位置:首页 > 蛋白库 > NS1_BRSVA
NS1_BRSVA
ID   NS1_BRSVA               Reviewed;         136 AA.
AC   Q65694; Q77L04;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   23-FEB-2022, entry version 72.
DE   RecName: Full=Non-structural protein 1;
DE   AltName: Full=Non-structural protein 1C;
GN   Name=1C; Synonyms=NS1;
OS   Bovine respiratory syncytial virus (strain A51908) (BRS).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=11247;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7844532; DOI=10.1099/0022-1317-76-1-193;
RA   Pastey M.K., Samal S.K.;
RT   "Nucleotide sequence analysis of the non-structural NS1 (1C) and NS2 (1B)
RT   protein genes of bovine respiratory syncytial virus.";
RL   J. Gen. Virol. 76:193-197(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=A51908, and ATCC 51908;
RX   PubMed=11724268; DOI=10.1023/a:1011888019966;
RA   Yunus A.S., Khattar S.K., Collins P.L., Samal S.K.;
RT   "Rescue of bovine respiratory syncytial virus from cloned cDNA: entire
RT   genome sequence of BRSV strain A51908.";
RL   Virus Genes 23:157-164(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=10954520; DOI=10.1128/jvi.74.18.8234-8242.2000;
RA   Schlender J., Bossert B., Buchholz U., Conzelmann K.K.;
RT   "Bovine respiratory syncytial virus nonstructural proteins NS1 and NS2
RT   cooperatively antagonize alpha/beta interferon-induced antiviral
RT   response.";
RL   J. Virol. 74:8234-8242(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=12885884; DOI=10.1128/jvi.77.16.8661-8668.2003;
RA   Bossert B., Marozin S., Conzelmann K.K.;
RT   "Nonstructural proteins NS1 and NS2 of bovine respiratory syncytial virus
RT   block activation of interferon regulatory factor 3.";
RL   J. Virol. 77:8661-8668(2003).
CC   -!- FUNCTION: Plays a major role in antagonizing the type I IFN-mediated
CC       antiviral response by degrading or inhibiting multiple cellular factors
CC       required for either IFN induction or response pathways. Acts
CC       cooperatively with NS2 to repress activation and nuclear translocation
CC       of host IFN-regulatory factor IRF3. Also disrupts the association of
CC       IRF3 with CREBBP. Interacts with host mitochondrial-associated membrane
CC       (MAM) MAVS and prevents the interaction with DDX58/RIG-I. Interacts
CC       with TRIM25 to suppress TRIM25-mediated DDX58 ubiquitination and
CC       thereby DDX58-MAVS interaction. Together with NS2, participates in the
CC       proteasomal degradation of host STAT2, IRF3, IRF7, TBK1 and DDX58/RIG-I
CC       through a NS-degradasome involving CUL2 and Elongin-C. The degradasome
CC       requires an intact mitochondrial MAVS. Decreases the levels of host
CC       TRAF3 and IKBKE/IKK-epsilon. As functions other than disruptions of the
CC       type I IFN-mediated antiviral signaling pathways, induces host SOCS1
CC       and SOCS3 expression. Suppresses premature apoptosis by an NF-kappa-B-
CC       dependent, interferon-independent mechanism and thus facilitates virus
CC       growth. Additionally, NS1 may serve some inhibitory role in viral
CC       transcription and RNA replication. Suppresses proliferation and
CC       activation of host CD103+ CD8+ cytotoxic T-lymphocytes and Th17 helper
CC       T-lymphocytes. {ECO:0000250|UniProtKB:P0DOE9}.
CC   -!- SUBUNIT: Monomer. Homomultimer. Heteromultimer with NS2. Interacts with
CC       the matrix protein M. Interacts with host ELOC and CUL2; this
CC       interaction allows NS1 to form an active E3 ligase with ELOC and CUL2.
CC       Interacts with host IRF3; this interaction leads to the disrupted
CC       association of IRF3 with CREBBP and thus reduced binding of IRF3 to the
CC       IFN-beta promoter. Interacts with host MAVS; this interaction prevents
CC       MAVS binding to DDX58 and inhibits signaling pathway leading to
CC       interferon production. Interacts with host TRIM25 (via SPRY domain);
CC       this interaction suppresses DDX58 ubiquitination and results in
CC       decreased interaction between DDX58 and MAVS.
CC       {ECO:0000250|UniProtKB:P0DOE9}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250|UniProtKB:P0DOE9}.
CC       Host mitochondrion {ECO:0000250|UniProtKB:P0DOE9}. Host nucleus
CC       {ECO:0000250|UniProtKB:P0DOE9}. Note=Most NS1 resides in the
CC       mitochondria as a heteromer with NS2. {ECO:0000250|UniProtKB:P0DOE9}.
CC   -!- SIMILARITY: Belongs to the pneumovirus non-structural protein 1 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U15937; AAA85671.1; -; mRNA.
DR   EMBL; AF295543; AAL49392.1; -; Genomic_RNA.
DR   EMBL; AF295544; AAL49403.1; -; Genomic_RNA.
DR   RefSeq; NP_048048.1; NC_001989.1.
DR   SMR; Q65694; -.
DR   GeneID; 1489807; -.
DR   KEGG; vg:1489807; -.
DR   Proteomes; UP000007616; Genome.
DR   GO; GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0039504; P:suppression by virus of host adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0039564; P:suppression by virus of host JAK-STAT cascade via inhibition of STAT2 activity; IEA:UniProtKB-KW.
DR   GO; GO:0039722; P:suppression by virus of host toll-like receptor signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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-KW.
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-KW.
DR   GO; GO:0039545; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity; IEA:UniProtKB-KW.
DR   GO; GO:0039723; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005099; Pneumo_NS1.
DR   Pfam; PF03438; Pneumo_NS1; 1.
PE   2: Evidence at transcript level;
KW   Host cytoplasm; Host mitochondrion; Host nucleus; Host-virus interaction;
KW   Inhibition of host adaptive immune response by virus;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host IRF3 by virus; Inhibition of host IRF7 by virus;
KW   Inhibition of host MAVS by virus; Inhibition of host RIG-I by virus;
KW   Inhibition of host RLR pathway by virus; Inhibition of host STAT2 by virus;
KW   Inhibition of host TBK1 by virus; Inhibition of host TLR pathway by virus;
KW   Interferon antiviral system evasion;
KW   Modulation of host cell apoptosis by virus; Reference proteome;
KW   Viral immunoevasion.
FT   CHAIN           1..136
FT                   /note="Non-structural protein 1"
FT                   /id="PRO_0000142780"
SQ   SEQUENCE   136 AA;  15247 MW;  AEB6A89D7BED2D24 CRC64;
     MGSETLSVIQ VRLRNIYDND KVALLKITCH TNRLILLTHT LAKSVIHTIK LSGIVFIHII
     TSSDYCPTSD IINSANFTSM PILQNGGYIW ELMELTHCFQ TNGLIDDNCE ITFSKRLSDS
     ELAKYSNQLS TLLGLN
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024