ID NSP1_ROTPC Reviewed; 393 AA. AC Q00033; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 08-NOV-2023, entry version 65. 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 C (strain RVC/Pig/United States/Cowden/1980) (RV-C). OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes; OC Reovirales; Sedoreoviridae; Rotavirus; Rotavirus C. OX NCBI_TaxID=10916; OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=8389118; DOI=10.1007/bf01318998; RA Bremont M., Chabanne-Vautherot D., Cohen J.; RT "Sequence analysis of three non structural proteins of a porcine group C RT (Cowden strain) rotavirus."; RL Arch. Virol. 130:85-92(1993). 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 -!- SIMILARITY: Belongs to the rotavirus NSP1 family. {ECO:0000255|HAMAP- CC Rule:MF_04088}. 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; X60546; CAA43036.1; -; mRNA. DR PIR; A48357; A48357. DR Proteomes; UP000008175; 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. 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..393 FT /note="Non-structural protein 1" FT /id="PRO_0000149560" FT REGION 2..79 FT /note="RNA-binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT REGION 39..77 FT /note="Zinc-binding domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT REGION 80..170 FT /note="Important for cytoskeleton localization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" FT REGION 267..393 FT /note="Interaction with host IRF3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088" SQ SEQUENCE 393 AA; 46438 MW; DB7FAD9AE2E3636F CRC64; MANSYREMLY WFGKTIDRNL PYVNTNGWRK QKGRKDGICL NCLDECKLYS CDHCGIKHKC GNCVLSECFL DVKNEFNKYR WLVFDEEPDQ AVLLQHWIMY KDYFLQKFNY RLATQAKILN MNKNQKFQLN EGRKRALSVP ITSQFLKFRL FGKIYIQFGT IMTNKIQPWL ELSTLKIGYL QLLNVERCSE LMATRGQFTT NVAKTACITE IKCRRPIYDN DCIIEAYLDK NDRGWKFAAI LGRRKIPVTQ KLAMEYFMKS LRAELFYYAH SRCHTLSNCP RWNEGLRLLN SSTLNIVFRR QFMNEIVEWF EIFSQYTGSH YEFITECVHD KSAITAFKQE IEDYIKEGKQ ITLKSVVPEE HAAYRHILRL RESLMLAIDA ALSRIRSQSM GVL //