ID F6LR22_9REOV Unreviewed; 880 AA. AC F6LR22; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 07-OCT-2020, entry version 18. 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; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; 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 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 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:0000256|HAMAP-Rule:MF_04127, ECO:0000256|RuleBase:RU363125}. 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:0000256|HAMAP-Rule:MF_04127, CC 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 infection CC 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 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:0000256|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:0000256|HAMAP- CC Rule:MF_04127}. CC -!- SIMILARITY: Belongs to the rotavirus VP2 family. {ECO:0000256|HAMAP- CC 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 Inner capsid protein {ECO:0000256|ARBA:ARBA00022996, ECO:0000256|HAMAP- KW Rule:MF_04127, ECO:0000256|RuleBase:RU363125}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, 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|ARBA:ARBA00022611, KW ECO:0000256|HAMAP-Rule:MF_04127}; KW Ubl conjugation {ECO:0000256|HAMAP-Rule:MF_04127}; KW Virion {ECO:0000256|HAMAP-Rule:MF_04127, ECO:0000256|RuleBase:RU363125}. FT REGION 1..80 FT /note="5-fold hub; involved in the encapsidation of VP1 and FT VP3" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT REGION 1..45 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 394..414 FT /note="Hydrophobic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT REGION 422..442 FT /note="Hydrophobic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT SITE 220 FT /note="Interaction with the intermediate capsid protein FT VP6" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT SITE 224 FT /note="Interaction with the intermediate capsid protein FT VP6" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT SITE 228 FT /note="Interaction with the intermediate capsid protein FT VP6" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT SITE 839 FT /note="Interaction with the intermediate capsid protein FT VP6" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04127" FT SITE 841 FT /note="Interaction with the intermediate capsid protein FT VP6" FT /evidence="ECO:0000256|HAMAP-Rule: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 //