ID F6LR22_9REOV Unreviewed; 880 AA. AC F6LR22; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 16-OCT-2019, entry version 15. DE RecName: Full=Inner capsid protein VP2 {ECO:0000256|HAMAP-Rule:MF_04127, ECO:0000256|RuleBase:RU363125}; GN Name=VP2 {ECO:0000313|EMBL:AEF32122.1}; OS Human rotavirus A. OC Viruses; Riboviria; Reoviridae; Sedoreovirinae; Rotavirus; OC Rotavirus A. OX NCBI_TaxID=10941 {ECO:0000313|EMBL:AEF32122.1, ECO:0000313|Proteomes:UP000106047}; RN [1] {ECO:0000313|EMBL:AEF32122.1, ECO:0000313|Proteomes:UP000106047} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KF17 {ECO:0000313|EMBL:AEF32122.1}; RX PubMed=21656185; DOI=10.1007/s11262-011-0624-6; RA Yamamoto D., Kawaguchiya M., Ghosh S., Ichikawa M., Numazaki K., RA Kobayashi N.; RT "Detection and full genomic analysis of G6P[9] human rotavirus in RT Japan."; RL Virus Genes 43:215-223(2011). CC -!- FUNCTION: Inner capsid protein that self-assembles to form an CC icosahedral capsid with a T=2 symmetry, which consists of 120 CC copies of VP2, with channels at each of its five-fold vertices. CC This capsid constitutes the innermost concentric layer of the CC viral mature particle. It encapsidates the polymerase VP1, the CC capping enzyme VP3 and the genomic dsRNA, thereby defining the CC core. The innermost VP2 capsid and the intermediate VP6 capsid CC remain intact following cell entry to protect the dsRNA from CC degradation and to prevent unfavorable antiviral responses in the CC host cell during all the replication cycle of the virus. Nascent CC transcripts are transcribed within the structural confines of this CC double-layered particle (DLP) and are extruded through the CC channels formed by VP2 N-termini. VP2 is required for the CC replicase activity of VP1 polymerase. Probably recruits a copy of CC a VP1-VP3 complex, potentially along with a segment of plus-strand CC RNA, as a decamer of VP2 assembles. May activate the autoinhibited CC VP1/RNA complex to coordinate packaging and genome replication. CC {ECO:0000256|HAMAP-Rule:MF_04127, ECO:0000256|RuleBase:RU363125}. CC -!- SUBUNIT: Homodecamer; each decamer is made up of two conformers of CC VP2, called VP2A and VP2B. Interacts with a VP1-VP3 complex. CC Interacts with the intermediate capsid protein VP6. Interacts with CC NSP5. Interacts (via N-terminus) with NSP2. {ECO:0000256|HAMAP- CC Rule:MF_04127, ECO:0000256|RuleBase:RU363125}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000256|HAMAP-Rule:MF_04127}. CC Note=Inner capsid protein. Also found in spherical cytoplasmic CC structures, called virus factories, that appear early after CC infection and are the site of viral replication and packaging. CC {ECO:0000256|HAMAP-Rule:MF_04127}. CC -!- DOMAIN: The N-terminus binds RNA. It is necessary for CC encapsidation of VP1 and VP3. The N-termini of 10 VP2 molecules CC form a cylindrical hub underneath each 5-fold axis of the inner CC capsid. {ECO:0000256|HAMAP-Rule:MF_04127}. CC -!- PTM: Sumoylated with SUMO1 and SUMO2. Sumoylation of viral CC proteins seems to have a positive role on viral replication. CC {ECO:0000256|HAMAP-Rule:MF_04127}. CC -!- SIMILARITY: Belongs to the rotavirus VP2 family. CC {ECO:0000256|HAMAP-Rule:MF_04127, ECO:0000256|RuleBase:RU363125}. 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; JF421976; AEF32122.1; -; Genomic_RNA. DR Proteomes; UP000106047; 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 3: Inferred from homology; KW Capsid protein {ECO:0000256|HAMAP-Rule:MF_04127, KW ECO:0000256|RuleBase:RU363125}; KW Complete proteome {ECO:0000313|Proteomes:UP000106047}; KW Inner capsid protein {ECO:0000256|HAMAP-Rule:MF_04127, KW ECO:0000256|RuleBase:RU363125}; KW Repeat {ECO:0000256|HAMAP-Rule:MF_04127}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04127, KW ECO:0000256|RuleBase:RU363125}; KW T=2 icosahedral capsid protein {ECO:0000256|HAMAP-Rule:MF_04127}; KW Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04127}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04127, KW ECO:0000256|RuleBase:RU363125}. FT REGION 1 80 5-fold hub; involved in the encapsidation FT of VP1 and VP3. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT REGION 1 45 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 394 414 Hydrophobic. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT REGION 422 442 Hydrophobic. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT SITE 220 220 Interaction with the intermediate capsid FT protein VP6. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT SITE 224 224 Interaction with the intermediate capsid FT protein VP6. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT SITE 228 228 Interaction with the intermediate capsid FT protein VP6. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT SITE 839 839 Interaction with the intermediate capsid FT protein VP6. {ECO:0000256|HAMAP-Rule: FT MF_04127}. FT SITE 841 841 Interaction with the intermediate capsid FT protein VP6. {ECO:0000256|HAMAP-Rule: FT MF_04127}. SQ SEQUENCE 880 AA; 102469 MW; 82640A27B7310BC3 CRC64; MAYRKRGARR EANVNSNDRM QEKDDEKQDQ NNKMQLSDKV LSKKEEVITD NQEEVKIADE VKKSTKEESK QLLEVLKTKE EHQKEIQYEI LQKTIPTFEP KESILKKLED IKPEQAKKQT KLFRIFEPRQ LPIYRANGEK ELRNRWYWKL KKDTLPDGDY DVREYFLNLY DQVLTEMPDY LLLKDMAVEN KNSRDAGKVV DSETASICDA IFQDEETEGA VRRFIAEMRQ RVQADRNVVN YPSILHPIDY AFNEYFLQHQ LVEPLNNDII FNYIPERIRN DVNYILNMDR NLPSTARYIR PNLLQDRLNL HDNFESLWDT ITTSNYILAR SVVPDLKELV STEAQIQKMS QDLQLEALTI QSETQFLTGI NSQAANDCFK TLIAAMLSQR TMSLDFVTTN YMSLISGMWL LTVVPNDMFI RESLVACQLA IVNTIVYPAF GMQRMHYRNG DPQTPFQIAE QQIQNFQVAN WLHFVNNNQF RQVVIDGVLN QVLNDNIRNG HVINQLMEAL MQLSRQQFPT MPVDYKRSIQ RGILLLSNRL GQLVDLTRLL AYNYETLMAC ITMNMRHVQT LTTEKLQLTS VTSLCMLIGN ATVIPSPQTL FHYYNVNVNF HSNYNERIND AVAIITAANR LNLYQKKMKA IVEDFLKRLH IFDVARVPDD QMYRLRDRLR LLPVEVRRLD IFNLILMNMD QIERASDKIA QGVIIAYRDM QLERDEMYGY VNIARNLDGF QQINLEELMR TGDYAQITNM LLNNQPVALV GALPFVTDSS VISLIAKLDA TVFAQIVKLR KVDTLKPILY KINSDSNDFY LVANYDWVPT STTKVYKQVP QQFDFRNSMH MLTSNLTFTV YSDLLAFVSA DTVEPINAVA FDNMRIMNEL //