NCAP_CVMA5
ID NCAP_CVMA5 Reviewed; 454 AA.
AC P03416; P18449; Q86648;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 02-JUN-2021, entry version 118.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04096};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04096}; ORFNames=7a;
OS Murine coronavirus (strain A59) (MHV-A59) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11142;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6687635; DOI=10.1093/nar/11.3.883;
RA Armstrong J., Smeekens S., Rottier P.J.M.;
RT "Sequence of the nucleocapsid gene from murine coronavirus MHV-A59.";
RL Nucleic Acids Res. 11:883-891(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND SEQUENCE REVISION.
RA Armstrong J., Smeekens S., Spaan W.J.M., Rottier P.J.M.,
RA van der Zeijst B.A.M.;
RT "Cloning and sequencing of the nucleocapsid and E1 genes of coronavirus.";
RL (In) Rottier P.J.M., van der Zeijst B.A.M., Spaan W.J.M., Horzinek M.
RL (eds.);
RL Molecular biology and pathogenesis of coronaviruses, pp.155-162, Plenum
RL Press, New York (1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2171216; DOI=10.1016/0042-6822(90)90316-j;
RA Parker M.M., Masters P.S.;
RT "Sequence comparison of the N genes of five strains of the coronavirus
RT mouse hepatitis virus suggests a three domain structure for the
RT nucleocapsid protein.";
RL Virology 179:463-468(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate C12 mutant;
RX PubMed=9426441; DOI=10.1006/viro.1997.8877;
RA Leparc-Goffart I., Hingley S.T., Chua M.M., Jiang X., Lavi E., Weiss S.R.;
RT "Altered pathogenesis of a mutant of the murine coronavirus MHV-A59 is
RT associated with a Q159L amino acid substitution in the spike protein.";
RL Virology 239:1-10(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 301-454.
RX PubMed=8395114; DOI=10.1006/viro.1993.1467;
RA Schaad M.C., Baric R.S.;
RT "Evidence for new transcriptional units encoded at the 3' end of the mouse
RT hepatitis virus genome.";
RL Virology 196:190-198(1993).
RN [6]
RP FUNCTION.
RX PubMed=12594208; DOI=10.1074/jbc.m212806200;
RA Ning Q., Lakatoo S., Liu M., Yang W., Wang Z., Phillips M.J., Levy G.A.;
RT "Induction of prothrombinase fgl2 by the nucleocapsid protein of virulent
RT mouse hepatitis virus is dependent on host hepatic nuclear factor-4
RT alpha.";
RL J. Biol. Chem. 278:15541-15549(2003).
RN [7]
RP PHOSPHORYLATION AT SER-162; SER-170; THR-177; SER-389; SER-424 AND THR-428.
RX PubMed=17367888; DOI=10.1016/j.virusres.2007.02.008;
RA White T.C., Yi Z., Hogue B.G.;
RT "Identification of mouse hepatitis coronavirus A59 nucleocapsid protein
RT phosphorylation sites.";
RL Virus Res. 126:139-148(2007).
RN [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17210170; DOI=10.1016/j.virol.2006.11.027;
RA Stertz S., Reichelt M., Spiegel M., Kuri T., Martinez-Sobrido L.,
RA Garcia-Sastre A., Weber F., Kochs G.;
RT "The intracellular sites of early replication and budding of SARS-
RT coronavirus.";
RL Virology 361:304-315(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH NSP3.
RX PubMed=23760243; DOI=10.1128/jvi.01275-13;
RA Hurst K.R., Koetzner C.A., Masters P.S.;
RT "Characterization of a critical interaction between the coronavirus
RT nucleocapsid protein and nonstructural protein 3 of the viral replicase-
RT transcriptase complex.";
RL J. Virol. 87:9159-9172(2013).
RN [10]
RP FUNCTION.
RX PubMed=28591694; DOI=10.18632/oncotarget.17912;
RA Ding Z., Fang L., Yuan S., Zhao L., Wang X., Long S., Wang M., Wang D.,
RA Foda M.F., Xiao S.;
RT "The nucleocapsid proteins of mouse hepatitis virus and severe acute
RT respiratory syndrome coronavirus share the same IFN-beta antagonizing
RT mechanism: attenuation of PACT-mediated RIG-I/ MDA5 activation.";
RL Oncotarget 8:49655-49670(2017).
RN [11]
RP SUBUNIT.
RX PubMed=28720894; DOI=10.1038/s41598-017-06062-w;
RA Cong Y., Kriegenburg F., de Haan C.A.M., Reggiori F.;
RT "Coronavirus nucleocapsid proteins assemble constitutively in high
RT molecular oligomers.";
RL Sci. Rep. 7:5740-5740(2017).
RN [12]
RP ADP-RIBOSYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=29199039; DOI=10.1016/j.virol.2017.11.020;
RA Grunewald M.E., Fehr A.R., Athmer J., Perlman S.;
RT "The coronavirus nucleocapsid protein is ADP-ribosylated.";
RL Virology 517:62-68(2018).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 60-197.
RX PubMed=19782089; DOI=10.1016/j.jmb.2009.09.040;
RA Grossoehme N.E., Li L., Keane S.C., Liu P., Dann C.E. III, Leibowitz J.L.,
RA Giedroc D.P.;
RT "Coronavirus N protein N-terminal domain (NTD) specifically binds the
RT transcriptional regulatory sequence (TRS) and melts TRS-cTRS RNA
RT duplexes.";
RL J. Mol. Biol. 394:544-557(2009).
CC -!- FUNCTION: Packages the positive strand viral genome RNA into a helical
CC ribonucleocapsid (RNP) and plays a fundamental role during virion
CC assembly through its interactions with the viral genome and membrane
CC protein M. Plays an important role in enhancing the efficiency of
CC subgenomic viral RNA transcription as well as viral replication.
CC {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:12594208,
CC ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:23760243}.
CC -!- SUBUNIT: Homooligomer. Both monomeric and oligomeric forms interact
CC with RNA. Interacts with protein M. Interacts with NSP3; this
CC interaction serves to tether the genome to the newly translated
CC replicase-transcriptase complex at a very early stage of infection.
CC {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:23760243,
CC ECO:0000269|PubMed:28720894}.
CC -!- INTERACTION:
CC P03416; O75569: PRKRA; Xeno; NbExp=6; IntAct=EBI-25639341, EBI-713955;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:29199039}. Host endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:17210170}. Host Golgi apparatus {ECO:0000255|HAMAP-
CC Rule:MF_04096}. Note=Located inside the virion, complexed with the
CC viral RNA. Probably associates with ER-derived membranes where it
CC participates in viral RNA synthesis and virus budding.
CC {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:29199039}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17367888}.
CC -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR EMBL; X00509; CAA25198.1; -; Genomic_RNA.
DR EMBL; M35256; AAA46447.1; -; Genomic_RNA.
DR EMBL; AF029248; AAB86821.1; -; Genomic_RNA.
DR EMBL; S64884; AAB27902.1; -; Genomic_DNA.
DR PIR; A45340; A45340.
DR RefSeq; NP_045302.1; NC_001846.1.
DR PDB; 3HD4; X-ray; 1.75 A; A=60-197.
DR PDBsum; 3HD4; -.
DR BMRB; P03416; -.
DR SMR; P03416; -.
DR IntAct; P03416; 2.
DR iPTMnet; P03416; -.
DR GeneID; 1489757; -.
DR KEGG; vg:1489757; -.
DR EvolutionaryTrace; P03416; -.
DR Proteomes; UP000007192; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
DR HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR043505; NCAP_bCoV.
DR InterPro; IPR001218; Nucleocap_CoV.
DR InterPro; IPR037179; Nucleocapsid_C.
DR InterPro; IPR037195; Nucleocapsid_N.
DR Pfam; PF00937; CoV_nucleocap; 1.
DR PIRSF; PIRSF003888; Corona_nucleocap; 1.
DR SUPFAM; SSF103068; SSF103068; 1.
DR SUPFAM; SSF110304; SSF110304; 1.
DR PROSITE; PS51929; COV_N_CTD; 1.
DR PROSITE; PS51928; COV_N_NTD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Host Golgi apparatus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Transcription;
KW Transcription regulation; Viral nucleoprotein; Virion.
FT CHAIN 1..454
FT /note="Nucleoprotein"
FT /id="PRO_0000106007"
FT DOMAIN 64..193
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 260..383
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..197
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 160..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..383
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 271..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 162
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:17367888"
FT MOD_RES 170
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:17367888"
FT MOD_RES 177
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:17367888"
FT MOD_RES 194
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 389
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:17367888"
FT MOD_RES 424
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:17367888"
FT MOD_RES 428
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:17367888"
FT CONFLICT 262
FT /note="E -> K (in Ref. 1 and 2)"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3HD4"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3HD4"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:3HD4"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:3HD4"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:3HD4"
SQ SEQUENCE 454 AA; 49729 MW; 7C4978F20954A227 CRC64;
MSFVPGQENA GGRSSSVNRA GNGILKKTTW ADQTERGPNN QNRGRRNQPK QTATTQPNSG
SVVPHYSWFS GITQFQKGKE FQFAEGQGVP IANGIPASEQ KGYWYRHNRR SFKTPDGQQK
QLLPRWYFYY LGTGPHAGAS YGDSIEGVFW VANSQADTNT RSDIVERDPS SHEAIPTRFA
PGTVLPQGFY VEGSGRSAPA SRSGSRSQSR GPNNRARSSS NQRQPASTVK PDMAEEIAAL
VLAKLGKDAG QPKQVTKQSA KEVRQKILNK PRQKRTPNKQ CPVQQCFGKR GPNQNFGGSE
MLKLGTSDPQ FPILAELAPT VGAFFFGSKL ELVKKNSGGA DEPTKDVYEL QYSGAVRFDS
TLPGFETIMK VLNENLNAYQ KDGGADVVSP KPQRKGRRQA QEKKDEVDNV SVAKPKSSVQ
RNVSRELTPE DRSLLAQILD DGVVPDGLED DSNV
