ID   VP2_ROTGI               Reviewed;         934 AA.
AC   Q86108;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-DEC-2020, entry version 45.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04123};
OS   Rotavirus B (isolate RVB/Rat/United States/IDIR/1984/G1P[X]) (RV-B)
OS   (Rotavirus B (isolate infectious diarrhea of infant rats)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=28877;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=10116; Rattus norvegicus (Rat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8116237; DOI=10.1006/viro.1994.1106;
RA   Lindsay D.A., Waggie K.S., Eiden J.J.;
RT   "Group B rotavirus VP2: sequence analysis, expression, and gene coding
RT   assignment.";
RL   Virology 199:141-150(1994).
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_04123}.
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_04123}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04123}.
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_04123}.
CC   -!- SIMILARITY: Belongs to the rotavirus VP2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04123}.
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DR   EMBL; U00673; AAA17401.1; -; Genomic_RNA.
DR   PIR; A49808; A49808.
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   InterPro; IPR007779; Rotavirus_VP2.
PE   3: Inferred from homology;
KW   Capsid protein; Inner capsid protein; RNA-binding;
KW   T=2 icosahedral capsid protein; Virion.
FT   CHAIN           1..934
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000369833"
SQ   SEQUENCE   934 AA;  106015 MW;  F61A623E0B4CA090 CRC64;
     MDFPNLVLSA KNSIQNVDSK DEKQKIIDQL ISDIRGQNDG VIPDEVLSEI QQVAEINGLS
     FNYEKPVKQE LLEQPDPTSV LSQEVFQIRT ILSKTLFVDV EAEDYSVYIP DETSNLSPVQ
     IDARPIQTYQ PKALMYKDTA ILPSNRDEVS DQYGADEILF DSHMFNDISQ AQIRDFETYV
     LDKAMQIQSS LPNLDFVSSL DKEVNPFNVH NTLCLNFGQR EYYNIIADRT NQSFQQRRQS
     VQFDNVVVDG VARRARVSLR LHPFDSQLLD IIRFNTIQDQ PLADTMAEYQ LVAADGFVAT
     PRFRTDRDAR LIADVRSRVM ARLCELSPYF HRTRILSSMT DFNSLWKVNV FSSSIDNAKD
     AIYRMAEISF TVADATTSAL SSVNIASAQQ TLLVLLNMSL FRFEIEPVGS QSNFGAAVSA
     ALMLVVFPTD EASMSNVTFD NLCNLVFNEL IAWTVDRPTF VKRTGMTNAF EANVNIGGGN
     MTRDITAYMR FVLLRRPWAV FQRTYDDQYV ADIMVPNIDE ANVNDQSYMA INNLFSGLIQ
     AAQRNPNPGR QIAATSFRKL LKSMKDSCCN RIMPLIRLMK YNVERIARIY RFFPYTADLV
     QRIPAFRDER IRIKVPVSGM LSIALGINKS PDVFDWYNLL RFADVIRTKN FAERQSLESI
     MVQALIRNDI NPARSRKEYI QQNIKPATNV VASITKVPSA TFTTILSDRM LNNEIRRTQS
     YIVVNRIRDA VRAAFEHVPT AEHGIAKGAL LLPYPQNFQR SSVYVRKDNI LYNAPVGVDR
     FSLDDLLNGR FYQGMVNRIQ NMSPFVIAGP LQVRASNASA IDSVTSAYLT MSSPYDACVK
     PEDLRHNRIV QPPIVDFFSD SSITRPNTQF EQLMSKTSVF VIDAPKLIVQ SDATVYNFDY
     RDIQLTTSVV DKLEFTSVKT PDVTLFNGML VFED