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 14-DEC-2022, entry version 47. 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; Sedoreoviridae; 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}. 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; 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 //