ID   NSP1_ROTSH              Reviewed;         496 AA.
AC   A2T3M4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   14-DEC-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 (isolate RVA/Monkey/South Africa/SA11-H96/1958/G3P5B[2]) (RV-A)
OS   (Simian Agent 11 (isolate SI/South Africa/H96/58)).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Sedoreoviridae; Rotavirus; Rotavirus A.
OX   NCBI_TaxID=450149;
OH   NCBI_TaxID=60710; Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=17059839; DOI=10.1016/j.virol.2006.09.024;
RA   Small C., Barro M., Brown T.L., Patton J.T.;
RT   "Genome heterogeneity of SA11 rotavirus due to reassortment with 'O'
RT   agent.";
RL   Virology 359:415-424(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   -!- 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   -!- INTERACTION:
CC       A2T3M4; Q7Z434: MAVS; Xeno; NbExp=4; IntAct=EBI-9522123, EBI-995373;
CC       A2T3M4; P13481: TP53; Xeno; NbExp=2; IntAct=EBI-9522123, EBI-10816181;
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; DQ838599; ABG75773.1; -; Genomic_RNA.
DR   RefSeq; YP_002302219.1; NC_011500.2.
DR   SMR; A2T3M4; -.
DR   IntAct; A2T3M4; 2.
DR   GeneID; 7011353; -.
DR   KEGG; vg:7011353; -.
DR   Proteomes; UP000001119; 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   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; Reference proteome;
KW   RNA-binding; Viral immunoevasion.
FT   CHAIN           1..496
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000367821"
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          321..496
FT                   /note="Interaction with host IRF3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   MOTIF           486..489
FT                   /note="pLxIS motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
SQ   SEQUENCE   496 AA;  58565 MW;  5877EA0A0C078CAD CRC64;
     MATFKDACFH YRRLTALNRR LCNIGANSIC MPVPDAKIKG WCLECCQIAD LTHCYGCSLP
     HVCKWCVQNR RCFLDNEPHL LKLRTVKHPI TKDKLQCIID LYNIIFPIND KVIRKFERMI
     KQRKCRNQYK IEWYNHLLLP ITLNAAAFKF DENNLYYVFG LYEKSVSDIY APYRIVNFIN
     EFDKLLLDDI NFTRMSNLPI ELRNHYAKKY FQLSRLPSSK LKQIYFSDFT KETVIFNTYT
     KTPGRSIYRN VTEFNWRDEL ELYSDLKNDK NKLIAAMMTS KYTRFYAHDN NFGRLKMTIF
     ELGHHCQPNY VASNHPGNAS DIQYCKWCNI KYFLSKIDWR IRDMYNLLME FIKDCYKSNV
     NVGHCSSVEN IYPLIKRLIW SLFTNHMDQT IEEVFNHMSP VSVEGTNVIM LILGLNISLY
     NEIKRTLNVD SIPMVLNLNE FSSIVKSISS KWYNVDELDK LPMSIKSTEE LIEMKNSGTL
     TEEFELLISN SEDDNE
//