ID   VP2_ROTHK               Reviewed;         892 AA.
AC   Q9QNB2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-JUN-2021, entry version 46.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS   Rotavirus A (strain RVA/Human/Japan/KU/1995/G1P1A[8]) (RV-A).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=10952;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Taniguchi K.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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; AB022766; BAA84963.1; -; mRNA.
DR   SMR; Q9QNB2; -.
DR   Proteomes; UP000001458; 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   2: Evidence at transcript level;
KW   Capsid protein; Inner capsid protein; Repeat; RNA-binding;
KW   T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT   CHAIN           1..892
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000368057"
FT   REGION          1..90
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..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..426
FT                   /note="Hydrophobic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   REGION          434..454
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            234
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            238
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            851
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT   SITE            853
FT                   /note="Interaction with the intermediate capsid protein
FT                   VP6"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ   SEQUENCE   892 AA;  104135 MW;  717BB8DCC285375E CRC64;
     MAYRKRGAKR EDLSQQHERL QEKEIENNTD VTMENKNNNN NRKQRLSDKV LSQKEEIITD
     VQDDIKIADE VKKSSKEESK QLLEILKTKE EHQKEVQYEI LQKTIPTFEP KESILKKLED
     IRPEQAKKQM KLFRIFEPRQ LPIYRTNGEK ELRNRWYWKL KKDTLPDGDY DVREYFLNLY
     DQILIEMPDY LLLKDMAVEN KNSRDAGKVV DSETANICDA IFQDEETEGV IRRFIADMRQ
     QVQSDRNIVN YPSILHPIDH AFNEYFLNHQ LVEPLNNEII FNYIPERIRN DVNYILNMDM
     NLPSTARYIR PNLLQDRLNL HDNFESLWDT ITTSNYVLAR SVVPDLKEKE LVSTEAQIQK
     MSQDLQLEAL TIQSETQFLA GINSQAANDC FKTLIAAMLS QRTMSLDFVT TNYMSLISGM
     WLLTVIPNDM FLRESLVACE LAIINTIVYP AFGMQRMHYR NGDPQTPFQI AEQQIQNFQV
     ANWLHFINNN RFRQVVIDGV LNQTLNDNIR NGQVINQLME ALMQLSRQQF PTMPVDYKRS
     IQRGILLLSN RLGQLVDLTR LVSYNYETLM ACITMNMQHV QTLTTEKLQL TSVTSLCMLI
     GNTTVIPSPQ TLFHYYNVSV NFHSNYNERI NDAVAIITAA NRLNLYQKKM KSIVEDFLKR
     LQIFDVPRVP DDQMYRLRDR LRLLPVERRR LDIFNLILMN MEQIERASDK IAQGVLIAYR
     DMQLERDEMY GFVNIARNLD GYQQINLEEL MRTGDYGQIT NMLLNNQPVA LVGALPFVTD
     SSVISLIAKL DATVFAQIVK LRKVDTLKPI LYKINSDSND FYLVANYDWI PTSTTKVYKQ
     VPQPFDFRAS MHMLTSNLTF TVYSDLLSFV SADTVEPINA IAFDNMRIMN EL