ID   NCAP_MEASE              Reviewed;         525 AA.
AC   P04851;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   27-NOV-2024, sequence version 2.
DT   02-SEP-2026, entry version 90.
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; Morbillivirus hominis; Measles 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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11134304; DOI=10.1128/jvi.75.2.910-920.2001;
RA   Parks C.L., Lerch R.A., Walpita P., Wang H.P., Sidhu M.S., Udem S.A.;
RT   "Comparison of predicted amino acid sequences of measles virus strains in
RT   the Edmonston vaccine lineage.";
RL   J. Virol. 75:910-920(2001).
RN   [4]
RP   SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND NUCLEAR EXPORT
RP   SIGNAL.
RX   PubMed=16716375; DOI=10.1016/j.virol.2006.04.013;
RA   Sato H., Masuda M., Miura R., Yoneda M., Kai C.;
RT   "Morbillivirus nucleoprotein possesses a novel nuclear localization signal
RT   and a CRM1-independent nuclear export signal.";
RL   Virology 352:121-130(2006).
RN   [5]
RP   INTERACTION WITH THE PHOSPHOPROTEIN.
RX   PubMed=27936158; DOI=10.1371/journal.ppat.1006058;
RA   Bloyet L.M., Brunel J., Dosnon M., Hamon V., Erales J., Gruet A.,
RA   Lazert C., Bignon C., Roche P., Longhi S., Gerlier D.;
RT   "Modulation of Re-initiation of Measles Virus Transcription at Intergenic
RT   Regions by PXD to NTAIL Binding Strength.";
RL   PLoS Pathog. 12:e1006058-e1006058(2016).
CC   -!- FUNCTION: Forms the helical nucleocapsid (NC) in a ratio of 1 N per 6
CC       ribonucleotides, protecting the genome from nucleases (By similarity).
CC       The nucleocapsid (NC) has a helical structure with either 12.35 or
CC       11.64 N per turn, approximately 20 nm in diameter, with a hollow
CC       central cavity approximately 5 nm in diameter (By similarity). The
CC       encapsidated genomic RNA serves as template for transcription and
CC       replication; encapsidation by N is coupled to RNA synthesis (By
CC       similarity). Forms the encapsidation complex with the phosphoprotein
CC       protein P (By similarity). Before encapsidation, the newly synthesized
CC       free N protein, so-called N0, is chaperoned by P (By similarity).
CC       Participates, together with P, in the formation of viral factories
CC       (viroplasms), which are large inclusions in the host cytoplasm where
CC       replication takes place (By similarity). N is released in the blood
CC       following lysis of measles infected cells, it interacts then with human
CC       FCGR2B on immune cells, inducing apoptosis and blocking inflammatory
CC       immune response (By similarity). {ECO:0000250|UniProtKB:P06159,
CC       ECO:0000250|UniProtKB:P0DXN6, ECO:0000250|UniProtKB:P10050,
CC       ECO:0000250|UniProtKB:Q9WMB5}.
CC   -!- SUBUNIT: Homomultimer; forms the nucleocapsid (By similarity). Binds to
CC       viral genomic RNA (By similarity). N0 interacts (via Ncore) with the
CC       phosphoprotein (via N-terminus); this interaction allows P to chaperon
CC       N0 to avoid N polymerization and non-specific RNA binding before
CC       encapsidation (By similarity). Interacts as N-RNA template (via the
CC       Ntail) with the phosphoprotein (via C-terminus XD); this interaction
CC       maintains the P/L complex anchored to the nucleocapsid template during
CC       the sequential transcription (PubMed:27936158). Interacts with the
CC       phosphoprotein; this interaction leads to the formation of membraneless
CC       organelles that function as viral replication factories (By
CC       similarity). Interacts with human FCGR2B protein (By similarity).
CC       Interacts with human PPIA/CYPA and PPIB/CYPB (By similarity).
CC       {ECO:0000250|UniProtKB:O57286, ECO:0000250|UniProtKB:P06159,
CC       ECO:0000250|UniProtKB:P0DXN6, ECO:0000250|UniProtKB:Q07097,
CC       ECO:0000250|UniProtKB:Q77M43, ECO:0000250|UniProtKB:Q89933,
CC       ECO:0000250|UniProtKB:Q9WMB5, ECO:0000269|PubMed:27936158}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC       {ECO:0000269|PubMed:16716375}. Host nucleus
CC       {ECO:0000269|PubMed:16716375}.
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 in the C-terminus. {ECO:0000250|UniProtKB:Q89933}.
CC   -!- PTM: Phosphorylation at Thr-279 is required for the formation of the
CC       nucleocapsid. {ECO:0000250|UniProtKB:Q9WMB5}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC       {ECO:0000305}.
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DR   EMBL; X01999; CAA26031.1; ALT_SEQ; mRNA.
DR   EMBL; K01711; AAA75494.1; -; Genomic_RNA.
DR   EMBL; AF266288; AAF85675.1; -; Genomic_RNA.
DR   EMBL; AF266289; AAF85683.1; -; Genomic_RNA.
DR   PIR; A04027; VHNZMV.
DR   SMR; P04851; -.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0030430; C:host cell cytoplasm; EXP:UniProtKB.
DR   GO; GO:0042025; C:host cell nucleus; EXP:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Capsid protein; Helical capsid protein; Host cytoplasm; Host nucleus;
KW   Host-virus interaction; Phosphoprotein; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..525
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142654"
FT   REGION          1..403
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250|UniProtKB:P06159"
FT   REGION          1..375
FT                   /note="RNA packaging and organization of the helical
FT                   nucleocapsid"
FT                   /evidence="ECO:0000250|UniProtKB:Q89933"
FT   REGION          1..36
FT                   /note="Homomultimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P10050"
FT   REGION          373..391
FT                   /note="Homomultimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P10050"
FT   REGION          404..525
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250|UniProtKB:P06159"
FT   REGION          418..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..505
FT                   /note="Interaction with the phosphoprotein"
FT                   /evidence="ECO:0000250|UniProtKB:Q77M43"
FT   MOTIF           70..77
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:16716375"
FT   MOTIF           425..440
FT                   /note="Nuclear export signal"
FT                   /evidence="ECO:0000269|PubMed:16716375"
FT   COMPBIAS        433..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         180
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:Q77M43"
FT   BINDING         195
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:Q77M43"
FT   BINDING         202
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:Q77M43"
FT   BINDING         260
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:Q77M43"
FT   BINDING         351
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /evidence="ECO:0000250|UniProtKB:Q77M43"
FT   MOD_RES         279
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WMB5"
FT   VARIANT         222
FT                   /note="I -> R"
FT   VARIANT         308..309
FT                   /note="KP -> ET"
FT   VARIANT         315
FT                   /note="N -> I"
FT   VARIANT         421
FT                   /note="Q -> H"
FT   VARIANT         479
FT                   /note="S -> T"
FT   VARIANT         493..494
FT                   /note="EP -> DA"
FT   VARIANT         516
FT                   /note="T -> I"
SQ   SEQUENCE   525 AA;  58103 MW;  95D2B3AA1E205C77 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 SAEPLLRLQA MAGISEEQGS DTDTPTVYND RNLLD
//