NCAP_CVHOC
ID NCAP_CVHOC Reviewed; 448 AA.
AC P33469; Q6TNF5;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 98.
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 Human coronavirus OC43 (HCoV-OC43).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=31631;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2541577; DOI=10.1016/0168-1702(89)90048-8;
RA Kamahora T., Soe L.H., Lai M.M.C.;
RT "Sequence analysis of nucleocapsid gene and leader RNA of human coronavirus
RT OC43.";
RL Virus Res. 12:1-9(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759, and Isolate clinical OC43-Paris;
RX PubMed=15280490; DOI=10.1128/jvi.78.16.8824-8834.2004;
RA St Jean J.R., Jacomy H., Desforges M., Vabret A., Freymuth F., Talbot P.J.;
RT "Human respiratory coronavirus OC43: genetic stability and neuroinvasion.";
RL J. Virol. 78:8824-8834(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ATCC VR-759;
RX PubMed=15650185; DOI=10.1128/jvi.79.3.1595-1604.2005;
RA Vijgen L., Keyaerts E., Moes E., Thoelen I., Wollants E., Lemey P.,
RA Vandamme A.M., Van Ranst M.;
RT "Complete genomic sequence of human coronavirus OC43: molecular clock
RT analysis suggests a relatively recent zoonotic coronavirus transmission
RT event.";
RL J. Virol. 79:1595-1604(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_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; AY585228; AAT84358.1; -; Genomic_RNA.
DR EMBL; AY391777; AAR01019.1; -; Genomic_RNA.
DR PIR; A60003; A60003.
DR PDB; 4J3K; X-ray; 2.00 A; A=58-191.
DR PDB; 4KXJ; X-ray; 2.65 A; A=58-191.
DR PDB; 4LI4; X-ray; 1.71 A; A=58-191.
DR PDB; 4LM7; X-ray; 1.72 A; A=58-191.
DR PDB; 4LM9; X-ray; 1.60 A; A=58-190.
DR PDB; 4LMC; X-ray; 1.74 A; A=58-190.
DR PDB; 4LMT; X-ray; 1.71 A; A=58-191.
DR PDBsum; 4J3K; -.
DR PDBsum; 4KXJ; -.
DR PDBsum; 4LI4; -.
DR PDBsum; 4LM7; -.
DR PDBsum; 4LM9; -.
DR PDBsum; 4LMC; -.
DR PDBsum; 4LMT; -.
DR SMR; P33469; -.
DR IntAct; P33469; 231.
DR ChEMBL; CHEMBL3232681; -.
DR Proteomes; UP000007552; Genome.
DR Proteomes; UP000180344; 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 Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..448
FT /note="Nucleoprotein"
FT /id="PRO_0000106001"
FT DOMAIN 61..190
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 259..384
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..194
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 158..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..384
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 266..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 174
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 191
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 390
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 423
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 427
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT VARIANT 33
FT /note="V -> F (in strain: Isolate ATCC VR-759 and Isolate
FT clinical OC43-Paris)"
FT VARIANT 86
FT /note="P -> V (in strain: Isolate ATCC VR-759 and Isolate
FT clinical OC43-Paris)"
FT VARIANT 107
FT /note="G -> R (in strain: Isolate ATCC VR-759 and Isolate
FT clinical OC43-Paris)"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4LM9"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4LM9"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4LM9"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4LM9"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:4LM9"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:4LM9"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:4LM7"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:4LM9"
SQ SEQUENCE 448 AA; 49316 MW; 5193AB1AE0D75626 CRC64;
MSFTPGKQSS SRASSGNRSG NGILKWADQS DQVRNVQTRG RRAQPKQTAT SQQPSGGNVV
PYYSWFSGIT QFQKGKEFEF VEGQGPPIAP GVPATEAKGY WYRHNRGSFK TADGNQRQLL
PRWYFYYLGT GPHAKDQYGT DIDGVYWVAS NQADVNTPAD IVDRDPSSDE AIPTRFPPGT
VLPQGYYIEG SGRSAPNSRS TSRTSSRASS AGSRSRANSG NRTPTSGVTP DMADQIASLV
LAKLGKDATK PQQVTKHTAK EVRQKILNKP RQKRSPNKQC TVQQCFGKRG PNQNFGGGEM
LKLGTSDPQF PILAELAPTA GAFFFGSRLE LAKVQNLSGN PDEPQKDVYE LRYNGAIRFD
STLSGFETIM KVLNENLNAY QQQDGMMNMS PKPQRQRGHK NGQGENDNIS VAVPKSRVQQ
NKSRELTAED ISLLKKMDEP YTEDTSEI
