NCAP_MEASF
ID NCAP_MEASF Reviewed; 525 AA.
AC Q89933; O92927; Q77M21; Q77M26; Q77M32; Q783Q8; Q83520; Q83523; Q83526;
AC Q83726; Q89890; Q91QN7; Q9IC39;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 02-JUN-2021, entry version 79.
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 B) (MeV) (Subacute sclerose panencephalitis
OS virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Paramyxoviridae; Orthoparamyxovirinae;
OC Morbillivirus.
OX NCBI_TaxID=70146;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA], AND RETRACTED PAPER.
RX PubMed=2303032; DOI=10.1002/j.1460-2075.1990.tb08121.x;
RA Ballart I., Eschle D., Cattaneo R., Schmid A., Metzler M., Chan J.,
RA Pifko-Hirst S., Udem S.A., Billeter M.A.;
RT "Infectious measles virus from cloned cDNA.";
RL EMBO J. 9:379-384(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8191786; DOI=10.1016/0168-1702(94)90025-6;
RA Rota J.S., Wang Z.D., Rota P.A., Bellini W.J.;
RT "Comparison of sequences of the H, F, and N coding genes of measles virus
RT vaccine strains.";
RL Virus Res. 31:317-330(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Philadelphia-26;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8846771; DOI=10.1002/j.1460-2075.1995.tb00266.x;
RA Radecke F., Spielhofer P., Schneider H., Kaelin K., Huber M., Doetsch C.,
RA Christiansen G., Billeter M.A.;
RT "Rescue of measles viruses from cloned DNA.";
RL EMBO J. 14:5773-5784(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=China93-5;
RX PubMed=9696123; DOI=10.1016/s0168-1702(98)00020-3;
RA Xu W.B., Tamin A., Rota J.S., Zhang L., Bellini W.J., Rota P.A.;
RT "New genetic group of measles virus isolated in the People's Republic of
RT China.";
RL Virus Res. 54:147-156(1998).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Billeter M.A.;
RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=China93-5;
RA Xu W.B., Tamin A., Rota J.S., LiBi Z., Bellini W.J., Rota P.A.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Komase K., Suzuki N., Nakayama T., Miki K., Kawanishi R., Fukuda K.;
RT "The phosophoprotein of attenuated measles virus vaccine strain, AIK-C,
RT contributes to its temperature-sensitive phenotype.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Baricevic M., Forcic D., Kosutic Gulija T., Jug R., Mazuran R.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Zhao D.;
RT "The whole gene sequence of Measles virus.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP RETRACTION NOTICE OF PUBMED:2303032.
RX PubMed=1915308; DOI=10.1002/j.1460-2075.1991.tb04920.x;
RA Eschle D., Cattaneo R., Schmid A., Metzler M., Chan J., Pifko-Hirst S.,
RA Udem S.A., Billeter M.A.;
RL EMBO J. 10:3558-3558(1991).
RN [13]
RP INTERACTION WITH HUMAN FCGR2B.
RX PubMed=15914856; DOI=10.1099/vir.0.80791-0;
RA Laine D., Bourhis J.-M., Longhi S., Flacher M., Cassard L., Canard B.,
RA Sautes-Fridman C., Rabourdin-Combe C., Valentin H.;
RT "Measles virus nucleoprotein induces cell-proliferation arrest and
RT apoptosis through NTAIL-NR and NCORE-FcgammaRIIB1 interactions,
RT respectively.";
RL J. Gen. Virol. 86:1771-1784(2005).
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.
CC {ECO:0000269|PubMed:15914856}.
CC -!- INTERACTION:
CC Q89933; P03422: P/V; Xeno; NbExp=3; IntAct=EBI-8589867, EBI-8589851;
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.
CC -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC {ECO:0000305}.
CC -!- CAUTION: The strains used in this publication turn out to be Edmonston
CC strain viruses, contrasting with their claimed origin from reconsituted
CC measles virus genomic cDNAs containing a genetic tag.
CC {ECO:0000305|PubMed:1915308}.
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DR EMBL; Z66517; CAA91363.1; -; Genomic_RNA.
DR EMBL; U03650; AAA56640.1; -; Genomic_RNA.
DR EMBL; U03653; AAA56643.1; -; Genomic_RNA.
DR EMBL; U03656; AAA56646.1; -; Genomic_RNA.
DR EMBL; U03658; AAA56648.1; -; Genomic_RNA.
DR EMBL; U03661; AAA56651.1; -; Genomic_RNA.
DR EMBL; U01987; AAA18986.1; -; mRNA.
DR EMBL; U01991; AAA18990.1; -; mRNA.
DR EMBL; U01992; AAA18991.1; -; mRNA.
DR EMBL; U01993; AAA18992.1; -; mRNA.
DR EMBL; U01994; AAA18993.1; -; mRNA.
DR EMBL; U01996; AAA18995.1; -; mRNA.
DR EMBL; AF045218; AAC03050.1; -; Genomic_RNA.
DR EMBL; AF266286; AAF85659.1; -; Genomic_RNA.
DR EMBL; AF266288; AAF85675.1; -; Genomic_RNA.
DR EMBL; AF266289; AAF85683.1; -; Genomic_RNA.
DR EMBL; AF266290; AAF85691.1; -; Genomic_RNA.
DR EMBL; AF266291; AAF85699.1; -; Genomic_RNA.
DR EMBL; AB046218; BAB60861.1; -; Genomic_RNA.
DR EMBL; AB052821; BAB60956.1; -; Genomic_RNA.
DR EMBL; AY486083; AAR32652.1; -; Genomic_RNA.
DR EMBL; AY486084; AAR32660.1; -; Genomic_RNA.
DR EMBL; AY730614; AAV84954.1; -; Genomic_RNA.
DR PIR; A49601; A49601.
DR PIR; PQ0386; PQ0386.
DR PDB; 5E4V; X-ray; 2.71 A; A=21-408.
DR PDBsum; 5E4V; -.
DR SMR; Q89933; -.
DR IntAct; Q89933; 1.
DR MINT; Q89933; -.
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:0039643; C:host cell viral nucleoid; IMP:CAFA.
DR GO; GO:0019013; C:viral nucleocapsid; IMP:CAFA.
DR GO; GO:0030544; F:Hsp70 protein binding; IPI:CAFA.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0039656; P:modulation by virus of host gene expression; IMP:CAFA.
DR GO; GO:0050434; P:positive regulation of viral transcription; IMP:CAFA.
DR DisProt; DP00640; -.
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_0000142655"
FT REGION 1..400
FT /note="Ncore"
FT REGION 1..375
FT /note="Homomultimerization"
FT /evidence="ECO:0000250"
FT REGION 401..525
FT /note="Ntail"
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"
FT VARIANT 58
FT /note="L -> S"
FT VARIANT 129
FT /note="Q -> K"
FT VARIANT 137
FT /note="I -> S"
FT VARIANT 148
FT /note="E -> G"
FT VARIANT 262
FT /note="V -> G"
FT VARIANT 405
FT /note="K -> R"
FT VARIANT 434
FT /note="G -> A"
FT VARIANT 448
FT /note="R -> G"
FT VARIANT 465
FT /note="A -> T"
FT VARIANT 474
FT /note="D -> A"
FT VARIANT 478
FT /note="A -> V"
FT VARIANT 479
FT /note="S -> T"
FT VARIANT 483
FT /note="Q -> L"
FT VARIANT 487
FT /note="D -> G"
FT VARIANT 493..494
FT /note="DA -> EP"
FT VARIANT 516
FT /note="I -> R"
FT VARIANT 521
FT /note="R -> G"
FT VARIANT 522
FT /note="N -> D"
FT STRAND 33..43
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 45..60
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:5E4V"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 84..91
FT /evidence="ECO:0007829|PDB:5E4V"
FT STRAND 95..106
FT /evidence="ECO:0007829|PDB:5E4V"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 160..183
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:5E4V"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:5E4V"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 306..309
FT /evidence="ECO:0007829|PDB:5E4V"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 313..316
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 318..323
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 359..384
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 388..403
FT /evidence="ECO:0007829|PDB:5E4V"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5E4V"
SQ SEQUENCE 525 AA; 58131 MW; 3C35DF4458769BA0 CRC64;
MATLLRSLAL FKRNKDKPPI TSGSGGAIRG IKHIIIVPIP GDSSITTRSR LLDRLVRLIG
NPDVSGPKLT GALIGILSLF VESPGQLIQR ITDDPDVSIR LLEVVQSDQS QSGLTFASRG
TNMEDEADQY FSHDDPISSD QSRFGWFENK 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 TPLDIDTASE
SSQDPQDSRR SADALLRLQA MAGISEEQGS DTDTPIVYND RNLLD
