NCAP_BRSVA
ID NCAP_BRSVA Reviewed; 391 AA.
AC P22677; Q77KZ2; Q77L02;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 23-FEB-2022, entry version 84.
DE RecName: Full=Nucleoprotein;
DE Short=Protein N;
DE AltName: Full=Nucleocapsid protein;
GN Name=N;
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=1984667; DOI=10.1016/0042-6822(91)90057-i;
RA Samal S.K., Zamora M., McPhillips T.H., Mohanty S.B.;
RT "Molecular cloning and sequence analysis of bovine respiratory syncytial
RT virus mRNA encoding the major nucleocapsid protein.";
RL Virology 180:453-456(1991).
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 INTERACTION WITH THE PHOSPHOPROTEIN.
RX PubMed=8609467; DOI=10.1099/0022-1317-77-5-1019;
RA Mallipeddi S.K., Lupiani B., Samal S.K.;
RT "Mapping the domains on the phosphoprotein of bovine respiratory syncytial
RT virus required for N-P interaction using a two-hybrid system.";
RL J. Gen. Virol. 77:1019-1023(1996).
RN [4]
RP INTERACTION WITH THE PHOSPHOPROTEIN, MUTAGENESIS OF LEU-3; CYS-48; CYS-156;
RP CYS-162 AND LEU-391, AND FUNCTION.
RX PubMed=10772994; DOI=10.1006/viro.2000.0264;
RA Khattar S.K., Yunus A.S., Collins P.L., Samal S.K.;
RT "Mutational analysis of the bovine respiratory syncytial virus nucleocapsid
RT protein using a minigenome system: mutations that affect encapsidation, RNA
RT synthesis, and interaction with the phosphoprotein.";
RL Virology 270:215-228(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOST NF-KAPPA-B.
RX PubMed=32878896; DOI=10.1128/jvi.01380-20;
RA Jobe F., Simpson J., Hawes P., Guzman E., Bailey D.;
RT "Respiratory syncytial virus sequesters NF-kappaB subunit p65 to
RT cytoplasmic inclusion bodies to inhibit innate immune signalling.";
RL J. Virol. 0:0-0(2020).
CC -!- FUNCTION: Encapsidates the viral RNA genome by forming a left-handed
CC helical nucleocapsid that protects the RNA from nucleases (Probable).
CC RNA replication depends on the availability of soluble nucleoprotein
CC (By similarity). The encapsidated genomic RNA is termed the NC and
CC serves as template for transcription and replication (By similarity).
CC Together with the phosphoprotein, sequesters host NF-kappa-B in
CC inclusion bodies (IBs) thereby inhibiting this host defense pathway
CC (PubMed:32878896). May also act as a modulator of the innate immune
CC response by sequestration of host IFIH1/MDA5 and MAVS into IBs (By
CC similarity). {ECO:0000250|UniProtKB:P03418,
CC ECO:0000269|PubMed:32878896, ECO:0000305|PubMed:10772994}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid (By similarity).
CC Binds to viral genomic RNA (By similarity). Interacts with the
CC phosphoprotein P (PubMed:8609467, PubMed:10772994). When in a monomeric
CC RNA-free form, interacts with the phosphoprotein (via N-terminus) (By
CC similarity). Interacts with protein M2-1; this interaction allows the
CC association of nucleocapsid with the matrix protein (By similarity).
CC Interacts with host EIF2AK2/PKR; this interaction inhibits EIF2AK2
CC phosphorylation of EIF2S1 and blocks EIF2AK2-mediated translation
CC shutoff (By similarity). Interacts with host EIF1AX; this interaction
CC recruits EIF1AX to the viral replication complex to facilitate viral
CC genomic RNA synthesis and virus production (By similarity). Interacts
CC with host NF-kappa-B; this interaction sequesters NF-kappa-B in
CC inclusion bodies (PubMed:32878896). {ECO:0000250|UniProtKB:P03418,
CC ECO:0000269|PubMed:10772994, ECO:0000269|PubMed:32878896,
CC ECO:0000269|PubMed:8609467}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03418}. Host
CC cytoplasm {ECO:0000269|PubMed:32878896}. Note=Localizes in cytoplasmic
CC inclusion bodies. {ECO:0000269|PubMed:32878896}.
CC -!- PTM: Tyrosine phosphorylation modulates viral transcription and
CC replication. {ECO:0000250|UniProtKB:P03418}.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
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DR EMBL; M35076; AAA42812.1; -; mRNA.
DR EMBL; AF295543; AAL49394.1; -; Genomic_RNA.
DR EMBL; AF295544; AAL49405.1; -; Genomic_RNA.
DR PIR; A38525; VHNZB4.
DR SMR; P22677; -.
DR DIP; DIP-1085N; -.
DR IntAct; P22677; 1.
DR Proteomes; UP000007616; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR GO; GO:0039580; P:suppression by virus of host PKR signaling; 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:0039554; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 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 InterPro; IPR004930; Pneumo_ncap.
DR Pfam; PF03246; Pneumo_ncap; 1.
PE 1: Evidence at protein level;
KW Capsid protein; Helical capsid protein; Host cytoplasm;
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 MAVS by virus; Inhibition of host MDA5 by virus;
KW Inhibition of host NF-kappa-B by virus; Inhibition of host PKR by virus;
KW Inhibition of host RLR pathway by virus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Viral immunoevasion;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..391
FT /note="Nucleoprotein"
FT /id="PRO_0000142648"
FT REGION 1..364
FT /note="Involved in RNA synthesis and encapsidation"
FT /evidence="ECO:0000269|PubMed:10772994"
FT REGION 244..290
FT /note="Interaction with the phosphoprotein"
FT /evidence="ECO:0000269|PubMed:10772994"
FT REGION 338..364
FT /note="Interaction with the phosphoprotein"
FT /evidence="ECO:0000269|PubMed:10772994"
FT MOD_RES 38
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P03418"
FT VARIANT 67
FT /note="I -> M (in strain: ATCC 51908)"
FT VARIANT 213
FT /note="I -> F (in strain: ATCC 51908)"
FT MUTAGEN 3
FT /note="L->A: Complete loss of encapsidation but no effect
FT on viral RNA synthesis."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 3
FT /note="L->E,K: About 80-95% inhibition of viral RNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 3
FT /note="L->G: No effect on viral RNA synthesis."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 48
FT /note="C->S: About 80-95% inhibition of viral RNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 156
FT /note="C->S: Complete loss of viral RNA synthesis and
FT encapsidation; when associated with S-162."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 162
FT /note="C->S: Complete loss of viral RNA synthesis and
FT encapsidation; when associated with S-156."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 391
FT /note="L->A,K: About 80-95% inhibition of viral RNA
FT synthesis."
FT /evidence="ECO:0000269|PubMed:10772994"
FT MUTAGEN 391
FT /note="L->E,G: Complete loss of viral RNA synthesis."
FT /evidence="ECO:0000269|PubMed:10772994"
SQ SEQUENCE 391 AA; 43445 MW; F6729E09F02E7F8A CRC64;
MALSKVKLND TFNKDQLLST SKYTIQRSTG DNIDIPNYDV QKHLNKLCGM LLITEDANHK
FTGLIGILYA MSRLGREDTL KILKDAGYQV RANGVDVITH RQDVNGKEMK FEVLTLVSLT
SEVQGNIEIE SRKSYKKMLK EMGEVAPEYR HDSPDCGMIV LCVAALVITK LAAGDRSGLT
AVIRRANNVL RNEMKRYKGL IPKDIANSFY EVIEKYPHYI DVFVHFGIAQ SSTRGGSRVE
GIFAGLFMNA YGAGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
YHILNNPKAS LLSLTQFPNF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA KAYAEQLKEN
GVINYSVLDL TTEELEAIKN QLNPKDNDVE L
