ID   VP2_ROTSR               Reviewed;         882 AA.
AC   Q86218;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 52.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/SA11-Ramig/G3P[X]) (RV-A) (Simian Agent 11 (strain
OS   Ramig)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=36435;
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8091686; DOI=10.1006/viro.1994.1511;
RA   Mansell E.A., Ramig R.F., Patton J.T.;
RT   "Temperature-sensitive lesions in the capsid proteins of the rotavirus
RT   mutants tsF and tsG that affect virion assembly.";
RL   Virology 204:69-81(1994).
RN   [2]
RP   INTERACTION WITH NSP2.
RX   PubMed=25165107; DOI=10.1128/jvi.02251-14;
RA   Viskovska M., Anish R., Hu L., Chow D.C., Hurwitz A.M., Brown N.G.,
RA   Palzkill T., Estes M.K., Prasad B.V.;
RT   "Probing the sites of interactions of rotaviral proteins involved in
RT   replication.";
RL   J. Virol. 88:12866-12881(2014).
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 (By
CC       similarity). Interacts (via N-terminus) with NSP2 (PubMed:25165107).
CC       {ECO:0000255|HAMAP-Rule:MF_04127, ECO:0000269|PubMed:25165107}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L33364; AAA47349.1; -; Genomic_RNA.
DR   SMR; Q86218; -.
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   1: Evidence at protein level;
KW   Capsid protein; Inner capsid protein; Repeat; RNA-binding;
KW   T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT   CHAIN           1..882
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000368065"
FT   REGION          1..82
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..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..416
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   REGION          424..444
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   SITE            222
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            226
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            230
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            841
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            843
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ   SEQUENCE   882 AA;  102669 MW;  8221C2211B35681D CRC64;
     MAYRKRGARR ETNLKQDERM QEKEDSKNIN NDSPKSQLSE KVLSKKEEII TDNQEEVKIS
     DEVKKSNKEE SKQLLEVLKT KEEHQKEVQY EILQKTIPTF EPKESILKKL EDIKPEQAKK
     QTKLFRIFEP KQLPIYRANG ERELRNRWYW KLKRDTLPDG DYDVREYFLN LYDQVLMEMP
     DYLLLKDMAV ENKNSRDAGK VVDSETAAIC DAIFQDEETE GAVRRFIAEM RQRVQADRNV
     VNYPSILHPI DHAFNGYFLQ HQLVEPLNND IIFNYIPERI RNDVNYILNM DRNLPSTARY
     IRPNLLQDRL NLHDNFESLW DTITTSNYIL ARSVVPDLKE LVSTEAQIQK MSQDLQLEAL
     TIQSETQFLT GINSQAANDC FKTLIAAMLS QRTMSLDFVT TNYMSLISGM WLLTVIPNDM
     FIRESLVACQ LAIINTIVYP AFGMQRMHYR NGDPQTPFQI AEQQIQNFQV ANWLHFVNYN
     QFRQVVIDGV LNQVLNDNIR NGHVVNQLME ALMQLSRQQF PTMPVDYKRS IQRGILLLSN
     RLGQLVDLTR LLSYNYETLM ACITMNMQHV QTLTTEKLQL TSVTSLCMLI GNATVIPSPQ
     TLFHYYNVNV NFHSNYNERI NDAVAIITAA NRLNLYQKKM KSIVEDFLKR LQIFDVARVP
     DDQMYRLRDR LRLLPVEIRR LDIFNLIAMN MEQIERASDK IAQGVIIAYR DMQLERDEMY
     GYVNIARNLD GFQQINLEEL MRSGDYAQIT NMLLNNQPVA LVGALPFITD SSVISLIAKL
     DATVFAQIVK LRKVDTLKPI LYKINSDSND FYLVANYDWI PTSTTKVYKQ VPQQFDFRAS
     MHMLTSNLTF TVYSDLLAFV SADTVEPINA VAFDNMRIMN EL