vacuolar protein
sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III
complexes. Minor capsid protein 6 contains one L domain: a PPXY
motif which binds to the WW domains of HECT (homologous to E6-AP
C-terminus) E3 ubiquitin ligases, like NEDD4. In adenoviruses,
this motif seems to play a role in microtubule-dependent
intracellular trafficking toward the nucleus during virus entry
into host cell and in suppression of DAXX-mediated repression of
the immediate early E1A promoter. {ECO:0000255|HAMAP-
Rule:MF_04048}.
-!- PTM: Ubiquitinated by Nedd4 following partial capsid disassembly;
which might play a role in intracellular virus movement during
entry. {ECO:0000255|HAMAP-Rule:MF_04048}.
-!- PTM: Protease cofactor: Contains the major nuclear import and
export signals. Proteolytically removed during virion maturation.
The processing of the C-terminus turns the precursor into a mature
viral structural protein and abrogates its ability to promote
hexon import and act as a potential chaperone protein.
{ECO:0000255|HAMAP-Rule:MF_04048}.
-!- MISCELLANEOUS: All late proteins expressed from the major late
promoter are produced by alternative splicing and alternative
polyadenylation of the same gene giving rise to non-overlapping
ORFs. A leader sequence is present in the N-terminus of all these
mRNAs and is recognized by the viral shutoff protein to provide
expression although conventional translation via ribosome scanning
from the cap has been shut off in the host cell.
{ECO:0000255|HAMAP-Rule:MF_04048}.
-!- SIMILARITY: Belongs to the adenoviridae protein VI family.
{ECO:0000255|HAMAP-Rule:MF_04048}.
-----------------------------------------------------------------------
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EMBL; Y07760; CAA69065.1; -; Genomic_DNA.
RefSeq; AP_000058.1; AC_000003.1.
RefSeq; NP_044197.1; NC_001734.1.
SMR; Q96686; -.
GeneID; 1488930; -.
KEGG; vg:1488930; -.
KO; K21076; -.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0039664; P:lysis of host organelle involved in viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0075521; P:microtubule-dependent intracellular transport of viral material towards nucleus; IEA:UniProtKB-KW.
HAMAP; MF_04048; ADV_CAP6; 1.
InterPro; IPR004243; McpVI.
Pfam; PF02993; MCPVI; 1.
3: Inferred from homology;
Capsid protein; Cytoplasmic inwards viral transport; Disulfide bond;
Host cytoplasm; Host nucleus; Host-virus interaction; Late protein;
Microtubular inwards viral transport; Phosphoprotein; Ubl conjugation;
Viral capsid assembly; Viral penetration into host cytoplasm;
Viral penetration via lysis of host organellar membrane;
Viral release from host cell; Virion; Virus entry into host cell.
CHAIN 1 238 Pre-protein VI. {ECO:0000255|HAMAP-
Rule:MF_04048}.
/FTId=PRO_0000421431.
PROPEP 1 33 {ECO:0000255|HAMAP-Rule:MF_04048}.
/FTId=PRO_0000036563.
CHAIN 34 227 Endosome lysis protein.
{ECO:0000255|HAMAP-Rule:MF_04048}.
/FTId=PRO_0000036564.
CHAIN 228 238 Protease cofactor. {ECO:0000255|HAMAP-
Rule:MF_04048}.
/FTId=PRO_0000036565.
REGION 34 54 Amphipathic alpha-helix essential for
membrane lytic activity.
{ECO:0000255|HAMAP-Rule:MF_04048}.
REGION 36 53 Involved in endosomal membrane lysis.
{ECO:0000255|HAMAP-Rule:MF_04048}.
REGION 48 74 Interaction with hexon protein.
{ECO:0000255|HAMAP-Rule:MF_04048}.
REGION 105 213 Disordered. {ECO:0000255|HAMAP-
Rule:MF_04048}.
REGION 221 227 Interaction with hexon protein.
{ECO:0000255|HAMAP-Rule:MF_04048}.
REGION 228 238 Binds to importin alpha/beta, involved in
hexon nuclear import. {ECO:0000255|HAMAP-
Rule:MF_04048}.
MOTIF 67 76 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_04048}.
MOTIF 153 156 PPXY motif. {ECO:0000255|HAMAP-
Rule:MF_04048}.
MOTIF 219 230 Nuclear export signal.
{ECO:0000255|HAMAP-Rule:MF_04048}.
MOTIF 233 236 Nuclear localization signal.
{ECO:0000255|HAMAP-Rule:MF_04048}.
SITE 33 34 Cleavage; by viral protease.
{ECO:0000255|HAMAP-Rule:MF_04048}.
SITE 227 228 Cleavage; by viral protease.
{ECO:0000255|HAMAP-Rule:MF_04048}.
DISULFID 237 237 Interchain (with Adenovirus protease).
{ECO:0000255|HAMAP-Rule:MF_04048}.
SEQUENCE 238 AA; 26337 MW; F24503E83D14F054 CRC64;
MDAVNFSILA PRYGSHPMMS AWSGIGTSDM NGGAFNWGGI WSGIKNFGSN VKNWGSRAWN
SQTGKLLRQK LNDTKVREKL VEGISTGVHG ALDIANQEIA KQIERRLERQ QPLEPEVEEE
TVETKSEAKA PLVVEMPLKR PRDEDLVITA DEPPSYEETI KTMAPLVPMT RPHPSMARPV
IADRPTTLEL KPSDQPPPYS PQSSNMPVTA PVRSRGWQGT LANIVGVGLS NVKRRRCF


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