NSP1_ROTB4
ID NSP1_ROTB4 Reviewed; 491 AA.
AC Q8JZ13;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 23-FEB-2022, 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 A (strain RVA/Cow/United States/B641/XXXX/G6P7[5]) (RV-A).
OC Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX NCBI_TaxID=10928;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12560571; DOI=10.1099/vir.0.18558-0;
RA Mitzel D.N., Weisend C.M., White M.W., Hardy M.E.;
RT "Translational regulation of rotavirus gene expression.";
RL J. Gen. Virol. 84:383-391(2003).
RN [2]
RP INTERACTION WITH HUMAN IRF3.
RX PubMed=12186937; DOI=10.1128/jvi.76.18.9545-9550.2002;
RA Graff J.W., Mitzel D.N., Weisend C.M., Flenniken M.L., Hardy M.E.;
RT "Interferon regulatory factor 3 is a cellular partner of rotavirus NSP1.";
RL J. Virol. 76:9545-9550(2002).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF CYS-54; HIS-79 AND HIS-136.
RX PubMed=17251580; DOI=10.1099/vir.0.82255-0;
RA Graff J.W., Ewen J., Ettayebi K., Hardy M.E.;
RT "Zinc-binding domain of rotavirus NSP1 is required for proteasome-dependent
RT degradation of IRF3 and autoregulatory NSP1 stability.";
RL J. Gen. Virol. 88:613-620(2007).
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 ECO:0000269|PubMed:17251580}.
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 ECO:0000269|PubMed:17251580}.
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; AF458087; AAM21601.1; -; mRNA.
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 1: Evidence at protein 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..491
FT /note="Non-structural protein 1"
FT /id="PRO_0000367819"
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 ECO:0000269|PubMed:17251580"
FT REGION 82..176
FT /note="Important for cytoskeleton localization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT REGION 320..491
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 MUTAGEN 54
FT /note="C->A: 90% loss of IRF3 binding. Complete loss of
FT IRF3 degradation."
FT /evidence="ECO:0000269|PubMed:17251580"
FT MUTAGEN 79
FT /note="H->L: 95% loss of IRF3 binding. Complete loss of
FT IRF3 degradation."
FT /evidence="ECO:0000269|PubMed:17251580"
FT MUTAGEN 136
FT /note="H->L: 70% loss of IRF3 binding. No effect on IRF3
FT degradation."
FT /evidence="ECO:0000269|PubMed:17251580"
SQ SEQUENCE 491 AA; 58600 MW; B91058CEC1D07E54 CRC64;
MATFKDACYH YKKLNKLNSL VLKLGANDEW RPAPVTKYKG WCLDCCQYTN LTYCRGCALY
HVCQWCSQYN RCFLDEEPHL LRMRTFKDVV TKEDIEGLLT MYETLFPINE KLVNKFINSV
KQRKCRNEYL LEWYNHLLMP ITLQALTINL EDNVYYMFGY YDCMEHENQT PFQFVNLLEK
YDKLLLDDRN FHRMSHLPVI LQQEYALRYF SKSRFLSKGK KRLSRSDFSD NLMEDRHSPT
SLMQVVRNCI SIHIDDCEWN KACTLIVDAR NYISIMNSSY TEHYSVSQRC KLFTKYKFGI
VSKLVKPNYI FSSHESCALN VHNCKWCQIN NHYKVWEDFR LRKIYNNVMD FIRALVKSNV
NVGHCSSQES VYKYVPDLFL ICKTEKWSEA VEMLFNYLEP VNVNGTEYVL LDYEVNWEVR
GLVMQNMDGK VPRILNMNDT KKILSAMIFD WFDTRYMRET PMTTSTTNQL RTLNKRNELI
DEYDLELSDV E
