VP2_ROTHT
ID VP2_ROTHT Reviewed; 890 AA.
AC B1NKT8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 02-JUN-2021, entry version 35.
DE RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS Rotavirus A (strain RVA/Human/United Kingdom/ST3/1975/G4P2A[6]) (RV-A)
OS (Rotavirus A (strain St. Thomas 3)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10960;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=18216098; DOI=10.1128/jvi.02257-07;
RA Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T.,
RA McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T.,
RA Rahman M., Van Ranst M.;
RT "Full genome-based classification of rotaviruses reveals a common origin
RT between human Wa-Like and porcine rotavirus strains and human DS-1-like and
RT bovine rotavirus strains.";
RL J. Virol. 82:3204-3219(2008).
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 {ECO:0000255|HAMAP-Rule:MF_04127}.
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. {ECO:0000255|HAMAP-Rule:MF_04127}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04127}.
CC Note=Inner capsid protein. Also found in spherical cytoplasmic
CC structures, called virus factories, that appear early after infection
CC and are the site of viral replication and packaging.
CC {ECO:0000255|HAMAP-Rule:MF_04127}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_04127}.
CC -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral proteins
CC seems to have a positive role on viral replication. {ECO:0000255|HAMAP-
CC Rule:MF_04127}.
CC -!- SIMILARITY: Belongs to the rotavirus VP2 family. {ECO:0000255|HAMAP-
CC Rule:MF_04127}.
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DR EMBL; EF583046; ABU87855.1; -; Genomic_RNA.
DR SMR; B1NKT8; -.
DR Proteomes; UP000007048; Genome.
DR GO; GO:0039616; C:T=2 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0039625; C:viral inner capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04123; Rota_VP2; 1.
DR HAMAP; MF_04127; Rota_VP2_A; 1.
DR InterPro; IPR007779; Rotavirus_VP2.
DR Pfam; PF05087; Rota_VP2; 1.
PE 3: Inferred from homology;
KW Capsid protein; Inner capsid protein; Repeat; RNA-binding;
KW T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT CHAIN 1..890
FT /note="Inner capsid protein VP2"
FT /id="PRO_0000368061"
FT REGION 1..88
FT /note="5-fold hub; involved in the encapsidation of VP1 and
FT VP3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..424
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT REGION 432..452
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT COMPBIAS 1..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 232
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 236
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 849
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 851
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ SEQUENCE 890 AA; 103836 MW; 70928736823562C0 CRC64;
MAYRKRGAKR ENLPQQNERL QEKEIENNTD VTMENKNNNR KQQLSDKVLS QKEEIITDVQ
DDIKIADEVK KSSKEESKQL LEILKTKEDH QKEVQYEILQ KTIPTFEPKE SILKKIEDIR
PEQAKKQMKL FRIFEPRQLP IYRANGEKEL RNRWYWKLKK DTLPDGDYDV REYFLNLYDQ
ILIEMPDYLL LKDMAVENKN SRDAGKVVDS ETASICDAIF QDEETEGVIR RFIADMRQQV
QADRNIVNYP SILHPIDHAF NEYFLNHQLV EPLNNEIIFN YIPERIRNDV NYILNMDMNL
PSTARYIRPN LLQDRLNLHD NFESLWDTIT TSNYILARSV VPDLKEKELV STEAQIQKMS
QDLQLEALTI QSETQFLAGI NSQAANDCFK TLIAAMLSQR TMSLDFVTTN YMSLISGMWL
LTVIPNDMFL RESLVACELA IINTIVYPAF GMQRMHYRNG DPQTPFQIAE QQIQNFQVAN
WLHFINNNRF RQVVIDGVLN QTLNDNIRNG QVINQLMEAL MQLSRQQFPT MPVDYKRSIQ
RGILLLSNRL GQLVDLTRLL SYNYETLMAC ITMNMQHVQT LTTEKLQLTS VTSLCMLIGN
TTVIPSPQTL FHYYNVNVNF HSNYNERIND AVAIITAANR LNLYQKKMKS IVEDFLKRLQ
IFDVPRVPDD QMYRLRDRLR LLPVERRRLD IFNLILMNME QIERASDKIA QGVIIAYRDM
QLERDEMYGF VNITRSLDGY QQINLEELMR TGDYGQITNM LLNNQPVALV GALPFVTDSS
VISLIAKLDA TVFAQIVKLR KVDTLKPILY KINSDSNDFY LVANYDWIPT STTKVYKQVP
QPFDFRASMH MLTSNLTFTV YSDLLSFVSA DTVEPINAIA FDNMRIMNEL
