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NSS_TOSV
ID   NSS_TOSV                Reviewed;         316 AA.
AC   P21699;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Non-structural protein NS-S;
DE            Short=NSs;
GN   Name=NSS;
OS   Toscana virus (Tos).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Phenuiviridae; Phlebovirus;
OC   Toscana phlebovirus.
OX   NCBI_TaxID=11590;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=13204; Phlebotomus perniciosus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1846496; DOI=10.1016/0042-6822(91)90087-r;
RA   Giorgi C., Accardi L., Nicoletti L., Gro M.C., Takehara K., Hilditch C.,
RA   Morikawa S., Bishop D.H.L.;
RT   "Sequences and coding strategies of the S RNAs of Toscana and Rift Valley
RT   fever viruses compared to those of Punta Toro, Sicilian Sandfly fever, and
RT   Uukuniemi viruses.";
RL   Virology 180:738-753(1991).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH HOST DDX58.
RX   PubMed=23552410; DOI=10.1128/jvi.03129-12;
RA   Gori-Savellini G., Valentini M., Cusi M.G.;
RT   "Toscana Virus NSs protein inhibits the induction of type I interferon by
RT   interacting with RIG-I.";
RL   J. Virol. 87:6660-6667(2013).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HOST EIF2AK2/PKR.
RX   PubMed=23325696; DOI=10.1128/jvi.02506-12;
RA   Kalveram B., Ikegami T.;
RT   "Toscana virus NSs protein promoftes degradation of double-stranded RNA-
RT   dependent protein kinase.";
RL   J. Virol. 87:3710-3718(2013).
CC   -!- FUNCTION: Promotes the proteasomal degradation of host EIF2AK2/PKR but
CC       is unable to suppress host general transcription (PubMed:23325696).
CC       Prevents the establishment of the host antiviral state by interfering
CC       with beta interferon (IFN-beta) production. Interacts with host
CC       DDX58/RIG-I and targets it for proteasomal degradation, thereby
CC       inhibiting DDX58-mediated signaling pathway (PubMed:23552410).
CC       {ECO:0000269|PubMed:23325696, ECO:0000269|PubMed:23552410}.
CC   -!- SUBUNIT: Interacts with host DDX58; this interaction targets DDX58 to
CC       proteasomal degradation (PubMed:23552410). Interacts with host
CC       EIF2AK2/PKR; this interaction leads to the proteasomal degradation of
CC       host EIF2AK2/PKR (PubMed:23325696). {ECO:0000269|PubMed:23325696,
CC       ECO:0000269|PubMed:23552410}.
CC   -!- INTERACTION:
CC       P21699; O95786: DDX58; Xeno; NbExp=3; IntAct=EBI-6693910, EBI-995350;
CC   -!- SIMILARITY: Belongs to the phlebovirus NS-S protein family.
CC       {ECO:0000305}.
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DR   EMBL; X53794; CAA37802.1; -; Genomic_RNA.
DR   PIR; A38552; MNVUTV.
DR   SMR; P21699; -.
DR   IntAct; P21699; 1.
DR   Proteomes; UP000204292; Genome.
DR   GO; GO:0039540; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity; IDA:UniProtKB.
DR   InterPro; IPR039434; NSs-like.
DR   Pfam; PF11073; NSs; 1.
PE   1: Evidence at protein level;
KW   Host-virus interaction; Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host PKR by virus; Inhibition of host RIG-I by virus;
KW   Inhibition of host RLR pathway by virus; Viral immunoevasion.
FT   CHAIN           1..316
FT                   /note="Non-structural protein NS-S"
FT                   /id="PRO_0000221981"
SQ   SEQUENCE   316 AA;  36678 MW;  EEA752F082D9A411 CRC64;
     MQSRAVILKY RSGSGHKRSL PRFYIDCDLD TFDFEKDCSL IENEFPIYIN NYKVVYKSKP
     TLSHFLIEKE FPAVLGPGMI SAVRTRLYEP TMRELYQESI HQLKRSNKKY LLSALRWPTG
     IPTLEFIDYY FEELLFLSEF DPGSIQRYLK LLVKASGLYN STNEEQIVEI HRRVLIEGKK
     HGLTAFDLPG NDILGDICVV QAARVTRLVA KTFSKMTRDT HLMIYFSISP VELVLSKLDK
     KGDKRAKAKG LMSMSAARSY DYFMRTDLGF RETALSTFWA KDWPTPQETI LSDKRCLKED
     MRVTKWLPSP PHYPPL
 
 
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