NSP1_ROTSP
ID NSP1_ROTSP Reviewed; 495 AA.
AC P35425;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 67.
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/SA11-Patton/G3P[X]) (RV-A) (Simian Agent 11 (strain
OS Patton)).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=36434;
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8395125; DOI=10.1006/viro.1993.1492;
RA Hua J.J., Mansell E.E., Patton J.T.;
RT "Comparative analysis of the rotavirus NS53 gene: conservation of basic and
RT cysteine-rich regions in the protein and possible stem-loop structures in
RT the RNA.";
RL Virology 196:372-378(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 -!- 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}.
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DR EMBL; L18944; AAA47302.1; -; Genomic_RNA.
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 3: Inferred from homology;
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..495
FT /note="Non-structural protein 1"
FT /id="PRO_0000149559"
FT REGION 1..81
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT REGION 42..79
FT /note="Zinc-binding domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT REGION 82..177
FT /note="Important for cytoskeleton localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT REGION 320..495
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"
SQ SEQUENCE 495 AA; 58514 MW; CE267A63837B2E36 CRC64;
MATFKDACFH YRRLTALNRR LCNIGANSIW MPVPDAKIKG WCLECCQIAD LTHCYGCSLP
HVCKWCVQNR RCFLDNEPHL LKLQQLKHPI TKDKLQCIID LYNIIFPIND KVIRKFERMI
KQRECRNQYK IEWYNHKLLP ITLNAAAFKF DENNLYYVFG LYEKSVSDIY APYRIVNFIN
EFDKLLLDHI NFTRMSNLPI ELRAITQEYF QLSRLPSSKL KQIYFSDFTK ETVIFNTYTK
TPGRSIYRNV TEFNWRDELE LYTDLKNDKN KLIAAMMTSK YTRFYAHDNN FGRLKMTIFE
LGHHCQPNYV ASNHPGNASD IQYCKWCNIK YFLSKIDWRI RDMYNLLMEF IKDCYKSNVN
VGHCSSVENI YPLIKRLIWS LFTNHMDQTI EEVFNHMSPV SVEGTNVIML ILGLNISLYN
EIKRTLNVDS IPMVLNLNEF SSIVKSISSK WYNVDELDKL PMSIKSTEEL IEMKNSGTLT
EEFELLISNS EDDNE