ID NSP3_ROTHP Reviewed; 310 AA. AC B3SRV3; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 28-MAR-2018, entry version 25. DE RecName: Full=Non-structural protein 3 {ECO:0000255|HAMAP-Rule:MF_04090}; DE Short=NSP3 {ECO:0000255|HAMAP-Rule:MF_04090}; DE AltName: Full=NCVP4 {ECO:0000255|HAMAP-Rule:MF_04090}; DE AltName: Full=Non-structural RNA-binding protein 34 {ECO:0000255|HAMAP-Rule:MF_04090}; DE Short=NS34 {ECO:0000255|HAMAP-Rule:MF_04090}; OS Rotavirus A (strain RVA/Human/United States/P/1974/G3P1A[8]) (RV-A). OC Viruses; dsRNA viruses; Reoviridae; Sedoreovirinae; Rotavirus; OC Rotavirus A. OX NCBI_TaxID=10957; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=18786998; DOI=10.1128/JVI.01402-08; RA Heiman E.M., McDonald S.M., Barro M., Taraporewala Z.F., Bar-Magen T., RA Patton J.T.; RT "Group A human rotavirus genomics: evidence that gene constellations RT are influenced by viral protein interactions."; RL J. Virol. 82:11106-11116(2008). 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, therebey facilitating the initiation CC of capped mRNA translation. {ECO:0000255|HAMAP-Rule:MF_04090}. CC -!- SUBUNIT: Homodimer. Interacts (via the coiled-coil region) with CC host ZC3H7B (via LD motif). Interacts with host EIF4G1. CC {ECO:0000255|HAMAP-Rule:MF_04090}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP- CC Rule:MF_04090}. CC -!- SIMILARITY: Belongs to the rotavirus NSP3 family. CC {ECO:0000255|HAMAP-Rule:MF_04090}. 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; EF672600; ABV53278.1; -; Genomic_RNA. DR SMR; B3SRV3; -. DR OrthoDB; VOG090000G7; -. DR Proteomes; UP000007047; Genome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW. DR HAMAP; MF_04090; ROTA_NSP3; 1. 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; Complete proteome; Host cytoplasm; KW Host-virus interaction; RNA-binding; Translation regulation. FT CHAIN 1 310 Non-structural protein 3. FT /FTId=PRO_0000369457. FT REGION 1 146 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_04090}. FT REGION 147 203 Dimerization. {ECO:0000255|HAMAP- FT Rule:MF_04090}. FT REGION 167 231 Interaction with host ZC3H7B. FT {ECO:0000255|HAMAP-Rule:MF_04090}. FT REGION 205 310 Interaction with host EIF4G1. FT {ECO:0000255|HAMAP-Rule:MF_04090}. FT COILED 164 230 {ECO:0000255|HAMAP-Rule:MF_04090}. SQ SEQUENCE 310 AA; 35826 MW; F756CB2EBF997FFE CRC64; MESTQQMVSS IINTSFEAAV VAATSTLELM GIQYDYNEVF TRVKSKFDYV MDDSGVKNNL LGKAITIDQA LNGKFGSAIR NRNWMTDSKT VAKLDEDVNK LRMTLSSKGI DQKMRVLNAC FSVKRIPGKS SSIIKCTRLM KDKIERGEVE VDDSYVDEKM EIDTIDWKSR YDQLEKRFES LKQRVSEKYN TWVQKAKKVN ENMYSLQNVI SQQQNQIADL QQYCNKLEAD LQGKFSSLVS SVEWYLRSME LSDDVKNDIE QQLNSIDLIN PINAIDDIES LIRNLIQDYD RTFLMLKGLL KQCNYEYAYE //