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Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]

 A0A2H4ZSW2_9REOV        Unreviewed;       749 AA.
A0A2H4ZSW2;
28-FEB-2018, integrated into UniProtKB/TrEMBL.
28-FEB-2018, sequence version 1.
02-JUN-2021, entry version 14.
RecName: Full=Outer capsid protein VP4 {ECO:0000256|HAMAP-Rule:MF_04125};
AltName: Full=Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04125};
Contains:
RecName: Full=Outer capsid protein VP8* {ECO:0000256|HAMAP-Rule:MF_04125};
Contains:
RecName: Full=Outer capsid protein VP5* {ECO:0000256|HAMAP-Rule:MF_04125};
Name=VP4 {ECO:0000313|EMBL:AUG45005.1};
Rotavirus B.
Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
NCBI_TaxID=28876 {ECO:0000313|EMBL:AUG45005.1};
[1] {ECO:0000313|EMBL:AUG45005.1}
NUCLEOTIDE SEQUENCE.
STRAIN=RVB/Pig-wt/USA/IL5/2012 {ECO:0000313|EMBL:AUG45005.1};
Herrera-Ibata D.M., Poulsen E., Hesse R., Bai J., Marthaler D.;
"Full genome classification and phylogenetic analyses of Rotavirus B
strains detected in the United States.";
Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Outer capsid protein VP4: Spike-forming protein that mediates
virion attachment to the host epithelial cell receptors and plays a
major role in cell penetration, determination of host range restriction
and virulence. Rotavirus attachment and entry into the host cell
probably involves multiple sequential contacts between the outer capsid
proteins VP4 and VP7, and the cell receptors. It is subsequently lost,
together with VP7, following virus entry into the host cell. Following
entry into the host cell, low intracellular or intravesicular Ca(2+)
concentration probably causes the calcium-stabilized VP7 trimers to
dissociate from the virion. This step is probably necessary for the
membrane-disrupting entry step and the release of VP4, which is locked
onto the virion by VP7. {ECO:0000256|HAMAP-Rule:MF_04125}.
-!- FUNCTION: Outer capsid protein VP5*: Forms the spike 'foot' and 'body'
and acts as a membrane permeabilization protein that mediates release
of viral particles from endosomal compartments into the cytoplasm.
During entry, the part of VP5* that protrudes from the virus folds back
on itself and reorganizes from a local dimer to a trimer. This
reorganization may be linked to membrane penetration.
{ECO:0000256|HAMAP-Rule:MF_04125}.
-!- FUNCTION: Outer capsid protein VP8*: Forms the head of the spikes and
mediates the recognition of specific host cell surface glycans. It is
the viral hemagglutinin and an important target of neutralizing
antibodies. {ECO:0000256|HAMAP-Rule:MF_04125}.
-!- SUBUNIT: Outer capsid protein VP4: Homotrimer. VP4 adopts a dimeric
appearance above the capsid surface, while forming a trimeric base
anchored inside the capsid layer. Only hints of the third molecule are
observed above the capsid surface. It probably performs a series of
molecular rearrangements during viral entry. Prior to trypsin cleavage,
it is flexible. The priming trypsin cleavage triggers its rearrangement
into rigid spikes with approximate two-fold symmetry of their
protruding parts. After an unknown second triggering event, cleaved VP4
may undergo another rearrangement, in which two VP5* subunits fold back
on themselves and join a third subunit to form a tightly associated
trimer, shaped like a folded umbrella. Outer capsid protein VP4:
Interacts with VP6. Outer capsid protein VP4: Interacts with VP7. Outer
capsid protein VP5*: Homotrimer. The trimer is coiled-coil stabilized
by its C-terminus, however, its N-terminus, known as antigen domain or
'body', seems to be flexible allowing it to self-associate either as a
dimer or a trimer. {ECO:0000256|HAMAP-Rule:MF_04125}.
-!- SUBCELLULAR LOCATION: [Outer capsid protein VP5*]: Virion
{ECO:0000256|HAMAP-Rule:MF_04125}. Note=Outer capsid protein.
{ECO:0000256|HAMAP-Rule:MF_04125}.
-!- SUBCELLULAR LOCATION: [Outer capsid protein VP8*]: Virion
{ECO:0000256|HAMAP-Rule:MF_04125}. Note=Outer capsid protein.
{ECO:0000256|HAMAP-Rule:MF_04125}.
-!- SUBCELLULAR LOCATION: [Outer capsid protein VP4]: Virion
{ECO:0000256|HAMAP-Rule:MF_04125}. Host rough endoplasmic reticulum
{ECO:0000256|HAMAP-Rule:MF_04125}. Host cell membrane
{ECO:0000256|HAMAP-Rule:MF_04125}. Host endoplasmic reticulum-Golgi
intermediate compartment {ECO:0000256|HAMAP-Rule:MF_04125}. Note=The
outer layer contains 180 copies of VP4, grouped as 60 dimers. Immature
double-layered particles assembled in the cytoplasm bud across the
membrane of the endoplasmic reticulum, acquiring during this process a
transient lipid membrane that is modified with the ER resident viral
glycoproteins NSP4 and VP7; these enveloped particles also contain VP4.
As the particles move towards the interior of the ER cisternae, the
transient lipid membrane and the non-structural protein NSP4 are lost,
while the virus surface proteins VP4 and VP7 rearrange to form the
outermost virus protein layer, yielding mature infectious triple-
layered particles. {ECO:0000256|HAMAP-Rule:MF_04125}.
-!- DOMAIN: Outer capsid protein VP4: The VP4 spike is divided into a foot,
a stalk and body, and a head. {ECO:0000256|HAMAP-Rule:MF_04125}.
-!- PTM: Outer capsid protein VP4: Proteolytic cleavage by trypsin results
in activation of VP4 functions and greatly increases infectivity. The
penetration into the host cell is dependent on trypsin treatment of
VP4. It produces two peptides, VP5* and VP8* that remain associated
with the virion. Cleavage of VP4 by trypsin probably occurs in vivo in
the lumen of the intestine prior to infection of enterocytes. Trypsin
seems to be incorporated into the three-layered viral particles but
remains inactive as long as the viral outer capsid is intact and would
only be activated upon the solubilization of the latter.
{ECO:0000256|HAMAP-Rule:MF_04125}.
-!- SIMILARITY: Belongs to the rotavirus VP4 family. {ECO:0000256|HAMAP-
Rule:MF_04125}.
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; MG272139; AUG45005.1; -; Genomic_RNA.
GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0044168; C:host cell rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0039624; C:viral outer capsid; IEA:UniProtKB-UniRule.
GO; GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-UniRule.
GO; GO:0099008; P:viral entry via permeabilization of inner membrane; IEA:UniProtKB-KW.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
HAMAP; MF_04125; Rota_VP4; 1.
InterPro; IPR000253; FHA_dom.
InterPro; IPR042546; Rota_A_VP4.
InterPro; IPR038017; Rota_VP4_MID_sf.
SUPFAM; SSF111379; SSF111379; 1.
PROSITE; PS50006; FHA_DOMAIN; 1.
3: Inferred from homology;
Capsid protein {ECO:0000256|ARBA:ARBA00022770, ECO:0000256|HAMAP-
Rule:MF_04125};
Cleavage on pair of basic residues {ECO:0000256|HAMAP-Rule:MF_04125};
Coiled coil {ECO:0000256|HAMAP-Rule:MF_04125};
Hemagglutinin {ECO:0000256|HAMAP-Rule:MF_04125};
Host cell membrane {ECO:0000256|HAMAP-Rule:MF_04125};
Host endoplasmic reticulum {ECO:0000256|HAMAP-Rule:MF_04125};
Host membrane {ECO:0000256|HAMAP-Rule:MF_04125};
Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04125};
Membrane {ECO:0000256|HAMAP-Rule:MF_04125};
Outer capsid protein {ECO:0000256|ARBA:ARBA00022770, ECO:0000256|HAMAP-
Rule:MF_04125};
Viral attachment to host cell {ECO:0000256|HAMAP-Rule:MF_04125};
Viral penetration into host cytoplasm {ECO:0000256|ARBA:ARBA00022648,
ECO:0000256|HAMAP-Rule:MF_04125};
Viral penetration via permeabilization of host membrane
{ECO:0000256|ARBA:ARBA00022648, ECO:0000256|HAMAP-Rule:MF_04125};
Virion {ECO:0000256|ARBA:ARBA00022770, ECO:0000256|HAMAP-Rule:MF_04125};
Virus entry into host cell {ECO:0000256|ARBA:ARBA00022648,
ECO:0000256|HAMAP-Rule:MF_04125}.
CHAIN 1..749
/note="Outer capsid protein VP4"
/evidence="ECO:0000256|HAMAP-Rule:MF_04125"
/id="PRO_5023396931"
CHAIN 1..199
/note="Outer capsid protein VP8*"
/evidence="ECO:0000256|HAMAP-Rule:MF_04125"
/id="PRO_5023396930"
CHAIN 215..749
/note="Outer capsid protein VP5*"
/evidence="ECO:0000256|HAMAP-Rule:MF_04125"
/id="PRO_5023396929"
DOMAIN 63..118
/note="FHA"
/evidence="ECO:0000259|PROSITE:PS50006"
REGION 13..34
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COILED 487..514
/evidence="ECO:0000256|HAMAP-Rule:MF_04125"
COMPBIAS 17..34
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
SITE 199..200
/note="Cleavage"
/evidence="ECO:0000256|HAMAP-Rule:MF_04125"
SITE 214..215
/note="Cleavage"
/evidence="ECO:0000256|HAMAP-Rule:MF_04125"
SEQUENCE 749 AA; 85408 MW; 67331B3AE43A3314 CRC64;
MLSYLRREWQ SYGENATNVK EEEDTMSDKK KESKIEKPIK TENRYCYKSP QKIDKYESDL
QGFSLGTQDE HINPTTLQIY DGVLTNGHTF ISTNPPCSTI FELSIKAENG AMVDGKPLTD
FSCFVISITK DENGVCDITY HCQSDLDDAQ KRILLRGFSN KGCSGLNDVK INSILRVVDK
ALGSEFHTRT QASLYTWDRD CVESYSTKVR VDERKVGNSR MIIYQQEEGF WKILTETIWI
DLRAVFKPYG IMGGAFKNWL VDSGFDKYEH QYSYEREGKM VSATTITYPK PTGKAGVNQP
WRPATDYNGQ YVCLQPGDTF SVWYFEDQWQ IRNAIYAKNF QSDTMAEGTL ENKGQLIFKM
NYIPSLANIK NKQGKVQYRY INGGFAQVDA SSYTGMALIF NFECIGKKFY TEDYKTKIDN
SITPYICFIG KNYTPDGYFY EKGCCSGFAA GYDTETISHK MTISYTVMRP SDPDFVTGGD
AYGQSITSSL EVSMRNLQDQ INSIRAELNI SQVTSAVLSA ITSLGDLPNL FSNITQIYSK
LKDALSKLKI KKSKPKPIKA TMIVDRNTVD VPNVSIMNRM PEELEVGIIY NSMRNTKKHD
ISKFALSTEL ELPYIQTTST LTPKFTKYLE QKGLLTVDDI AVQFDPLNTT FSTLRRKNAE
IMRYKIDPEV AHEVLSQMSN SATRSLFSLN VRKQISTHNE FSTPTYEQLI NRILNDKEIL
DVLGKLNPHS VGNMFQEFVD RMQDMLSYY


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WP1675: Nitrogen metabolism
WP813: G Protein Signaling Pathways
WP1685: Peptidoglycan biosynthesis
WP1616: ABC transporters
WP2199: Seed Development
WP1644: DNA replication
WP2272: Pathogenic Escherichia coli infection
WP1692: Protein export
WP1700: Selenoamino acid metabolism
WP1657: Glycerolipid metabolism
WP2324: AGE/RAGE pathway
WP1663: Homologous recombination
WP35: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways

Related Genes :
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[VP4] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]
[] Outer capsid protein VP4 (Hemagglutinin) [Cleaved into: Outer capsid protein VP8*; Outer capsid protein VP5*]

Bibliography :