ID C5IAV4_9REOV Unreviewed; 313 AA. AC C5IAV4; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 13-NOV-2019, entry version 27. DE RecName: Full=Non-structural protein 3 {ECO:0000256|HAMAP-Rule:MF_04094}; DE Short=NSP3 {ECO:0000256|HAMAP-Rule:MF_04094}; DE AltName: Full=NCVP4 {ECO:0000256|HAMAP-Rule:MF_04094}; DE AltName: Full=Non-structural RNA-binding protein 34 {ECO:0000256|HAMAP-Rule:MF_04094}; DE Short=NS34 {ECO:0000256|HAMAP-Rule:MF_04094}; OS Rotavirus A. OC Viruses; Riboviria; Reoviridae; Sedoreovirinae; Rotavirus. OX NCBI_TaxID=28875 {ECO:0000313|EMBL:ACR56744.1, ECO:0000313|Proteomes:UP000145116}; RN [1] {ECO:0000313|Proteomes:UP000145116} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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). CC -!- FUNCTION: Plays an important role in stimulating the translation CC of viral mRNAs. These mRNAs are capped but not polyadenylated, CC instead terminating in a conserved sequence 'GACC' at the 3' that CC is recognized by NSP3, which competes with host PABPC1 for EIF4G1 CC binding. The interaction between NSP3 and host EIF4G1 stabilizes CC the EIF4E-EIF4G1 interaction, thereby facilitating the initiation CC of capped mRNA translation. {ECO:0000256|HAMAP-Rule:MF_04094}. CC -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with CC host ZC3H7B (via LD motif). Interacts with host EIF4G1. CC {ECO:0000256|HAMAP-Rule:MF_04094}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000256|HAMAP- CC Rule:MF_04094}. CC -!- SIMILARITY: Belongs to the rotavirus A NSP3 protein family. CC {ECO:0000256|HAMAP-Rule:MF_04094}. 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; FJ816613; ACR56744.1; -; Genomic_RNA. DR Proteomes; UP000145116; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-UniRule. DR GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. DR Gene3D; 1.20.58.550; -; 1. DR HAMAP; MF_04094; ROTA_A_NSP3; 1. DR HAMAP; MF_04090; ROTA_NSP3; 1. DR InterPro; IPR042519; NSP3_N. DR InterPro; IPR036082; NSP3_sf. DR InterPro; IPR002873; Rotavirus_NSP3. DR Pfam; PF01665; Rota_NSP3; 1. DR SUPFAM; SSF69903; SSF69903; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|HAMAP-Rule:MF_04094}; KW Complete proteome {ECO:0000313|Proteomes:UP000145116}; KW Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04094}; KW Host-virus interaction {ECO:0000256|HAMAP-Rule:MF_04094}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_04094}; KW Translation regulation {ECO:0000256|HAMAP-Rule:MF_04094}. FT REGION 1 149 RNA-binding. {ECO:0000256|HAMAP-Rule: FT MF_04094}. FT REGION 150 206 Dimerization. {ECO:0000256|HAMAP-Rule: FT MF_04094}. FT REGION 170 234 Interaction with host ZC3H7B. FT {ECO:0000256|HAMAP-Rule:MF_04094}. FT REGION 208 313 Interaction with host EIF4G1. FT {ECO:0000256|HAMAP-Rule:MF_04094}. FT COILED 166 237 {ECO:0000256|HAMAP-Rule:MF_04094}. SQ SEQUENCE 313 AA; 36262 MW; 9DECF22F4233F5D1 CRC64; MLKMESTQQM ASSIINSSFE AAVVAATSTL ELMGTQYDYN EVYTRVKSKF DFVMDDSGVK NNLMGKAVTI DQALNGKFGS AIRNRNWMID SRTVAKLDED VNKLRMMLSS KGIDQKMRVL NACFSVKRVP GKSSSIVKCT RLMKDKLERG EVEVDDSFVE EKMEIDTIDW KSRYEQLEKR FESLKHRVNE KYNNWVLKAR KVNENMNSLQ NVISQQQAHI NDLQMYNNKL ERDLQSKIGS VVSSIEWYLR SMELSDDVKS DIEQQLNSID QLNPVNAMDD FESILRNLIS DYDRLFIMFK GLLQQCNYTC TYE //