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NSP1_ROTS1
ID   NSP1_ROTS1              Reviewed;         495 AA.
AC   P15687;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   23-FEB-2022, entry version 88.
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-Both/G3P5B[2]) (RV-A) (Simian Agent 11 (strain
OS   Both)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=37137;
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2154894; DOI=10.1016/0042-6822(90)90117-a;
RA   Mitchell D.B., Both G.W.;
RT   "Conservation of a potential metal binding motif despite extensive sequence
RT   diversity in the rotavirus nonstructural protein NS53.";
RL   Virology 174:618-621(1990).
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; X14914; CAA33039.1; -; Genomic_RNA.
DR   PIR; S08215; MNXRSA.
DR   Proteomes; UP000007180; 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   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; Reference proteome;
KW   RNA-binding; Viral immunoevasion.
FT   CHAIN           1..495
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000149558"
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;  58484 MW;  D988A936CD1B534B CRC64;
     MATFKDACFH YRRLTALNRR LCNIGANSIC MPVPDEKIKG WCLECCQIAD LTHCYGCSLP
     HVCKWCVQNR RCFLDNEPHL LKLRTVKHPI TKDKLQCIID LYNIIFPIND KVIRKFERMI
     KQRKCRNQYK IEWYNHLLLP ITLNAAAFKF DENNLYYVFG LYEKSVSDIY APYRIVNFIN
     EFDKLLLDDI NFTRMSNLPI ELRTIMQEYF QLSRLPSSKL KQIYFSDFTK ETVIFNTYTK
     TPGRSIYRNV TEFNWRDELE LYSDLKNDKN KLIAAMMTSK YTRFYAHDNN FGRLKMTIFE
     LGHHCQPNYV ASNHPGNASD IQYCKWCNIK YFLSKIDWRI RDMYNLLMEF IKDCYKSNVN
     VGHCSSVENI YPLIKRLIWS LFTNHMDQTI EEVFNHMSPV SVEGTNVIML ILGLNISLYN
     EIKRTLNVDS IPMVLNLNEF SSIVKSISSK WYNVDELDKL PMSIKSTEEL IEMKNSGTLT
     EEFELLISNS EDDNE
 
 
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