NCAP_BRSV3
ID NCAP_BRSV3 Reviewed; 391 AA.
AC P35943;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 23-FEB-2022, entry version 66.
DE RecName: Full=Nucleoprotein;
DE Short=Protein N;
DE AltName: Full=Nucleocapsid protein;
GN Name=N;
OS Bovine respiratory syncytial virus (strain 391-2) (BRS).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Pneumoviridae; Orthopneumovirus.
OX NCBI_TaxID=31611;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1634882; DOI=10.1099/0022-1317-73-4-999;
RA Amann V.L., Lerch R.A., Anderson K., Wertz G.W.;
RT "Bovine respiratory syncytial virus nucleocapsid protein: mRNA sequence
RT analysis and expression from recombinant vaccinia virus vectors.";
RL J. Gen. Virol. 73:999-1003(1992).
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 with the phosphoprotein P. When in a monomeric
CC RNA-free form, interacts with the phosphoprotein (via N-terminus).
CC Interacts with protein M2-1; this interaction allows the association of
CC nucleocapsid with the matrix protein. Interacts with host EIF2AK2/PKR;
CC this interaction inhibits EIF2AK2 phosphorylation of EIF2S1 and blocks
CC EIF2AK2-mediated translation shutoff. Interacts with host EIF1AX; this
CC interaction recruits EIF1AX to the viral replication complex to
CC facilitate viral genomic RNA synthesis and virus production (By
CC similarity). Interacts with host NF-kappa-B; this interaction
CC sequesters NF-kappa-B in inclusion bodies (By similarity).
CC {ECO:0000250|UniProtKB:P03418, 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; S40504; AAB22601.1; -; mRNA.
DR PIR; JQ1533; JQ1533.
DR SMR; P35943; -.
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 2: Evidence at transcript 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; Ribonucleoprotein;
KW RNA-binding; Viral immunoevasion; Viral nucleoprotein; Virion.
FT CHAIN 1..391
FT /note="Nucleoprotein"
FT /id="PRO_0000142647"
FT REGION 1..364
FT /note="Involved in RNA synthesis and encapsidation"
FT /evidence="ECO:0000250|UniProtKB:P22677"
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; 43557 MW; ABBCC2AD5534D23C CRC64;
MALSKVKLND TFNKDQLLST SKYTIQRSTG DNIDIPNYDV QKHLNKLCGM LLITEDANHK
FTGLIGMLYA MSRLGREDTL KILKDAGYQV RANGVDVITH RQDVNGKEMK FEVLTLVSLT
SEVQGNIEIE SRKSYKKMLK EMGEVAPEYR HDFPDCGMIV LCVAALVITK LAAGDRSGLT
AVIRRANNVL RNEMKRYKGL IPKDIANSFY EVFEKYPHYI DVFVHFGIAQ SSTRGGSRVE
GIFAGLFMNA YGAGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
YHILNNPKAS LLSLTQFPNF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA KAYAEQLKEN
GVINYSVLDL TTEELEAIKN QLNPKDNDVE L
