AC   MF_04131;
DC   Protein; auto
TR   HAMAP; MF_04131; -; 1; level=0
XX
Names: Rota_VP7_A
XX
ID   VP7
DE   RecName: Full=Outer capsid glycoprotein VP7;
DE   Flags: Precursor;
XX
CC   -!- FUNCTION: Calcium-binding protein that interacts with rotavirus cell
CC       receptors once the initial attachment by VP4 has been achieved.
CC       Rotavirus attachment and entry into the host cell probably involves
CC       multiple sequential contacts between the outer capsid proteins VP4 and
CC       VP7, and the cell receptors. Following entry into the host cell, low
CC       intracellular or intravesicular Ca(2+) concentration probably causes
CC       the calcium-stabilized VP7 trimers to dissociate from the virion. This
CC       step is probably necessary for the membrane-disrupting entry step and
CC       the release of VP4, which is locked onto the virion by VP7.
CC   -!- SUBUNIT: Homotrimer; disulfide-linked. 2 Ca(2+) ions bound at each
CC       subunit interface in the trimer hold the trimer together. Interacts
CC       with the intermediate capsid protein VP6. Interacts with the outer
CC       capsid protein VP5*.
CC   -!- SUBCELLULAR LOCATION: Virion. Host endoplasmic reticulum lumen.
CC       Note=The outer layer contains 780 copies of VP7, grouped as 260
CC       trimers. Immature double-layered particles assembled in the cytoplasm
CC       bud across the membrane of the endoplasmic reticulum, acquiring during
CC       this process a transient lipid membrane that is modified with the ER
CC       resident viral glycoproteins NSP4 and VP7; these enveloped particles
CC       also contain VP4. As the particles move towards the interior of the ER
CC       cisternae, the transient lipid membrane and the non-structural protein
CC       NSP4 are lost, while the virus surface proteins VP4 and VP7 rearrange
CC       to form the outermost virus protein layer, yielding mature infectious
CC       triple-layered particles.
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: The N-terminus is blocked possibly by pyroglutamic acid.
CC   -!- MISCELLANEOUS: Some rotavirus strains are neuraminidase-sensitive and
CC       require sialic acid to attach to the cell surface. Some rotavirus
CC       strains are integrin-dependent. Some rotavirus strains depend on
CC       ganglioside for their entry into the host cell. Hsp70 also seems to be
CC       involved in the entry of some strains.
CC   -!- MISCELLANEOUS: In group A rotaviruses, VP7 defines the G serotype.
CC   -!- SIMILARITY: Belongs to the rotavirus VP7 family.
XX
DR   Pfam; PF00434; VP7; 1; trigger=no
DR   General; Signal; -; 1; trigger=no
XX
KW   Calcium
KW   Capsid protein
KW   Disulfide bond
KW   Glycoprotein
KW   Host endoplasmic reticulum
KW   Host-virus interaction
KW   Metal-binding
KW   Outer capsid protein
KW   Signal
KW   T=13 icosahedral capsid protein
KW   Virion
XX
GO   GO:0044166; C:host cell endoplasmic reticulum lumen
GO   GO:0039621; C:T=13 icosahedral viral capsid
GO   GO:0039624; C:viral outer capsid
XX
FT   From: VP7_ROTSH (A2T3P5)
FT   SIGNAL          Nter..50
FT   CHAIN           51..Cter
FT                   /note="Outer capsid glycoprotein VP7"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   Condition: D
FT   BINDING         206
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   Condition: G
FT   BINDING         214
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   Condition: [TS]
FT   BINDING         216
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT   Condition: E
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Condition: Q
FT   BINDING         228
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         229
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Condition: V
FT   BINDING         231
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Condition: D
FT   BINDING         301
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT   Condition: D
FT   DISULFID        82..135
FT   Condition: C-x*-C
FT   DISULFID        165..249
FT   Condition: C-x*-C
FT   DISULFID        191..244
FT   Condition: C-x*-C
FT   DISULFID        196..207
FT   Condition: C-x*-C
FT   REGION          237..239
FT                   /note="LVD motif; interaction with ITGA4/ITGB1 heterodimer"
FT   Condition: L-D-V
FT   REGION          253..255
FT                   /note="GPR motif; interaction with ITGAX/ITGB2"
FT   Condition: G-P-R
FT   REGION          165..167
FT                   /note="CNP motif; interaction with ITGAV/ITGB3"
FT   Condition: C-N-P
XX
Size: 300-331;
Related: None;
Template: A2T3P5; P12476; Q86515; P03533;
Scope:
 Viruses; Rotavirus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.6 2022/11/19
//