ID   VP2_ROTS1               Reviewed;         881 AA.
AC   P22672;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   14-DEC-2022, entry version 84.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/SA11-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS   Both)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=37137;
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2162107; DOI=10.1016/0042-6822(90)90487-c;
RA   Mitchell D.B., Both G.W.;
RT   "Completion of the genomic sequence of the simian rotavirus SA11:
RT   nucleotide sequences of segments 1, 2, and 3.";
RL   Virology 177:324-331(1990).
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; X16831; CAA34733.1; -; Genomic_RNA.
DR   PIR; B35321; P2XRSR.
DR   SMR; P22672; -.
DR   Proteomes; UP000007180; 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; Reference proteome; Repeat;
KW   RNA-binding; T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT   CHAIN           1..881
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000149535"
FT   REGION          1..82
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          395..415
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   REGION          423..443
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            221
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            225
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            229
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            840
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            842
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ   SEQUENCE   881 AA;  102697 MW;  984AB341AD2F0B75 CRC64;
     MAYRKRGARR ETNLKQDERM QEKEDSKNIN NDSPKSQLSE KVLSKKEEII TDNQEEVKIS
     DEVKKSNKEE SKQLLEVLKT KEEHQKEVQY EILQKTIPTF EPKESILKKL EDIKPEQAKK
     QTKLFRIFEP KQLPIYRANG ERELRNRWYW KLKRDTLPDG DYDVREYFLN LYDQVLMEMP
     DYLLLKDMAV ENKNSRDAGK VVDSETAAIC DAIFQDEEPK AVRRFIAEMR QRVQADRNVV
     NYPSILHPID HAFNEYFLQH QLVEPLNNVY IFNYIPERIR NDVNYILNMD RNLPSTARYI
     RPNLLQDRLN LHDNFESLWD TITTSNYILA RSVVPDLKEL VSTEAQIQKM SQDLQLEALT
     IQSETQFLTG INSQAANDCF KTLIAAMLSQ RTMSLDFVTT NYMSLISGMW LLTVIPNDMF
     IRESLVACQL AIINTIVYPA FGMQRMHYRN GDPQTPFQIA EQQIQNFQVA NWLHFVNYNQ
     FRQVVIDGVL NQVLNDNIRN GHVVNQLMEA LMQLSRQQFP TMPVDYKRSI QRGIFLLSNR
     LGQLVDLTRL LSYINETLMA CITMNMQHVQ TLTTEKLQLT SVTSLCMLIG NATVIPSPQT
     LFHYYNVNVN FHSNYNERIN DAVAIITAAN RLNLYQKKMK SIVEDFLKRL QIFDVARVPD
     DQMYRLRDRL RLLPVEIRRL DIFNLIAMNM EQIERASDKI AQGVIIAYRD MQLERDEMYG
     YVNIARNLDG FQQINLEELM RSGDYAQITN MLLNNQPVAL VGALPFITDS SVISLIAKLD
     ATVFAQIVKL RKVDTLKPIL YKINSDSNDF YLVANYDWIP TSTTKVYKQV PQQFDFRASM
     HMLTSNLTFT VYSDLLAFVS ADTVEPINAV AFDNMRIMNE L
//