ID   NCAP_MEASH              Reviewed;         525 AA.
AC   P10050;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   29-SEP-2021, entry version 76.
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 Halle) (MeV) (Subacute sclerose panencephalitis
OS   virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC   Morbillivirus.
OX   NCBI_TaxID=11236;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3211755; DOI=10.1093/nar/16.24.11821;
RA   Buckland R., Gerald C., Barker D., Wild F.;
RT   "Cloning and sequencing of the nucleoprotein gene of measles virus (Halle
RT   strain).";
RL   Nucleic Acids Res. 16:11821-11821(1988).
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).
RN   [3]
RP   3D-STRUCTURE, AND ELECTRON MICROSCOPY.
RX   PubMed=15136034; DOI=10.1016/j.jmb.2004.03.073;
RA   Schoehn G., Mavrakis M., Albertini A., Wade R., Hoenger A., Ruigrok R.W.;
RT   "The 12 A structure of trypsin-treated measles virus N-RNA.";
RL   J. Mol. Biol. 339:301-312(2004).
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; X13480; CAA31831.1; -; mRNA.
DR   PIR; A34040; VHNZMH.
DR   PDB; 4UFT; EM; 4.30 A; B=1-391.
DR   PDBsum; 4UFT; -.
DR   SMR; P10050; -.
DR   DIP; DIP-61650N; -.
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   3D-structure; 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_0000142656"
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;  58160 MW;  09DE00E733068485 CRC64;
     MATLLRSLAL FKRNKDKPPI TSGSGGAIRG IKHIIIVPIP GDSSITTRSR LLDRLVRLIG
     NPDVSGPKLT GALIGILSLF VESPGQLIQR ITDDPDVSIR LLEVVQSDQS QSGLTFASRG
     TNMEDEADQY FSHDDPISSD QSRFGWFENK EISDIEVQDP EGFNMILGTI LAQIWVLVAK
     AVTAPDTAAD SELRRWIKYT QQRRVVGEFR LERKWLDVVR NRIAEDLSLR RFMVALILDI
     KRTPGNKPRI AEMICNIDTY IVEAGLASFI LTIKFGIETM YPALGLHEFD GELSTLESLM
     NLYQQMGETA PYMVILENSI QNKFSAGSYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA
     YFRLGQEMVR RSAGKVSSTL ASELGITAED ARLVSEIAMH TTEDKISRAV GPRQAQVSFL
     HGDQSENELP RLGGKEDRRV KQSRGEARES YRETGPSRAS DARAAHLPTG TPLDIDTASE
     SSQDPQDSRR SADALLRLQA MAGISEEQGS DTDTPIVYND RNLLD