ID   VP2_ROTH3               Reviewed;         887 AA.
AC   A4ZCW5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   14-DEC-2022, entry version 38.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/Human/Japan/AU-1/1982/G3P3[9]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=39013;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
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; DQ490536; ABF67543.1; -; Genomic_RNA.
DR   SMR; A4ZCW5; -.
DR   Proteomes; UP000001454; 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..887
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000368056"
FT   REGION          1..87
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..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..421
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   REGION          429..449
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            231
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            235
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            846
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            848
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ   SEQUENCE   887 AA;  103235 MW;  433AB813153C53B4 CRC64;
     MAYRKRGARR ETNLKQDDRM QEKEENKSTN SVIENKNGTK TQLSEKVLSQ KEEVITDNQE
     ETRIADEVKK SNKEESKQLL EVLKTKEEHQ KEVQYEILQK TIPTFEPKES ILKKLEDIKP
     EQAKKQTKLF RIFEPKQLPI YRANGEKELR NRWYWKLKRD TLPDGDYDVR EYFLNLYDQV
     LTEMPDYLLL KDMAVENKNS RDAGKVVDSE TAAICDAIFQ DEETEGVVRR FIAEMRQRVQ
     ADQNVVNYPS ILHPIDHAFN EYFLQHQLVE PLNNDIIFNY IPERIRNDVN YILNMDRNLP
     STARYIRPNL LQDRLNLHDN FESLWDTITT SNYILARSVV PDLKELVSTE AQIQKMSQDL
     QLEALTIQSE TQFLTGINSQ AANDCFKTLI AAMLSQRTMS LDFVTTNYMS LISGMWLLTV
     IPNDMFIRES LVACQLAIIN TIIYPAFGMQ RMHYRNGDPQ TPFQIAEQQI QNFQVANWLH
     FVNNNQFRQV IIDGVLNQVL NDNIRNGHVV NQLMEALMQL SRQQFPTMPV DYKRSIQRGI
     LLLSNRLGQL VDLTRLLAYN YETLMACITM NMQHVQTLTT EKLQLTSVTS LCMLIGNATV
     IPSPQTLFHY YNVNVNFHSN YNERINDAVA IITAANRLNL YQKKMKSIVE DFLKRLQIFD
     VSRVPDDQMY RLRDRLRLLP VEIRRLDIFN LILMNMEQIE RASDKIAQGV IIAYRDMQLE
     RDEMYGYVNI ARNLDGFQQI NLEELMRTGD YAQITNMLLN NQPVALVGAL PFITDSSVIS
     LIAKLDATVF AQIVKLRKVD TLKPILYKIN SDSNDFYLVA NYDWVPTSTT KVYKQVPQQF
     DFRASMHMLT SNLTFTVYSD LLAFVSADTV EPINAVAFDN MRIMNEL
//