ID   VP2_ROTHW               Reviewed;         890 AA.
AC   P11231;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   08-NOV-2023, entry version 93.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/Human/United States/Wa/1974/G1P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10962;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18216104; DOI=10.1128/jvi.02492-07;
RA   McDonald S.M., Patton J.T.;
RT   "Molecular characterization of a subgroup specificity associated with the
RT   rotavirus inner capsid protein VP2.";
RL   J. Virol. 82:2752-2764(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2544861; DOI=10.1093/nar/17.11.4382;
RA   Ernst H., Duhl J.A.;
RT   "Nucleotide sequence of genomic segment 2 of the human rotavirus Wa.";
RL   Nucleic Acids Res. 17:4382-4382(1989).
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; X14942; CAA33074.1; -; Genomic_RNA.
DR   PIR; A34008; P2XRWA.
DR   SMR; P11231; -.
DR   Proteomes; UP000006581; 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_0000149533"
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..35
FT                   /note="Basic and acidic 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;  103751 MW;  0E0933ED56EB4295 CRC64;
     MAYRKRGAKR ENLPQQNERL QEKEIEKDVD VTMENKNNNR KQQLSDKVLS QKEEIITDAQ
     DDIKIAGEIK KSSKEESKQL LEILKTKEDH QKEIQYEILQ KTIPTFESKE SILKKLEDIR
     PEQAKKQMKL FRIFEPKQLP IYRANGEKEL RNRWYWKLKK DTLPDGDYDV REYFLNLYDQ
     ILIEMPDYLL LKDMAVENKN SRDAGKVVDS ETANICDAIF QDEETEGVVR 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 GQLVDLTRLV SYNYETLMAC VTMNMQHVQT LTTEKLQLTS VTSLCMLIGN
     TTVIPSPQTL FHYYNINVNF HSNYNERIND AVAIITAANR LNLYQKKMKS IVEDFLKRLQ
     IFDVPRVPDD QMYRLRDRLR LLPVERRRLD IFNLILMNME QIERASDKIA QGVIIAYRDM
     QLERDEMYGY VNIARNLDGY QQINLEELMR TGDYGQITNM LLNNQPVALV GALPFVTDSS
     VISLIAKLDA TVFAQIVKLR KVDTLKPILY KINSDSNDFY LVANYDWIPT STTKVYKQVP
     QPFDFRASMH MLTSNLTFTV YSDLLSFVSA DTVEPINAVA FDNMRIMNEL
//