ID   NCAP_PPRV               Reviewed;         525 AA.
AC   Q08823;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   29-SEP-2021, entry version 72.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Peste-des-petits-ruminants virus (PPRV).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=31604;
OH   NCBI_TaxID=9925; Capra hircus (Goat).
OH   NCBI_TaxID=9940; Ovis aries (Sheep).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8113734; DOI=10.1099/0022-1317-75-1-233;
RA   Diallo A., Barrett T., Barbron M., Meyer G., Lefevre P.C.;
RT   "Cloning of the nucleocapsid protein gene of peste-des-petits-ruminants
RT   virus: relationship to other morbilliviruses.";
RL   J. Gen. Virol. 75:233-237(1994).
RN   [2]
RP   INTERACTION WITH HUMAN NR PROTEIN.
RX   PubMed=14557619; DOI=10.1128/jvi.77.21.11332-11346.2003;
RA   Laine D., Trescol-Biemont M.C., Longhi S., Libeau G., Marie J.C.,
RA   Vidalain P.O., Azocar O., Diallo A., Canard B., Rabourdin-Combe C.,
RA   Valentin H.;
RT   "Measles virus (MV) nucleoprotein binds to a novel cell surface receptor
RT   distinct from FcgammaRII via its C-terminal domain: role in MV-induced
RT   immunosuppression.";
RL   J. Virol. 77:11332-11346(2003).
CC   -!- FUNCTION: Encapsidates the genome in a ratio of 1 N per 6
CC       ribonucleotides, protecting it from nucleases. The nucleocapsid (NC)
CC       has a helical structure. The encapsidated genomic RNA is termed the NC
CC       and serves as template for transcription and replication. During
CC       replication, encapsidation by N is coupled to RNA synthesis and all
CC       replicative products are resistant to nucleases. N is released in the
CC       blood following lysis of infected cells, it interacts then probably
CC       with FCGR2B on immune cells, inducing apoptosis and blocking
CC       inflammatory immune response. Ntail binds to a protein on thymic
CC       epithelial cells, termed Nucleoprotein Receptor (NR), inducing growth
CC       arrest (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. In nucleocapsid, binds the P protein and thereby positions
CC       the polymerase on the template. Interacts with human FCGR2B protein ex
CC       vivo (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC   -!- DOMAIN: Ncore is globular and carries regions required for N self-
CC       assembly and RNA-binding. Ntail is an intrinsically disordered
CC       monomeric domain (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC       {ECO:0000305}.
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DR   EMBL; X74443; CAA52454.1; -; mRNA.
DR   PIR; S36405; S36405.
DR   SMR; Q08823; -.
DR   Proteomes; UP000180906; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR002021; Paramyx_ncap.
DR   Pfam; PF00973; Paramyxo_ncap; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Helical capsid protein; Host cytoplasm;
KW   Host-virus interaction; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..525
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142674"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          401..525
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          418..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          506..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        442..459
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58032 MW;  079E477792E95D9C CRC64;
     MATLLKSLAL FKRNKDKAPT ASGSGGAIRG IKNVIIVPIP GDSSIITRSR LLDRLVRLAG
     DPDINGSKLT GVMISMLSLF VESPGQLIQR ITDDPDVSIR LVEVVQSTRS QSGLTFASRG
     ADLDNEADMY FSTEGPSSGS KKRINWFENR EIIDIEVQDA EEFNMLLASI LAQVWILLAK
     AVTAPDTAAD SELRRWVKYT QQRRVIGEFR LDKGWLDAVR NRIAEDLSLR RFMVSLILDI
     KRTPGNKPRI AEMICDIDNY IVEAGLASFI LTIKFGIETM YPALGLHEFA GELSTIESLM
     NLYQQLGEVA PYMVILENSI QNKFSAGAYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA
     YFRLGQEMVR RSAGKVSSVI AAELGITAEE AKLVSEIASQ TGDERTVRGT GPRQAQVSFL
     QHKTDEGESP TPATREEVKA AIPNGSEGRD TKRTRSGKPR GETPGQLLPE IMQEDELSRE
     SSQNPREAQR SAEALFRLQA MAKILEDQEE GEDNSQIYND KDLLS