NCAP_CVH22
ID NCAP_CVH22 Reviewed; 389 AA.
AC P15130; Q66175;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-APR-2003, sequence version 2.
DT 25-MAY-2022, entry version 106.
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=7;
OS Human coronavirus 229E (HCoV-229E).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Duvinacovirus.
OX NCBI_TaxID=11137;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2922924; DOI=10.1016/0042-6822(89)90050-0;
RA Schreiber S.S., Kamahora T., Lai M.M.C.;
RT "Sequence analysis of the nucleocapsid protein gene of human coronavirus
RT 229E.";
RL Virology 169:142-151(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2167350; DOI=10.1002/jmv.1890310216;
RA Myints S., Harmsen D., Raabe T., Siddell S.G.;
RT "Characterization of a nucleic acid probe for the diagnosis of human
RT coronavirus 229E infections.";
RL J. Med. Virol. 31:165-172(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11369870; DOI=10.1099/0022-1317-82-6-1273;
RA Thiel V., Herold J., Schelle B., Siddell S.G.;
RT "Infectious RNA transcribed in vitro from a cDNA copy of the human
RT coronavirus genome cloned in vaccinia virus.";
RL J. Gen. Virol. 82:1273-1281(2001).
RN [4]
RP FUNCTION.
RX PubMed=15890900; DOI=10.1128/jvi.79.11.6620-6630.2005;
RA Schelle B., Karl N., Ludewig B., Siddell S.G., Thiel V.;
RT "Selective replication of coronavirus genomes that express nucleocapsid
RT protein.";
RL J. Virol. 79:6620-6630(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_04095, ECO:0000269|PubMed:15890900}.
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}.
CC -!- INTERACTION:
CC P15130; P15130: N; NbExp=19; IntAct=EBI-8172439, EBI-8172439;
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; J04419; AAA45463.1; -; Genomic_RNA.
DR EMBL; X51325; CAA35708.1; -; mRNA.
DR EMBL; AF304460; AAG48597.1; -; Genomic_RNA.
DR PIR; A30119; VHIH2E.
DR PIR; S08031; S08031.
DR RefSeq; NP_073556.1; NC_002645.1.
DR PDB; 7LGT; X-ray; 1.97 A; E/F=75-83.
DR PDBsum; 7LGT; -.
DR SMR; P15130; -.
DR IntAct; P15130; 228.
DR MINT; P15130; -.
DR PRIDE; P15130; -.
DR DNASU; 918763; -.
DR GeneID; 918763; -.
DR KEGG; vg:918763; -.
DR Proteomes; UP000006716; 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-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Reference proteome; Ribonucleoprotein; RNA-binding; Transcription;
KW Transcription regulation; Viral nucleoprotein; Virion.
FT CHAIN 1..389
FT /note="Nucleoprotein"
FT /id="PRO_0000106000"
FT DOMAIN 20..141
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 236..352
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 22..148
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 111..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..347
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 363..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT CONFLICT 35
FT /note="P -> S (in Ref. 1; AAA45463)"
FT CONFLICT 115
FT /note="Y -> H (in Ref. 1)"
FT CONFLICT 117
FT /note="V -> A (in Ref. 1)"
FT CONFLICT 160
FT /note="R -> P (in Ref. 1; AAA45463)"
FT CONFLICT 175
FT /note="N -> Y (in Ref. 1; AAA45463)"
FT CONFLICT 244..245
FT /note="MQ -> IE (in Ref. 1; AAA45463)"
FT CONFLICT 351
FT /note="H -> Q (in Ref. 1; AAA45463)"
FT CONFLICT 378
FT /note="V -> F (in Ref. 1; AAA45463)"
SQ SEQUENCE 389 AA; 43467 MW; D3D86CFE10EEDCA1 CRC64;
MATVKWADAS EPQRGRQGRI PYSLYSPLLV DSEQPWKVIP RNLVPINKKD KNKLIGYWNV
QKRFRTRKGK RVDLSPKLHF YYLGTGPHKD AKFRERVEGV VWVAVDGAKT EPTGYGVRRK
NSEPEIPHFN QKLPNGVTVV EEPDSRAPSR SQSRSQSRGR GESKPQSRNP SSDRNHNSQD
DIMKAVAAAL KSLGFDKPQE KDKKSAKTGT PKPSRNQSPA SSQTSAKSLA RSQSSETKEQ
KHEMQKPRWK RQPNDDVTSN VTQCFGPRDL DHNFGSAGVV ANGVKAKGYP QFAELVPSTA
AMLFDSHIVS KESGNTVVLT FTTRVTVPKD HPHLGKFLEE LNAFTREMQQ HPLLNPSALE
FNPSQTSPAT AEPVRDEVSI ETDIIDEVN
