NSP1_ROTRH
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 23-FEB-2022, entry version 53.
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; Reoviridae; Sedoreovirinae; 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;
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DR EMBL; U08433; AAA50496.1; ALT_FRAME; Genomic_RNA.
DR EMBL; AY117048; AAM92466.1; -; mRNA.
DR EMBL; Z32535; CAA83546.1; -; Genomic_RNA.
DR PRIDE; Q6YLT2; -.
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
