NCAP_CVM3
ID NCAP_CVM3 Reviewed; 454 AA.
AC P18447;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 02-JUN-2021, entry version 97.
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 3) (MHV-3) (Murine hepatitis virus).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=11140;
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).
RN [2]
RP MUTAGENESIS, AND 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).
CC -!- FUNCTION: Major structural component of virions that associates with
CC genomic RNA to form a long, flexible, helical nucleocapsid. Interaction
CC with the M protein leads to the formation of virus particles. Binds to
CC cellular membranes and phospholipids. Elicits cell-mediated immunity.
CC May play roles in viral transcription and translation, and/or
CC replication. Induces transcription of the prothrombinase (FGL2) and
CC elevates procoagulant activity. {ECO:0000269|PubMed:12594208}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M35254; AAA46444.1; -; Genomic_RNA.
DR PIR; B45340; B45340.
DR BMRB; P18447; -.
DR SMR; P18447; -.
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 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_0000106006"
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 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"
FT MUTAGEN 12
FT /note="G->S: Almost no FGL2 transcription."
FT /evidence="ECO:0000269|PubMed:12594208"
FT MUTAGEN 38
FT /note="P->L: Almost no FGL2 transcription."
FT /evidence="ECO:0000269|PubMed:12594208"
FT MUTAGEN 38
FT /note="Missing: Almost no FGL2 transcription."
FT /evidence="ECO:0000269|PubMed:12594208"
FT MUTAGEN 40..42
FT /note="Missing: Almost no FGL2 transcription."
FT /evidence="ECO:0000269|PubMed:12594208"
FT MUTAGEN 85
FT /note="E->Q: No effect on FGL2 transcription."
FT /evidence="ECO:0000269|PubMed:12594208"
FT MUTAGEN 321
FT /note="V->A: No effect on FGL2 transcription."
FT /evidence="ECO:0000269|PubMed:12594208"
SQ SEQUENCE 454 AA; 49687 MW; 9C46DB2317E3A849 CRC64;
MSFVPGQENA GGRSSSGNRA 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
