ID   VP2_ROTHL               Reviewed;         879 AA.
AC   A3DSK6; B1NKS6;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   14-DEC-2022, entry version 39.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/Human/Philippines/L26/1987/G12P1B[4]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10953;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17166908; DOI=10.1128/jvi.01622-06;
RA   Rahman M., Matthijnssens J., Yang X., Delbeke T., Arijs I., Taniguchi K.,
RA   Iturriza-Gomara M., Iftekharuddin N., Azim T., Van Ranst M.;
RT   "Evolutionary history and global spread of the emerging G12 human
RT   rotaviruses.";
RL   J. Virol. 81:2382-2390(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=18216098; DOI=10.1128/jvi.02257-07;
RA   Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T.,
RA   McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T.,
RA   Rahman M., Van Ranst M.;
RT   "Full genome-based classification of rotaviruses reveals a common origin
RT   between human Wa-Like and porcine rotavirus strains and human DS-1-like and
RT   bovine rotavirus strains.";
RL   J. Virol. 82:3204-3219(2008).
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; DQ146694; ABA34197.1; -; Genomic_RNA.
DR   EMBL; EF583034; ABU87843.1; -; Genomic_RNA.
DR   SMR; A3DSK6; -.
DR   Proteomes; UP000001459; 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; Repeat; RNA-binding;
KW   T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT   CHAIN           1..879
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000368060"
FT   REGION          1..79
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..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..413
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   REGION          421..441
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            219
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            223
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            227
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            838
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"
SQ   SEQUENCE   879 AA;  102408 MW;  CA32597E757389A2 CRC64;
     MAYRKRGARR EANLNNDDRM QEKNDEKQDS NKIQLSDKVL SKKEEVVTDS HEEVKITDEA
     KKSTKEESKQ LLEVLKTKEE HQKEIQYEIL QKTIPTFEPK ETILRKLEDI KPELAKKQTK
     LFRIFEPKQL PIYRANGERE LRNRWYWKLK KDTLPDGDYD VREYFLNLYD QVLTEMPDYL
     LLKDMAVENK NSRDAGKVVD SETASICDAI FQDEETEGAV RRFIAEMRQR VQADRNVVNY
     PSILHPIDYA FNEYFLQHQL VEPLNNDIIF NYIPERIRND VNYILNMDRN LPSTARYIRP
     NLLQDRLNLH DNFESLWDTI TTSNYILARS VVPDLKELVS TEAQIQKMSQ DLQLEALTIQ
     SETQFLTGIN SQAANDCFKT LIAAMLSQRT MSLDFVTTNY MSLISGMWLL TVIPNDMFIR
     ESLVACQLAI VNTIIYPAFG MQRMHYRNGD PQTPFHIAEQ QIQNFQVANW LHFVNNNQFR
     QVVIDGVLNQ VLNDNIRNGH VINQLMEALM QLSRQQFPTM PVDYKRSIQR GILLLSNRLG
     QLVDLTRLLA YNYETLMACI TMNMQHVQTL TTEKLQLTSV TSLCMLIGNA TVIPSPQTLF
     HYYNVNVNFH SNYNERINDA VAIITAANRL NLYQKKMKAI VEDFLKRLYI FDVSRVPDDQ
     MYRLRDRLRL LPVEIRRLDI FNLILMNMDQ IERASDKIAQ GVIIAYRDMH LERDEMYGYV
     NIARNLDGFQ QINLEELMRS GDYAQITNML LNNQPVALVG ALPFITDSSV ISLIAKLDAT
     VFAQIVKLRK VDTLKPILYK INSDSNDFYL VANYDWVPTS TTKVYKQVPQ QFDFRNSMHM
     LTSNLTFTVY SDLLAFVSAD TVEPINAVAF DNMRIMNEL
//