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NCAP_HRSVB
ID   NCAP_HRSVB              Reviewed;         391 AA.
AC   O42053;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   23-FEB-2022, entry version 65.
DE   RecName: Full=Nucleoprotein;
DE            Short=Protein N;
DE   AltName: Full=Nucleocapsid protein;
GN   Name=N;
OS   Human respiratory syncytial virus B (strain B1).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX   NCBI_TaxID=79692;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9391135; DOI=10.1073/pnas.94.25.13961;
RA   Karron R.A., Buonagurio D.A., Georgiu A.F., Whitehead S.S., Adamus J.E.,
RA   Clements-Mann M.L., Harris D.O., Randolph V.B., Udem S.A., Murphy B.R.,
RA   Sidhu M.S.;
RT   "Respiratory syncytial virus (RSV) SH and G proteins are not essential for
RT   viral replication in vitro: clinical evaluation and molecular
RT   characterization of a cold-passaged, attenuated RSV subgroup B mutant.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:13961-13966(1997).
CC   -!- FUNCTION: Encapsidates the viral RNA genome by forming a left-handed
CC       helical nucleocapsid that protects the RNA from nucleases. RNA
CC       replication depends on the availability of soluble nucleoprotein. The
CC       encapsidated genomic RNA is termed the NC and serves as template for
CC       transcription and replication. Together with the phosphoprotein,
CC       sequesters host NF-kappa-B in inclusion bodies (IBs) thereby inhibiting
CC       this host defense pathway. May also act as a modulator of the innate
CC       immune response by sequestration of host IFIH1/MDA5 and MAVS into IBs.
CC       {ECO:0000250|UniProtKB:P03418}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. Interacts (via N-terminus) with the phosphoprotein P (via
CC       C-terminus); the phosphorylated phosphoprotein P binds to N-RNA
CC       complex. When in a monomeric RNA-free form, interacts with the
CC       phosphoprotein (via N-terminus). Interacts with protein M2-1; this
CC       interaction allows the association of nucleocapsid with the matrix
CC       protein. Interacts with host EIF2AK2/PKR; this interaction inhibits
CC       EIF2AK2 phosphorylation of EIF2S1 and blocks EIF2AK2-mediated
CC       translation shutoff. 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 (By similarity). {ECO:0000250|UniProtKB:P03418,
CC       ECO:0000250|UniProtKB:P22677}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03418}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P03418}. Note=Localizes in cytoplasmic
CC       inclusion bodies. {ECO:0000250|UniProtKB:P03418}.
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; AF013254; AAB82431.1; -; Genomic_RNA.
DR   EMBL; AF013255; AAB82442.1; -; Genomic_RNA.
DR   RefSeq; NP_056858.1; NC_001781.1.
DR   SMR; O42053; -.
DR   PRIDE; O42053; -.
DR   GeneID; 1489820; -.
DR   KEGG; vg:1489820; -.
DR   Proteomes; UP000002472; Genome.
DR   Proteomes; UP000180717; 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   3: Inferred from homology;
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_0000365782"
FT   REGION          31..252
FT                   /note="Interaction with the phosphoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P03418"
FT   REGION          244..290
FT                   /note="Interaction with the phosphoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P22677"
FT   REGION          338..364
FT                   /note="Interaction with the phosphoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:P22677"
FT   MOD_RES         38
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P03418"
SQ   SEQUENCE   391 AA;  43411 MW;  9A2B4E578E3B6D35 CRC64;
     MALSKVKLND TLNKDQLLSS SKYTIQRSTG DNIDTPNYDV QKHLNKLCGM LLITEDANHK
     FTGLIGMLYA MSRLGREDTI KILKDAGYHV KANGVDITTY RQDINGKEMK FEVLTLSSLT
     SEIQVNIEIE SRKSYKKMLK EMGEVAPEYR HDSPDCGMII LCIAALVITK LAAGDRSGLT
     AVIRRANNVL KNEIKRYKGL IPKDIANSFY EVFEKHPHLI DVFVHFGIAQ SSTRGGSRVE
     GIFAGLFMNA YGSGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
     YHILNNPKAS LLSLTQFPNF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA KAYAEQLKEN
     GVINYSVLDL TAEELEAIKN QLNPKEDDVE L
 
 
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