ID   VP2_ROTB2               Reviewed;         973 AA.
AC   A9Q1K8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04123};
OS   Rotavirus X (isolate RVX/Human/Bangladesh/NADRV-B219/2002/GXP[X]) (RV
OS   ADRV-N) (Rotavirus (isolate novel adult diarrhea rotavirus-B219)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus.
OX   NCBI_TaxID=348136;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=18814255; DOI=10.1002/jmv.21286;
RA   Nagashima S., Kobayashi N., Ishino M., Alam M.M., Ahmed M.U., Paul S.K.,
RA   Ganesh B., Chawla-Sarkar M., Krishnan T., Naik T.N., Wang Y.-H.;
RT   "Whole genomic characterization of a human rotavirus strain B219 belonging
RT   to a novel group of the genus Rotavirus.";
RL   J. Med. Virol. 80:2023-2033(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_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; EF453356; ABR32123.1; -; mRNA.
DR   SMR; A9Q1K8; -.
DR   Proteomes; UP000174021; 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.
PE   2: Evidence at transcript level;
KW   Capsid protein; Inner capsid protein; RNA-binding;
KW   T=2 icosahedral capsid protein; Virion.
FT   CHAIN           1..973
FT                   /note="Inner capsid protein VP2"
FT                   /id="PRO_0000369834"
SQ   SEQUENCE   973 AA;  111085 MW;  03B08088108FBFD6 CRC64;
     MEVIEKLETI RETLNDTKDK KDFQKIHDEL VQYLDGVDSL TIDDDKWNEI LKLFKTIIIK
     LKSSTIKTTP LENELLQHEK KRTVKEVEKV EEDIKTDVTN DTSKPTLMDK VLQVSNQPNN
     PYSADVLQIR TILSKTLFVD TDSEAYSLYV PESQKLDVSP ITIELTTIEK YQPKVNILKQ
     AVIVPSQNPL LADTYGAPEI LFSTDFFDDI TSNSSEGLQL YFFDKAYKLK KELPNLPFLS
     SLDKDVNPLN PLNSVCKSFG QEKYYDMVMD RTDRGLDARR AAMQFDNVIV DAQNRTVQFN
     VRMHPFDLQL LRISQQFAEP MQDLAPVVRE YMMLGADGYV LTQKIRLDRD QQLIANRRSV
     VFDRMCELSG PLYRSRIIHS MRMMSKLWRT NVFRTSLEDE ITKIYAAAEV SMISIDATTS
     ALSTINIASA EQTLNALLNM SFFRCELDLI GSQSSFGAAM SAMIALMILP TDQENMDDEV
     FDVLCNLVYN ELIAWAADRP VFVRRAGATN AFRQFVNAGL NRDITNYMRF VLLRRPWLPL
     YNSRDVRRNA HVLVPNVDLA NINDQVYVAI NSFLNGIIEA SRRNPNPNKT ISANSFRKLM
     KNMRDICVNR LMPVIRLIRY NVERIGMILH MLPYSADIFD INRNLRDERL RIKIPMSGFL
     SLVMGITKAP DAFDWSQILN FADDVRKMDY AEAISIEDSA SVAIMRNDAN RATSKKEIFI
     SEVRPPTPTV ASIQKIPSAT LTAIFSDRQL INLIRDTHSF RVIREIAVAL QAAFDNSPTS
     QHGVGKGAVL HPVPQNFGRS SQFVRRDNIL LQRPAGIQQF TIEDLKQGRY FQGLMAQIRA
     RQPIIVNGPI PLRISDAAEI EQVTLAFLTM NSPYDAYIDP RDLKQQKLLT DREVDLFIDQ
     SPARPNDEFD NVMARTSVFI IDAPRAIVPI NPQRLNFPYH DIMVTDSVTK FIEFTVALTP
     DLQLFNGLLV FEQ
//