ID   VP2_ROTHC               Reviewed;         884 AA.
AC   Q91E96;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   02-JUN-2021, entry version 55.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04123};
OS   Rotavirus C (isolate RVC/Human/United Kingdom/Bristol/1989) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=31567;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11864750; DOI=10.1016/s0168-1702(01)00442-7;
RA   Chen Z., Lambden P.R., Lau J., Caul E.O., Clarke I.N.;
RT   "Human group C rotavirus: completion of the genome sequence and gene coding
RT   assignments of a non-cultivatable rotavirus.";
RL   Virus Res. 83:179-187(2002).
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; AJ303139; CAC44890.1; -; Genomic_RNA.
DR   RefSeq; YP_392489.1; NC_007546.1.
DR   SMR; Q91E96; -.
DR   PRIDE; Q91E96; -.
DR   GeneID; 3773136; -.
DR   KEGG; vg:3773136; -.
DR   Proteomes; UP000007664; 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   InterPro; IPR007779; Rotavirus_VP2.
DR   Pfam; PF05087; Rota_VP2; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Inner capsid protein; Reference proteome; RNA-binding;
KW   T=2 icosahedral capsid protein; Virion.
FT   CHAIN           1..884
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000369870"
SQ   SEQUENCE   884 AA;  101673 MW;  3C0C7A4570C69E81 CRC64;
     MISRNRRRNN QQKNIEKEKQ LETIINKEVK ENKDSMKEDK LVVTEESNGD VTTAKEQSNN
     INLQKNDLVK EVMNIQNQTL NTVVTENKVE IEEIVKKYIP SYNTDSLIVK KLTEIQESSA
     KTYNTLFRLF TPVKSYLYDI NGEKKLSTRW YWKLLKDDLP AGDYSVRQFF LSLYLNVLEE
     MPDYIMLRDM AVDNPYSAEA GKIVDGKSKE ILIELYQDQM TEGYIRRYMS ELRHKISGET
     NTAKYPAILH PVDNELNQYF LEHQLIQPLT TRNIAELIPT QLYHDPNYVF NIDAAFLTNS
     RFVPPYLTQD RIGLHDGFES IWDSKTHADY VSARRFIPDL TELVDAEKQI KEMAAHLQLE
     AITVQVESQF LAGISAAAAN EAFKFIIGSV LSTRTIAVEF ITSNYMSLAS CMYLMTIMPS
     EIFLRESLVA MQLAIINTLI YPALGLAQMH YQAGEVRTPF ELAEMQVANR SIRQWLHHCN
     TLQFGRQITE GIIHLRFTND IMTGRIVNLF STMLVALSSQ PFATYPLDYK RSVQRALQLL
     SNRTAQIADL TRLIVYNYTT LSACIVMNMH LVGTLTVERI QATSLTSLMM LISNKTVIPE
     PSSLFSYFSS NINFLTNYNE QIDNVVAEIM AAYRLNLYQQ KMLMLVTRFV SKLYIFDAPK
     IPPDQMYRLR NRLRNIPVER RRADVFRIIM NNRDLIEKTS ERICQGVLLS YTPMPLTYVE
     DVGLTNVIND TNSFQIINIE EIEKTGDYSA ITNALLRDTP IILKGAIPYV TNSSVIDVLS
     KVDTTVFASI VKDRDISKLK PIKFIINSDS SEYYLVHNNK WTPTTTTAVY KARSQQFDIQ
     HSVSMLESNL FFVVYNDLFK YIKTTTVLPI NAVSYDGARI MQET