NCAP_IBVB
ID NCAP_IBVB Reviewed; 409 AA.
AC P69596; Q4ZJS4; Q89902;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 02-JUN-2021, entry version 85.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04097};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04097};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04097};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04097};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04097}; ORFNames=6;
OS Avian infectious bronchitis virus (strain Beaudette) (IBV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Gammacoronavirus; Igacovirus.
OX NCBI_TaxID=11122;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2983001; DOI=10.1099/0022-1317-66-3-573;
RA Boursnell M.E.G., Binns M.M., Foulds I.J., Brown T.D.K.;
RT "Sequences of the nucleocapsid genes from two strains of avian infectious
RT bronchitis virus.";
RL J. Gen. Virol. 66:573-580(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3027249; DOI=10.1099/0022-1317-68-1-57;
RA Boursnell M.E.G., Brown T.D.K., Foulds I.J., Green P.F., Tomley F.M.,
RA Binns M.M.;
RT "Completion of the sequence of the genome of the coronavirus avian
RT infectious bronchitis virus.";
RL J. Gen. Virol. 68:57-77(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Vero cell-adapted p65;
RX PubMed=16137658; DOI=10.1016/j.bbrc.2005.08.105;
RA Fang S.G., Shen S., Tay F.P., Liu D.X.;
RT "Selection of and recombination between minor variants lead to the
RT adaptation of an avian coronavirus to primate cells.";
RL Biochem. Biophys. Res. Commun. 336:417-423(2005).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11119619; DOI=10.1128/jvi.75.1.506-512.2001;
RA Hiscox J.A., Wurm T., Wilson L., Britton P., Cavanagh D., Brooks G.;
RT "The coronavirus infectious bronchitis virus nucleoprotein localizes to the
RT nucleolus.";
RL J. Virol. 75:506-512(2001).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11533198; DOI=10.1128/jvi.75.19.9345-9356.2001;
RA Wurm T., Chen H., Hodgson T., Britton P., Brooks G., Hiscox J.A.;
RT "Localization to the nucleolus is a common feature of coronavirus
RT nucleoproteins, and the protein may disrupt host cell division.";
RL J. Virol. 75:9345-9356(2001).
RN [6]
RP PHOSPHORYLATION AT SER-190; SER-192; THR-378 AND SER-379, AND DISULFIDE
RP BONDS.
RX PubMed=15613344; DOI=10.1128/jvi.79.2.1164-1179.2005;
RA Chen H., Gill A., Dove B.K., Emmett S.R., Kemp C.F., Ritchie M.A., Dee M.,
RA Hiscox J.A.;
RT "Mass spectroscopic characterization of the coronavirus infectious
RT bronchitis virus nucleoprotein and elucidation of the role of
RT phosphorylation in RNA binding by using surface plasmon resonance.";
RL J. Virol. 79:1164-1179(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-160.
RX PubMed=16338414; DOI=10.1016/j.str.2005.08.021;
RA Fan H., Ooi A., Tan Y.W., Wang S., Fang S., Liu D.X., Lescar J.;
RT "The nucleocapsid protein of coronavirus infectious bronchitis virus:
RT crystal structure of its N-terminal domain and multimerization
RT properties.";
RL Structure 13:1859-1868(2005).
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_04097}.
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_04097}.
CC -!- INTERACTION:
CC P69596; P69596: N; NbExp=4; IntAct=EBI-15561295, EBI-15561295;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04097}. Host
CC endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|HAMAP-Rule:MF_04097}. Host Golgi apparatus
CC {ECO:0000255|HAMAP-Rule:MF_04097}. 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_04097}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04097}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04097, ECO:0000269|PubMed:15613344}.
CC -!- SIMILARITY: Belongs to the gammacoronavirus nucleocapsid protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04097}.
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DR EMBL; M95169; AAA70242.1; -; Genomic_RNA.
DR EMBL; M28565; AAA46214.1; -; Genomic_RNA.
DR EMBL; DQ001339; AAY24440.1; -; Genomic_RNA.
DR RefSeq; NP_040838.1; NC_001451.1.
DR PDB; 2BTL; X-ray; 1.95 A; A/B=29-160.
DR PDB; 2BXX; X-ray; 1.85 A; A/B=29-160.
DR PDB; 2CA1; X-ray; 2.60 A; A/B=218-326.
DR PDBsum; 2BTL; -.
DR PDBsum; 2BXX; -.
DR PDBsum; 2CA1; -.
DR SMR; P69596; -.
DR iPTMnet; P69596; -.
DR GeneID; 1489745; -.
DR KEGG; vg:1489745; -.
DR EvolutionaryTrace; P69596; -.
DR Proteomes; UP000006717; 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:0042802; F:identical protein binding; IPI:IntAct.
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_04097; GAMMA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR042547; NCAP_gCoV.
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; Disulfide bond; Host Golgi apparatus;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Transcription; Transcription regulation; Viral nucleoprotein; Virion.
FT CHAIN 1..409
FT /note="Nucleoprotein"
FT /id="PRO_0000105976"
FT DOMAIN 31..156
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 215..331
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..160
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT REGION 121..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..333
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097"
FT REGION 327..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 190
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097,
FT ECO:0000269|PubMed:15613344"
FT MOD_RES 192
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097,
FT ECO:0000269|PubMed:15613344"
FT MOD_RES 378
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097,
FT ECO:0000269|PubMed:15613344"
FT MOD_RES 379
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097,
FT ECO:0000269|PubMed:15613344"
FT DISULFID 281..308
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097,
FT ECO:0000269|PubMed:15613344"
FT DISULFID 320..323
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04097,
FT ECO:0000269|PubMed:15613344"
FT VARIANT 108
FT /note="D -> Y (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 208
FT /note="Q -> H (in strain: Isolate Vero cell-adapted p65)"
FT VARIANT 391..392
FT /note="YD -> DY (in strain: Isolate Vero cell-adapted p65)"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2BXX"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2BXX"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2BTL"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:2BXX"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:2BXX"
FT STRAND 81..95
FT /evidence="ECO:0007829|PDB:2BXX"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:2BXX"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:2BXX"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2BXX"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2CA1"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 256..261
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 266..272
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:2CA1"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:2CA1"
FT STRAND 295..306
FT /evidence="ECO:0007829|PDB:2CA1"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:2CA1"
SQ SEQUENCE 409 AA; 45032 MW; 562F39C475DB8872 CRC64;
MASGKAAGKT DAPAPVIKLG GPKPPKVGSS GNASWFQAIK AKKLNTPPPK FEGSGVPDNE
NIKPSQQHGY WRRQARFKPG KGGRKPVPDA WYFYYTGTGP AADLNWGDTQ DGIVWVAAKG
ADTKSRSNQG TRDPDKFDQY PLRFSDGGPD GNFRWDFIPL NRGRSGRSTA ASSAAASRAP
SREGSRGRRS DSGDDLIARA AKIIQDQQKK GSRITKAKAD EMAHRRYCKR TIPPNYRVDQ
VFGPRTKGKE GNFGDDKMNE EGIKDGRVTA MLNLVPSSHA CLFGSRVTPK LQLDGLHLRF
EFTTVVPCDD PQFDNYVKIC DQCVDGVGTR PKDDEPKPKS RSSSRPATRG NSPAPRQQRP
KKEKKLKKQD DEADKALTSD EERNNAQLEF YDEPKVINWG DAALGENEL
