NCAP_MEASM
ID NCAP_MEASM Reviewed; 525 AA.
AC Q77M43; Q89794;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, 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 Edmonston-Moraten vaccine) (MeV) (Subacute sclerose
OS panencephalitis virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=132484;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8291252; DOI=10.1006/viro.1994.1086;
RA Rota P.A., Bloom A.E., Vanchiere J.A., Bellini W.J.;
RT "Evolution of the nucleoprotein and matrix genes from wild-type strains of
RT measles virus isolated from recent epidemics.";
RL Virology 198:724-730(1994).
RN [2]
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 [3]
RP INTERACTION WITH PHOSPHOPROTEIN.
RX PubMed=15280472; DOI=10.1128/jvi.78.16.8630-8640.2004;
RA Kingston R.L., Baase W.A., Gay L.S.;
RT "Characterization of nucleocapsid binding by the measles virus and mumps
RT virus phosphoproteins.";
RL J. Virol. 78:8630-8640(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 -!- INTERACTION:
CC Q77M43; Q77M42: P; NbExp=2; IntAct=EBI-21943629, EBI-21943616;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC {ECO:0000250}.
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; U01999; AAA18998.1; -; mRNA.
DR EMBL; AF266287; AAF85667.1; -; Genomic_RNA.
DR PIR; PQ0386; PQ0386.
DR PDB; 1T6O; X-ray; 2.00 A; B=486-505.
DR PDB; 6H5S; EM; 3.30 A; C=1-405.
DR PDBsum; 1T6O; -.
DR PDBsum; 6H5S; -.
DR BMRB; Q77M43; -.
DR SMR; Q77M43; -.
DR IntAct; Q77M43; 1.
DR EvolutionaryTrace; Q77M43; -.
DR Proteomes; UP000154340; 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 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_0000142658"
FT REGION 1..400
FT /note="Ncore"
FT /evidence="ECO:0000250"
FT REGION 1..375
FT /note="Homomultimerization"
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 COMPBIAS 428..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 13..16
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 45..59
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 66..76
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 77..80
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 98..106
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 160..171
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 172..177
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 228..241
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 261..265
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 267..275
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:6H5S"
FT TURN 313..317
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:6H5S"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6H5S"
FT HELIX 486..502
FT /evidence="ECO:0007829|PDB:1T6O"
SQ SEQUENCE 525 AA; 58073 MW; 10D0D3A538761717 CRC64;
MATLLRSLAL FKRNKDKPPI TSGSGGAIRG IKHIIIVPIP GDSSITTRSR LLDRLVRLIG
NPDVSGPKLT GALIGILSLF VESPGQLIQR ITDDPDVSIR LLEVVQSDQS QSGLTFASRG
TNMEDEADQY FSHDDPISSD QSRFGWFGNK EISDIEVQDP EGFNMILGTI LAQIWVLLAK
AVTAPDTAAD SELRRWIKYT QQRRVVGEFR LERKWLDVVR NRIAEDLSLR RFMVALILDI
KRTPGNKPRI AEMICDIDTY IVEAGLASFI LTIKFGIETM YPALGLHEFA GELSTLESLM
NLYQQMGETA PYMVILENSI QNKFSAGSYP LLWSYAMGVG VELENSMGGL NFGRSYFDPA
YFRLGQEMVR RSAGKVSSTL ASELGITAED ARLVSEIAMH TTEDKISRAV GPRQAQVSFL
HGDQSENELP RLGGKEDRRV KQSRGEARES YRETGPSRAS DARAAHLPTG TPLDIDTATE
SSQDPQDSRR SADALLRLQA MAGISEEQGS DTDTPIVYND RNLLD
