ID   NCAP_MEASI              Reviewed;         525 AA.
AC   P26029;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   29-SEP-2021, entry version 71.
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 IP-3-Ca) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11237;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1585658; DOI=10.1016/0042-6822(92)90552-z;
RA   Schmid A., Spielhofer P., Cattaneo R., Baczko K., Ter Meulen V.,
RA   Billeter M.A.;
RT   "Subacute sclerosing panencephalitis is typically characterized by
RT   alterations in the fusion protein cytoplasmic domain of the persisting
RT   measles virus.";
RL   Virology 188:910-915(1992).
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; X16566; CAA34563.1; -; Genomic_RNA.
DR   SMR; P26029; -.
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   3: Inferred from homology;
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_0000142657"
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..525
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          418..525
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        428..456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   525 AA;  58207 MW;  34D3471E57129E55 CRC64;
     MATLLRSLAL FKRNKDKPPI TSGSGGAIRG IKHIIIVPIP GDSSITTRSR LLDRLVRLTG
     NPDVSGPKLT GALIGILSLF VESPGQLIQR ITDDPGVSIR LLEVVQSDQS QSGLTFASRG
     TNMEDEADQY FSHDDPSSSA QSRFGWFENK EISDIEVQDP EGFNMILGTI LAQIWVLLAK
     AVTAPDTAAD SELRRWIKYT QQRRVVGEFR LERKWLDVVR NRIAEDLPLR RFMVALILDI
     KRTPGNKPRI AEMICDIDTY IVEAGLASFI LTIKFGIETM YPALGLHEFA GELSTLESLM
     NLYQQMGETA PYMVILENSI QNKFSAGSYP LLWSYAMGVG VELENSMGGL NFSRSYFDPA
     YFRLGQEMVR RSAGKVSSTL ASELGITAED ARLVSEIAMH TTEDRISRAV GPRQAQVSFL
     HGDQSENEPP RWGGKEDMRV KQSRGEARES YRETGPSRAS DARAAHLPTD TPLDIDTASE
     SSQDPQDSRR SAEALLRLQA MAGISEEQGS DTDTPRVYND RDLLD