ID   VP2_ROTPC               Reviewed;         872 AA.
AC   P26191;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04123};
OS   Rotavirus C (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=10916;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1310192; DOI=10.1016/0042-6822(92)90035-n;
RA   Bremont M., Juste-Lesage P., Chabanne-Vautherot D., Charpilienne A.,
RA   Cohen J.;
RT   "Sequences of the four larger proteins of a porcine group C rotavirus and
RT   comparison with the equivalent group A rotavirus proteins.";
RL   Virology 186:684-692(1992).
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; M74217; AAA19561.1; -; Unassigned_DNA.
DR   PIR; B40822; P2XRCW.
DR   SMR; P26191; -.
DR   PRIDE; P26191; -.
DR   Proteomes; UP000008175; 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..872
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000149534"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..53
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   872 AA;  101019 MW;  1AB1EF62AB9F51AF CRC64;
     MISRNRRRNT QQKDAEKEKQ TENVEEKEIK EAKEQVKDEK QVITEENVDS PKDVKEQSNT
     VNLQKNDLVK EVINIQNQTL NTIVAENKVE IEEVVKKYIP SYSTDKLIVK NYRNSRIKCQ
     TYNKLFRLLH VKSYLYDVNG EKKLSTRWYW KLLKDDLPAG DYSVRQFFLS LYLNVLDEMP
     DYVMLRDMAV DNPYSAEAGK IVDEKSKEIL VEIYQDQMTE GYIRRYMSDL RHRISGETNT
     AKYPAILHPV DEELNKYFLE HQLIQPLTTR NIAELIPTQL YHDPNYVFNI DAAFLTNSRF
     VPPYLTQDRI GLHDGFESIW DAKTHADYVS ARRFVPDLTE LVDAEKQMKE MLQCKLNHNS
     WQELVHGRNE AFKFIIGTVL STRTIAVEFI TSNYMSLASC MYLMTIMPSE IFLRESLVAM
     QLAVINTLIY PALGLAQMHY QAGEIRRLEL AEMQVANRPI RQWLHHCNTL QFGRQVTEGV
     THLRFTNDIM TGRIVNLFST MLVALSSQPF ATYPLDYKRS VQRALQLLSN RTAQIADLTR
     LIVYNYTTLS ACIVMNMHLV GTLTVERIQA TALTSLIMLI SNKTVIPEPS SLFSYFSSNI
     NFLTNYNEQI DNVVAEIMAA YRLDLYQQKM LMLVTRFVSR LYIFDAPKIP PDQMYRLRNR
     LRNIPVERRR ADVFRIIMNN RDLIEKTSER ICQGVLLSYS PMPLTYVEDV GLTNVVNDTN
     GFQIINIEEI EKTGDYSAIT NALLRDTPII LKGAIPYVTN SSVIDVLSKI DTTVFASIVK
     DRDISKLKPI KFTINSDSSE YYLVHNNKWT PTTTTAVYKA RSQQFNIQHS VSMLESNLFF
     VVYNDLFKYI KTTTVLPINA VSYDGARIMQ ET