VP2_ROTB2
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 03-AUG-2022, entry version 40.
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; Reoviridae; Sedoreovirinae; Rotavirus; unclassified 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 PRIDE; 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; Reference proteome; 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