ID NSP1_ROTRH Reviewed; 494 AA. AC Q6YLT2; Q86280; Q88349; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 2. DT 24-JAN-2024, entry version 57. DE RecName: Full=Non-structural protein 1 {ECO:0000255|HAMAP-Rule:MF_04088}; DE Short=NSP1 {ECO:0000255|HAMAP-Rule:MF_04088}; DE AltName: Full=NCVP2 {ECO:0000255|HAMAP-Rule:MF_04088}; DE AltName: Full=Non-structural RNA-binding protein 53 {ECO:0000255|HAMAP-Rule:MF_04088}; DE Short=NS53 {ECO:0000255|HAMAP-Rule:MF_04088}; OS Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A. OX NCBI_TaxID=444185; OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=8030275; DOI=10.1006/viro.1994.1471; RA Dunn S.J., Cross T.L., Greenberg H.B.; RT "Comparison of the rotavirus nonstructural protein NSP1 (NS53) from RT different species by sequence analysis and northern blot hybridization."; RL Virology 203:178-183(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=15372078; DOI=10.1038/sj.emboj.7600408; RA Kearney K., Chen D., Taraporewala Z.F., Vende P., Hoshino Y., RA Tortorici M.A., Barro M., Patton J.T.; RT "Cell-line-induced mutation of the rotavirus genome alters expression of an RT IRF3-interacting protein."; RL EMBO J. 23:4072-4081(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RA McCrae M.A.; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Plays a role in the inhibition of host innate immunity by CC inducing the degradation of key host factors required to activate CC interferon production such as IRF3, IRF5 or IRF7. Associates with CC components of cullin RING ligases (CRLs) including CUL1 or CUL3, which CC are essential multisubunit ubiquitination complexes, to modulate their CC activities. {ECO:0000255|HAMAP-Rule:MF_04088}. CC -!- SUBUNIT: Interacts (via C-terminus) with host IRF3; this interaction CC leads to IRF3 degradation. Interacts with host IRF7; this interaction CC leads to IRF7 degradation. Interacts with host CUL1 and CUL3. CC {ECO:0000255|HAMAP-Rule:MF_04088}. CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host cytoskeleton CC {ECO:0000255|HAMAP-Rule:MF_04088}. CC -!- DOMAIN: The integrity of the zinc-binding domain in NSP1 is important CC for degradation of host IRF3. {ECO:0000255|HAMAP-Rule:MF_04088}. CC -!- DOMAIN: The pLxIS motif targets host IRF3 for degradation; however CC phosphorylation of NSP1 pLxIS motif is not required for its activity. CC {ECO:0000255|HAMAP-Rule:MF_04088}. CC -!- SIMILARITY: Belongs to the rotavirus NSP1 family. {ECO:0000255|HAMAP- CC Rule:MF_04088}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA50496.1; Type=Frameshift; 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; U08433; AAA50496.1; ALT_FRAME; Genomic_RNA. DR EMBL; AY117048; AAM92466.1; -; mRNA. DR EMBL; Z32535; CAA83546.1; -; Genomic_RNA. DR Proteomes; UP000174556; Genome. DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-UniRule. DR GO; GO:0044163; C:host cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0039548; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity; IEA:UniProtKB-UniRule. DR GO; GO:0039557; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity; IEA:UniProtKB-UniRule. DR HAMAP; MF_04088; ROTA_NSP1; 1. DR InterPro; IPR002148; Rotavirus_NSP1. DR Pfam; PF00981; Rota_NS53; 1. PE 2: Evidence at transcript level; KW Host cytoplasm; Host cytoskeleton; Host-virus interaction; KW Inhibition of host innate immune response by virus; KW Inhibition of host IRF3 by virus; Inhibition of host IRF7 by virus; KW Inhibition of host RLR pathway by virus; KW Interferon antiviral system evasion; Metal-binding; RNA-binding; KW Viral immunoevasion. FT CHAIN 1..494 FT /note="Non-structural protein 1" FT /id="PRO_0000369090" FT REGION 1..83 FT /note="RNA-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT REGION 44..81 FT /note="Zinc-binding domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT REGION 84..178 FT /note="Important for cytoskeleton localization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT REGION 320..494 FT /note="Interaction with host IRF3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT MOTIF 485..488 FT /note="pLxIS motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT CONFLICT 50 FT /note="L -> V (in Ref. 2; AAM92466)" FT CONFLICT 74 FT /note="C -> Y (in Ref. 3; CAA83546)" FT CONFLICT 85 FT /note="L -> F (in Ref. 3; CAA83546)" FT CONFLICT 280 FT /note="S -> F (in Ref. 3; CAA83546)" FT CONFLICT 434 FT /note="T -> I (in Ref. 3; CAA83546)" FT CONFLICT 482 FT /note="E -> G (in Ref. 1; AAA50496)" SQ SEQUENCE 494 AA; 58010 MW; 56C1EC0D832CEF10 CRC64; MATFKDACFH YRRVTKLNRE LLRIGANSVW TPVSSNKIKI KGWCIECCQL TGLTFCHGCS LAHVCQWCIQ NKRCFLDNEP HLLKLRTFES PITKEKLQCI INLYELLFPI NHGVINKFKK TIKQRKCRNE FDKSWYNQLL LPITLNAAVF KFHSRDVYVF GFYEGSSPCI DLPYRLVNCI DLYDKLLLDQ VNFERMSSLP DNLQSIYANK YFKLSRLPSM KLKRIYYSDF SKQNLINKYK TKSRIVLRNL TEFTWDSQTD LHHDLINDKD KILAALSTSS LKQFETHDLN LGRIKADIFE LGHHCKPNYI SSNHWQPASK ISKCKWCNVK YAFRDMDWKM ESMYNELLSF IQSCYKSNVN VGHCSSIEKA YPLVKDILWH SITEYIDQTV EKLFNTMNPV QVNEQQVIKF CWQIDIALYM HIKMILETEA LPFTFTLNQF NSIIKGIVNQ WCDVAELDHL PLCTEQTDAL VKLEEEGKLS EEYELLISDS EDDD //