ID   NCAP_MEASE              Reviewed;         523 AA.
AC   P04851;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   23-FEB-2022, entry version 81.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Measles virus (strain Edmonston) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11235;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3838193; DOI=10.1128/jvi.53.2.684-690.1985;
RA   Rozenblatt S., Eizenberg O., Ben-Levy R., Lavie V., Bellini W.J.;
RT   "Sequence homology within the morbilliviruses.";
RL   J. Virol. 53:684-690(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-165.
RX   PubMed=6198802; DOI=10.1016/0042-6822(84)90099-0;
RA   Billeter M.A., Baczko K., Schmid A., Ter Meulen V.;
RT   "Cloning of DNA corresponding to four different measles virus genomic
RT   regions.";
RL   Virology 132:147-159(1984).
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 with either 12.35 or 11.64 N per turn,
CC       approximately 20 nm in diameter, with a hollow central cavity
CC       approximately 5 nm in diameter. The encapsidated genomic RNA is termed
CC       the NC 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 measles infected cells, it interacts then with
CC       human FCGR2B on immune cells, inducing apoptosis and blocking
CC       inflammatory immune response. Ntail binds to a protein on human thymic
CC       epithelial cells, termed Nucleoprotein Receptor (NR), inducing growth
CC       arrest.
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 (By
CC       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; X01999; CAA26031.1; -; mRNA.
DR   EMBL; K01711; AAA75494.1; ALT_SEQ; Genomic_RNA.
DR   PIR; A04027; VHNZMV.
DR   SMR; P04851; -.
DR   Proteomes; UP000000833; 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; IDA:CACAO.
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   2: Evidence at transcript level;
KW   Capsid protein; Helical capsid protein; Host cytoplasm;
KW   Host-virus interaction; Reference proteome; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..523
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142654"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          1..375
FT                   /note="Homomultimerization"
FT                   /evidence="ECO:0000250"
FT   REGION          401..523
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          418..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..505
FT                   /note="P protein-binding"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        429..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        474..490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   523 AA;  58105 MW;  51544BF86C349BD6 CRC64;
     MATLLRSLAL FKRNKDKPPI TSGSGGAIRG IKHIIIVPIP GDSSITTRSR LLDRLVRLIG
     NPDVSGPKLT GALIGILSLF VESPGQLIQR ITDDPDVSIR LLEVVQSDQS QSGLTFASRG
     TNMEDEADQY FSHDDPISSD QSRFGWFENK EISDIEVQDP EGFNMILGTI LAQIWVLLAK
     AVTAPDTAAD SELRRWIKYT QQRRVVGEFR LERKWLDVVR NIIAEDLSLR RFMVALILDI
     KRTPGNKPRI AEMICDIDTY IVEAGLASFI LTIKFGIETM YPALGLHEFA GELSTLESLM
     NLYQQMGKPA PYMVNLENSI QNKFSAGSYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA
     YFRLGQEMVR RSAGKVSSTL ASELGITAED ARLVSEIAMH TTEDKISRAV GPRQAQVSFL
     QGDQSENELP RLGGKEDRRV KQSRGEARES YRETGPSRAS DARAAHLPTG TPLDIDTASE
     SSQDPQDSRR SAEPLLSCKP WQESRKNKAQ TRTPLQCTMT EIF