AC   MF_04127;
DC   Protein; auto
TR   HAMAP; MF_04127; -; 1; level=0
XX
Names: Rota_VP2_A
XX
ID   VP2
DE   RecName: Full=Inner capsid protein VP2;
XX
CC   -!- FUNCTION: Inner capsid protein that self-assembles to form an
CC       icosahedral capsid with a T=2 symmetry, which consists of 120 copies of
CC       VP2, with channels at each of its five-fold vertices. This capsid
CC       constitutes the innermost concentric layer of the viral mature
CC       particle. It encapsidates the polymerase VP1, the capping enzyme VP3
CC       and the genomic dsRNA, thereby defining the core. The innermost VP2
CC       capsid and the intermediate VP6 capsid remain intact following cell
CC       entry to protect the dsRNA from degradation and to prevent unfavorable
CC       antiviral responses in the host cell during all the replication cycle
CC       of the virus. Nascent transcripts are transcribed within the structural
CC       confines of this double-layered particle (DLP) and are extruded through
CC       the channels formed by VP2 N-termini. VP2 is required for the replicase
CC       activity of VP1 polymerase. Probably recruits a copy of a VP1-VP3
CC       complex, potentially along with a segment of plus-strand RNA, as a
CC       decamer of VP2 assembles. May activate the autoinhibited VP1/RNA
CC       complex to coordinate packaging and genome replication.
CC   -!- SUBUNIT: Homodecamer; each decamer is made up of two conformers of VP2,
CC       called VP2A and VP2B. Interacts with a VP1-VP3 complex. Interacts with
CC       the intermediate capsid protein VP6. Interacts with NSP5. Interacts
CC       (via N-terminus) with NSP2.
CC   -!- SUBCELLULAR LOCATION: Virion. Note=Inner capsid protein. Also found in
CC       spherical cytoplasmic structures, called virus factories, that appear
CC       early after infection and are the site of viral replication and
CC       packaging.
CC   -!- DOMAIN: The N-terminus binds RNA. It is necessary for encapsidation of
CC       VP1 and VP3. The N-termini of 10 VP2 molecules form a cylindrical hub
CC       underneath each 5-fold axis of the inner capsid.
CC   -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins
CC       seems to have a positive role on viral replication.
CC   -!- SIMILARITY: Belongs to the rotavirus VP2 family.
XX
DR   Pfam; PF05087; Rota_VP2; 1; trigger=no
DR   General; Coiled_coil; -; 0-unlimited; trigger=no
XX
KW   Capsid protein
KW   Inner capsid protein
KW   Repeat
KW   RNA-binding
KW   T=2 icosahedral capsid protein
KW   Virion
KW   Ubl conjugation
XX
GO   GO:0039625; C:viral inner capsid
GO   GO:0019013; C:viral nucleocapsid
GO   GO:0003723; F:RNA binding
GO   GO:0039616; C:T=2 icosahedral viral capsid
XX
FT   From: VP2_ROTRF (P12472)
FT   REGION          Nter..80
FT                   /note="5-fold hub; involved in the encapsidation of VP1 and
FT                   VP3"
FT   REGION          394..414
FT                   /note="Hydrophobic"
FT   REGION          422..442
FT                   /note="Hydrophobic"
FT   SITE            220
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT   Condition: A
FT   SITE            224
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT   Condition: F
FT   SITE            228
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT   Condition: M
FT   SITE            839
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT   Condition: M
FT   SITE            841
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT   Condition: M
XX
Size: 872-973;
Related: MF_04123;
Template: P12472; A2T3R5; P17462;
Scope:
 Viruses; Rotavirus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.4 2021/11/10
//