NCAP_CVHNL
ID NCAP_CVHNL Reviewed; 377 AA.
AC Q6Q1R8;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04095};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04095};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04095};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04095};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04095}; ORFNames=6;
OS Human coronavirus NL63 (HCoV-NL63).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Setracovirus.
OX NCBI_TaxID=277944;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Amsterdam I;
RX PubMed=15034574; DOI=10.1038/nm1024;
RA Van Der Hoek L., Pyrc K., Jebbink M.F., Vermeulen-Oost W., Berkhout R.J.,
RA Wolthers K.C., Wertheim-Van Dillen P.M., Kaandorp J., Spaargaren J.,
RA Berkhout B.;
RT "Identification of a new human coronavirus.";
RL Nat. Med. 10:368-373(2004).
RN [2]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25700263; DOI=10.1371/journal.pone.0117833;
RA Zuwala K., Golda A., Kabala W., Burmistrz M., Zdzalik M., Nowak P.,
RA Kedracka-Krok S., Zarebski M., Dobrucki J., Florek D., Zeglen S.,
RA Wojarski J., Potempa J., Dubin G., Pyrc K.;
RT "The nucleocapsid protein of human coronavirus NL63.";
RL PLoS ONE 10:E0117833-E0117833(2015).
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_04095}.
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_04095, ECO:0000269|PubMed:25700263}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04095}. Host
CC endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|HAMAP-Rule:MF_04095}. Host Golgi apparatus
CC {ECO:0000255|HAMAP-Rule:MF_04095}. 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_04095}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04095}.
CC -!- PTM: Phosphorylated on serine and threonine residues.
CC {ECO:0000255|HAMAP-Rule:MF_04095}.
CC -!- SIMILARITY: Belongs to the alphacoronavirus nucleocapsid protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04095}.
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DR EMBL; AY567487; AAS58181.1; -; Genomic_RNA.
DR RefSeq; YP_003771.1; NC_005831.2.
DR PDB; 5EPW; X-ray; 1.50 A; A/B=221-340.
DR PDB; 5N4K; X-ray; 1.49 A; A/B=2-140.
DR PDBsum; 5EPW; -.
DR PDBsum; 5N4K; -.
DR SMR; Q6Q1R8; -.
DR IntAct; Q6Q1R8; 226.
DR PRIDE; Q6Q1R8; -.
DR DNASU; 2943504; -.
DR GeneID; 2943504; -.
DR KEGG; vg:2943504; -.
DR Proteomes; UP000008573; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
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-KW.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
DR HAMAP; MF_04095; ALPHA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR042548; NCAP_aCoV.
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..377
FT /note="Nucleoprotein"
FT /id="PRO_0000283928"
FT DOMAIN 17..139
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 223..337
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 19..151
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 140..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..334
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT COMPBIAS 196..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:5N4K"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:5N4K"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:5N4K"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5N4K"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5N4K"
FT STRAND 53..63
FT /evidence="ECO:0007829|PDB:5N4K"
FT STRAND 70..80
FT /evidence="ECO:0007829|PDB:5N4K"
FT TURN 85..88
FT /evidence="ECO:0007829|PDB:5N4K"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5N4K"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5N4K"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5EPW"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 246..249
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 262..267
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 274..278
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 284..290
FT /evidence="ECO:0007829|PDB:5EPW"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:5EPW"
FT STRAND 301..313
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 319..325
FT /evidence="ECO:0007829|PDB:5EPW"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5EPW"
SQ SEQUENCE 377 AA; 42252 MW; 704C71C0EF9CDB42 CRC64;
MASVNWADDR AARKKFPPPS FYMPLLVSSD KAPYRVIPRN LVPIGKGNKD EQIGYWNVQE
RWRMRRGQRV DLPPKVHFYY LGTGPHKDLK FRQRSDGVVW VAKEGAKTVN TSLGNRKRNQ
KPLEPKFSIA LPPELSVVEF EDRSNNSSRA SSRSSTRNNS RDSSRSTSRQ QSRTRSDSNQ
SSSDLVAAVT LALKNLGFDN QSKSPSSSGT STPKKPNKPL SQPRADKPSQ LKKPRWKRVP
TREENVIQCF GPRDFNHNMG DSDLVQNGVD AKGFPQLAEL IPNQAALFFD SEVSTDEVGD
NVQITYTYKM LVAKDNKNLP KFIEQISAFT KPSSIKEMQS QSSHVAQNTV LNASIPESKP
LADDDSAIIE IVNEVLH
