ID   VP2_ROTGA               Reviewed;         933 AA.
AC   Q86195;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   12-AUG-2020, entry version 43.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04123};
OS   Rotavirus B (isolate RVB/Human/China/ADRV/1982) (RV-B) (Rotavirus B
OS   (isolate adult diarrhea rotavirus)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=10942;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8178482; DOI=10.1006/viro.1994.1279;
RA   Mackow E.R., Fay M.E., Shaw R., Tao H., Chen G.;
RT   "Cloning sequencing and expression of the gene encoding the VP2 protein of
RT   the human group B rotavirus, ADRV.";
RL   Virology 201:162-168(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; M91433; AAA47350.1; -; Genomic_RNA.
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..933
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000369832"
SQ   SEQUENCE   933 AA;  105635 MW;  3FCF4CE129F14341 CRC64;
     MDSTVLVESA KTNIHGVDSK AEKQTIFDQL ISDIKSQTDG QIPDEVLPDL QQLAEINGLT
     FEYKPKEKLS IMDHPDPTSV LSQDVFQIRT ILSKTLFVDV ENEDYSVYIP NDTAKLTPVL
     IDARPIQTYQ PKALMHKDTA ILPSHRDEIS DQYGTDEILF DSHMFNDISQ AQIRDFDTYI
     LDKSIQIQNT LPNLEFISSL EKEVNPFNIH NTLCLNFGQK EYYNIIADRT NLSFQQRRQS
     VQFDNVIVDG VARTARVSLR LHPFDSQLLD IVRFNVIQDQ PLADTLMEYQ LVAADGFVAT
     PKFRVDRDAR LIADVRSPVM ARLCELSPFF HRTRILSSMT DFTPLWKVNV FSSSIDNAKD
     AIYRMAEISF TVADATTSAL ASVNVASAQQ TLLTLLNLSL FRFEIDPTGS QSNFGSAVSA
     ALMLIVFPTD EQSMSNITFD NLCNLVFNEL IAWTVDRPTF VKRTGMTNAF EANVNIGGGN
     MTRDIIAYMR FVLLRRPWAV FQRTYDDRYV SDIMVPNIDE ANVNDQCYVA INNLFNGLIQ
     AAQRNPNPGR QIAATSFRKL LKSMKDSCCN RIIPLIRLLK YNIERIARVY RFFPYTADLV
     HVIPAFRDER LRVKVPVSGM LSIALGINKA PDSFDWYNLL KFADVVRTKN FADQSLESIM
     VHALIRNDIN PARSKKDYIQ QNIKPATNVV ASLSKLPSAT FTTILADRML NNEIRRTQSY
     VVTNRIRDAV RAAFEHVPTA EHGIAKGALL LPIPQNFQRS SVYVRKDNIL YDPPVGVDRF
     NLSDLLDGRF YQGLINRVQN MAPFVISGPL QVKPSDASAI ESVTSAYLTM SSPYDACVRP
     EDLRHNRVVH PPTVDYFSDA SITRPNTQFE QLMSKTSVFV IDAPRLIVQN DATVYTFDYK
     DIQLTTSVVD KLEFTSVKTP DVTLFNGMLV YED