VP2_ROTSH
ID VP2_ROTSH Reviewed; 882 AA.
AC A2T3R5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 02-JUN-2021, entry version 44.
DE RecName: Full=Inner capsid protein VP2 {ECO:0000255|HAMAP-Rule:MF_04127};
OS Rotavirus A (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=450149;
OH NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA Small C., Barro M., Brown T.L., Patton J.T.;
RT "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT agent.";
RL Virology 359:415-424(2007).
RN [2]
RP RNA-BINDING.
RX PubMed=9371626; DOI=10.1128/jvi.71.12.9618-9626.1997;
RA Patton J.T., Jones M.T., Kalbach A.N., He Y.-W., Xiaobo J.;
RT "Rotavirus RNA polymerase requires the core shell protein to synthesize the
RT double-stranded RNA genome.";
RL J. Virol. 71:9618-9626(1997).
RN [3]
RP FUNCTION.
RX PubMed=19000820; DOI=10.1016/j.str.2008.09.006;
RA Lu X., McDonald S.M., Tortorici M.A., Tao Y.J., Vasquez-Del Carpio R.,
RA Nibert M.L., Patton J.T., Harrison S.C.;
RT "Mechanism for coordinated RNA packaging and genome replication by
RT rotavirus polymerase VP1.";
RL Structure 16:1678-1688(2008).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY OF CAPSID SHELL, INTERACTION WITH THE
RP INTERMEDIATE CAPSID PROTEIN VP6, AND FUNCTION.
RC STRAIN=SA11-4F;
RX PubMed=19036817; DOI=10.1128/jvi.01855-08;
RA Li Z., Baker M.L., Jiang W., Estes M.K., Prasad B.V.V.;
RT "Rotavirus architecture at subnanometer resolution.";
RL J. Virol. 83:1754-1766(2009).
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 (PubMed:19036817).
CC This capsid constitutes the innermost concentric layer of the viral
CC mature particle (PubMed:19036817). It encapsidates the polymerase VP1,
CC the capping enzyme VP3 and the genomic dsRNA, thereby defining the
CC core. The innermost VP2 capsid and the intermediate VP6 capsid remain
CC intact following cell entry to protect the dsRNA from degradation and
CC to prevent unfavorable antiviral responses in the host cell during all
CC the replication cycle of the virus. Nascent transcripts are transcribed
CC within the structural confines of this double-layered particle (DLP)
CC and are extruded through the channels formed by VP2 N-termini. VP2 is
CC required for the replicase activity of VP1 polymerase. Probably
CC recruits a copy of a VP1-VP3 complex, potentially along with a segment
CC of plus-strand RNA, as a decamer of VP2 assembles (By similarity). May
CC activate the autoinhibited VP1/RNA complex to coordinate packaging and
CC genome replication (PubMed:19000820). {ECO:0000255|HAMAP-Rule:MF_04127,
CC ECO:0000269|PubMed:19000820, ECO:0000269|PubMed:19036817}.
CC -!- SUBUNIT: Homodecamer; each decamer is made up of two conformers of VP2,
CC called VP2A and VP2B (By similarity). Interacts with a VP1-VP3 complex
CC (By similarity). Interacts with the intermediate capsid protein VP6
CC (PubMed:19036817). Interacts with NSP5 (By similarity). Interacts (via
CC N-terminus) with NSP2 (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_04127, ECO:0000269|PubMed:19036817}.
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; DQ838635; ABG75814.1; -; Genomic_RNA.
DR RefSeq; YP_002302226.1; NC_011506.2.
DR SMR; A2T3R5; -.
DR GeneID; 7011366; -.
DR KEGG; vg:7011366; -.
DR Proteomes; UP000001119; Genome.
DR GO; GO:0039616; C:T=2 icosahedral viral capsid; IDA:UniProtKB.
DR GO; GO:0039625; C:viral inner capsid; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Capsid protein; Inner capsid protein; Reference proteome; Repeat;
KW RNA-binding; T=2 icosahedral capsid protein; Ubl conjugation; Virion.
FT CHAIN 1..882
FT /note="Inner capsid protein VP2"
FT /id="PRO_0000367813"
FT REGION 1..82
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..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..416
FT /note="Hydrophobic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT REGION 424..444
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 222
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 226
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 230
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 841
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
FT SITE 843
FT /note="Interaction with the intermediate capsid protein
FT VP6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04127"
SQ SEQUENCE 882 AA; 102741 MW; D2D7006501643EC6 CRC64;
MAYRKRGARR ETNLKQDERM QEKEDSKNIN NDSPKSQLSE KVLSKKEEII TDNQEEVKIS
DEVKKSNKEE SKQLLEVLKT KEEHQKEVQY EILQKTIPTF EPKESILKKL EDIKPEQAKK
QTKLFRIFEP KQLPIYRANG ERELRNRWYW KLKRDTLPDG DYDVREYFLN LYDQVLMEMP
DYLLLKDMAV ENKNSRDAGK VVDSETAAIC DAIFQDEETE GAVRRFIAEM RQRVQADRNV
VNYPSILHPI DHAFNEYFLQ HQLVEPLNND IIFNYIPERI RNDVNYILNM DRNLPSTARY
IRPNLLQDRL NLHDNFESLW DTITTSNYIL ARSVVPDLKE LVSTEAQIQK MSQDLQLEAL
TIQSETQFLT GINSQAANDC FKTLIAAMLS QRTMSLDFVT TNYMSLISGM WLLTVIPNDM
FIRESLVACQ LAIINTIVYP AFGMQRMHYR NGDPQTPFQI AEQQIQNFQV ANWLHFVNYN
QFRQVVIDGV LNQVLNDNIR NGHVVNQLME ALMQLSRQQF PTMPVDYKRS IQRGILLLSN
RLGQLVDLTR LLSYNYETLM ACITMNMQHV QTLTTEKLQL TSVTSLCMLI GNATVIPSPQ
TLFHYYNVNV NFHSNYNERI NDAVAIITAA NRLNLYQKKM KSIVEDFLKR LQIFDVARVP
DDQMYRLRDR LRLLPVEIRR LDIFNLIAMN MEQIERASDK IAQGVIIAYR DMQLERDEMY
GYVNIARNLD GFQQINLEEL MRSGDYAQIT NMLLNNQPVA LVGALPFITD SSVISLIAKL
DATVFAQIVK LRKVDTLKPI LYKINSDSND FYLVANYDWI PTSTTKVYKQ VPQQFDFRAS
MHMLTSNLTF TVYSDLLAFV SADTVEPINA VAFDNMRIMN EL
