ID   VP2_ROTH6               Reviewed;         880 AA.
AC   B1NKQ6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   02-JUN-2021, entry version 38.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/Human/Indonesia/69M/1980/G8P4[10]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10947;
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; EF583014; ABU87823.1; -; Genomic_RNA.
DR   SMR; B1NKQ6; -.
DR   Proteomes; UP000001455; 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..880
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000368055"
FT   REGION          1..80
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..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..414
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   REGION          422..442
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            220
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            224
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            228
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            839
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"
SQ   SEQUENCE   880 AA;  102437 MW;  6865BD1AA4BFFB65 CRC64;
     MAYRKRGARR EANVNNNNRM QEKDNEKQDQ NNKIQLSDKV LSKKEEVITD NQEEIKIADE
     VKKSTKEESK QLLEVLKTKE EHQKEIQYEI LQKTIPTFEP KESILKKLED IKPEQAKKQT
     KLFRIFEPRQ LPIYRANGEK ELRNRWYWKL KKDTLPDGDY DVREYFLNLY DQVLTEMPDY
     LLLKDMAVEN KNSRDAGKVV DSETASICDA IFQDEETEGA VRRFIAEMRQ RVQADRNVVN
     YPSILHPIDY AFNEYFLQHQ LVEPLNNDII FNYIPERIRN DVNYILNMDR NLPSTARYIR
     PNLLQDRLNL HDNFESLWDT ITTSNYILAR SVVPDLKELV STEAQIQKMS QDLQLEALTI
     QSETQFLTGI NSQAANDCFK TLIAAMLSQR TMSLDFVTTN YMSLISGMWL LTVVPNDMFI
     RESLVACQLA IVNTIVYPAF GMQRMHYRNG DPQTPFQIAE QQTQNFQVAN WLHFVNNNQF
     RQVVIDGVLN QVLNDNIRNG HVINQLMEAL MQLSRQQFPT MPVDYKRSIQ RGILLLSNRL
     GQLVDLTRLL AYNYETLMAC ITMNMQHVQT LTTEKLQLTS VTSLCMLIGN ATVIPSPQTL
     FHYYNVNVNF HSNYNERIND AVAIITAANR LNLYQKKMKA IVEDFLKRLH IFDVARVPDD
     QMYRLRDRLR LLPVEVRRLD IFNLILMNMD QIERASDKIA QGVIIAYRDM QLERDEMYGY
     VNIARNLDGF QQINLEELMR TGDYAQITNM LLNNQPVALV GALPFITDSS VISLIAKLDA
     TVFAQIVKLR KVDTLKPILY KINSDSNDFY LVANYDWVPT STTKVYKQVP QQFDFRSSMH
     MLTSNLTFTV YSDLLAFVSA DTVEPINAVA FDNMRIMNEL