ID   NCAP_ORSVW              Reviewed;         391 AA.
AC   Q83957;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, 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   Ovine respiratory syncytial virus (strain WSU 83-1578) (ORSV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Pneumoviridae; unclassified Pneumoviridae.
OX   NCBI_TaxID=79699;
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7996153; DOI=10.1099/0022-1317-75-12-3597;
RA   Alansari H.M., Potgieter L.N.D.;
RT   "Molecular cloning and sequence analysis of the phosphoprotein,
RT   nucleocapsid protein, matrix protein and 22K (M2) protein of the ovine
RT   respiratory syncytial virus.";
RL   J. Gen. Virol. 75:3597-3601(1994).
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. {ECO:0000250|UniProtKB:P03418}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Interacts with the
CC       phosphoprotein P. 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. {ECO:0000250|UniProtKB:P03418}.
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   -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC       {ECO:0000305}.
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DR   EMBL; U07233; AAA62434.1; -; mRNA.
DR   SMR; Q83957; -.
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: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   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 PKR by virus; Ribonucleoprotein; RNA-binding;
KW   Viral immunoevasion; Viral nucleoprotein; Virion.
FT   CHAIN           1..391
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142650"
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"
SQ   SEQUENCE   391 AA;  43422 MW;  F8191CEA860A370D CRC64;
     MALSKVKLND TFNKDQLLST SKYTIQRSTG DNIDIPNYDV QKHLNKLCGM LLITEDANHK
     FTGLIGMLYA MSRLGREDTL KILKDAGYQV KANGVDVITH RQDVNGKEMK FEVLTLVSLT
     SEVQVNIEVE SRKSYKKMLK EMGEVAPEYR HDSPDCGMIV LCIAALVIAK LAAGDRSGLT
     AVIRRANNVL KNEIERYKGL IPKDVANSFY EVFEKYPHYI DVFVHFGIAQ SSTRGGSRVE
     GIFAGLFMNA YGAGQVMLRW GVLAKSVKNI MLGHASVQAE MEQVVEVYEY AQKLGGEAGF
     YHILNNPKAS LLSLTQFPNF SSVVLGNAAG LGIMGEYRGT PRNQDLYDAA KAYAEQLKEN
     GVINYSVLDL TTEELEAIKN QLNPKDNDVE L