ID   NSP1_ROTPC              Reviewed;         393 AA.
AC   Q00033;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 60.
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 C (strain RVC/Pig/United States/Cowden/1980) (RV-C).
OC   Viruses; Riboviria; Orthornavirae; Duplornaviricota; Resentoviricetes;
OC   Reovirales; Reoviridae; Sedoreovirinae; Rotavirus.
OX   NCBI_TaxID=10916;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8389118; DOI=10.1007/bf01318998;
RA   Bremont M., Chabanne-Vautherot D., Cohen J.;
RT   "Sequence analysis of three non structural proteins of a porcine group C
RT   (Cowden strain) rotavirus.";
RL   Arch. Virol. 130:85-92(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   -!- SIMILARITY: Belongs to the rotavirus NSP1 family. {ECO:0000255|HAMAP-
CC       Rule:MF_04088}.
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DR   EMBL; X60546; CAA43036.1; -; mRNA.
DR   PIR; A48357; A48357.
DR   Proteomes; UP000008175; 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.
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; Reference proteome;
KW   RNA-binding; Viral immunoevasion.
FT   CHAIN           1..393
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000149560"
FT   REGION          2..79
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   REGION          39..77
FT                   /note="Zinc-binding domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   REGION          80..170
FT                   /note="Important for cytoskeleton localization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
FT   REGION          267..393
FT                   /note="Interaction with host IRF3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04088"
SQ   SEQUENCE   393 AA;  46438 MW;  DB7FAD9AE2E3636F CRC64;
     MANSYREMLY WFGKTIDRNL PYVNTNGWRK QKGRKDGICL NCLDECKLYS CDHCGIKHKC
     GNCVLSECFL DVKNEFNKYR WLVFDEEPDQ AVLLQHWIMY KDYFLQKFNY RLATQAKILN
     MNKNQKFQLN EGRKRALSVP ITSQFLKFRL FGKIYIQFGT IMTNKIQPWL ELSTLKIGYL
     QLLNVERCSE LMATRGQFTT NVAKTACITE IKCRRPIYDN DCIIEAYLDK NDRGWKFAAI
     LGRRKIPVTQ KLAMEYFMKS LRAELFYYAH SRCHTLSNCP RWNEGLRLLN SSTLNIVFRR
     QFMNEIVEWF EIFSQYTGSH YEFITECVHD KSAITAFKQE IEDYIKEGKQ ITLKSVVPEE
     HAAYRHILRL RESLMLAIDA ALSRIRSQSM GVL