NCAP_HRSV1
ID NCAP_HRSV1 Reviewed; 391 AA.
AC P24566;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 23-FEB-2022, entry version 71.
DE RecName: Full=Nucleoprotein;
DE Short=Protein N;
DE AltName: Full=Nucleocapsid protein;
GN Name=N;
OS Human respiratory syncytial virus B (strain 18537).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=11251;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2525176; DOI=10.1099/0022-1317-70-6-1539;
RA Johnson P.R., Collins P.L.;
RT "The 1B (NS2), 1C (NS1) and N proteins of human respiratory syncytial virus
RT (RSV) of antigenic subgroups A and B: sequence conservation and divergence
RT within RSV genomic RNA.";
RL J. Gen. Virol. 70:1539-1547(1989).
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}.
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; D00736; BAA00637.1; -; Genomic_RNA.
DR PIR; C32063; VHNZ3.
DR SMR; P24566; -.
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; Ribonucleoprotein;
KW RNA-binding; Viral immunoevasion; Viral nucleoprotein; Virion.
FT CHAIN 1..391
FT /note="Nucleoprotein"
FT /id="PRO_0000142651"
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; 43416 MW; 9A2BBB50103B2835 CRC64;
MALSKVKLND TLNKDQLLSS SKYTIQRSTG DNIDTPNYDV QKHLNKLCGM LLITEDANHK
FTGLIGMLYA MSRLGREDTI KILKDAGYHV KANGVDITTY RQDINGKEMK FEVLTLSSLT
SEIQVNIEIE SRKSYKKLLK EMGEVAPEYR HDSPDCGMII LCIAALVITK LAAGDRSGLT
AVIRRANNVL KNEIKRYKGL IPKDIANSFY EVFEKHPHLI DVFVHFGIAQ SSTRGGSRVE
GIFAGLFMNA YGSGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
YHILNNPKAS LLSLTQFPNF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA KAYAEQLKEN
GVINYSVLDL TAEELEAIKH QLNPKEDDVE L
