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 14-DEC-2022, entry version 45. 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; Sedoreoviridae; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //