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NCAP_CVMS
ID   NCAP_CVMS               Reviewed;         454 AA.
AC   P18448;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   03-AUG-2022, entry version 91.
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 S) (MHV-S) (Murine hepatitis virus).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=11145;
OH   NCBI_TaxID=10090; Mus musculus (Mouse).
RN   [1]
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).
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}.
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}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC       endoplasmic reticulum-Golgi intermediate compartment
CC       {ECO:0000255|HAMAP-Rule:MF_04096}. Host Golgi apparatus
CC       {ECO:0000255|HAMAP-Rule:MF_04096}. Note=Located inside the virion,
CC       complexed with the viral RNA. Probably associates with ER-derived
CC       membranes where it participates in viral RNA synthesis and virus
CC       budding. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC       during infection. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR   EMBL; M35255; AAA46468.1; -; Genomic_RNA.
DR   PIR; C45340; C45340.
DR   SMR; P18448; -.
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   3: Inferred from homology;
KW   ADP-ribosylation; Host Golgi apparatus; Phosphoprotein; Ribonucleoprotein;
KW   RNA-binding; Transcription; Transcription regulation; Viral nucleoprotein;
KW   Virion.
FT   CHAIN           1..454
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000106010"
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          159..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..292
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          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         170
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         177
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
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   MOD_RES         424
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         428
FT                   /note="Phosphothreonine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
SQ   SEQUENCE   454 AA;  49587 MW;  4992187AB0EB131E CRC64;
     MSFVPGQENA GSRSSSGSRS GNGILKKTTW ADQTERAGNN GNRGRRNQPK QTATTQPNSG
     SVVPHYSWFS GITQFQKGKE FQFVQGQGVP IANGIPASEQ KGYWYRHNRR SFKTPDGQQK
     QLLPRWYFYY LGTGPHAGAE YGDDIEGVVW VASQQADTKT TADIVERDPS SHEAIPTRFA
     PGTVLPQGFY VEGSGRSAPA SRSGSRSQSR GPNNRARSSS NQRQPASTVK PDMAEEIAAL
     VLAKLGKDAG QPKQVTKQSA KEVRQKILNK PRQKRTPNKQ CPVQQCFGKR GPNQNFGGSE
     MLKLGTSDPQ FPILAELAPT AGAFFFGSKL ELVKKNSGGA DEPTKDVYEL QYSGAVRFDS
     TLPGFETIMK VLNENLNAYQ KDGGADVVSP KPQRKGRRQA QEKKDEVDNV SVAKPKSSVQ
     RNVSRELTPE DRSLLAQILD DGVVPDGLED DSNV
 
 
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