NCAP_CVHN5
ID NCAP_CVHN5 Reviewed; 441 AA.
AC Q0ZME3;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 68.
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 HKU1 (isolate N5) (HCoV-HKU1).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Embecovirus.
OX NCBI_TaxID=443241;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16809319; DOI=10.1128/jvi.00509-06;
RA Woo P.C.Y., Lau S.K.P., Yip C.C.Y., Huang Y., Tsoi H.-W., Chan K.-H.,
RA Yuen K.-Y.;
RT "Comparative analysis of 22 coronavirus HKU1 genomes reveals a novel
RT genotype and evidence of natural recombination in coronavirus HKU1.";
RL J. Virol. 80:7136-7145(2006).
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; DQ339101; ABC70723.1; -; Genomic_RNA.
DR SMR; Q0ZME3; -.
DR IntAct; Q0ZME3; 226.
DR Proteomes; UP000001985; 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 3: Inferred from homology;
KW ADP-ribosylation; Host Golgi apparatus; Phosphoprotein; Ribonucleoprotein;
KW RNA-binding; Transcription; Transcription regulation; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..441
FT /note="Nucleoprotein"
FT /id="PRO_0000297769"
FT DOMAIN 60..189
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 257..379
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..193
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 186..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..382
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 380..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 158
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 173
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 190
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 388
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 417
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT MOD_RES 421
FT /note="Phosphothreonine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
SQ SEQUENCE 441 AA; 49146 MW; 14AC881F4035536F CRC64;
MSYTPGHHAG SRSSSGNRSG ILKKTSWVDQ SERSHQTYNR GRKPQPKFTV STQPQGNPIP
HYSWFSGITQ FQKGRDFKFP DGQGVPIAYG IPPSEAKGYW YKHNRRSFKT ADGQQKQLLP
RWYFYYLGTG PYASSSYGDA HEGIFWVASH QADTSIPSDV SARDPTIQEA IPTRFSPGTI
LPQGYYVEGS GRSASNSRPG SRSQSRGPNN RSLSRSNSNF RHSDSIVKPD MADEIASLVL
AKLGKDSKPQ QVTKQNAKEI RHKILMKPRQ KRTPNKFCNV QQCFGKRGPL QNFGNSEMLK
LGTNDPQFPI LAELAPTPGA FFFGSKLELF KRDSDADSPS KDTFELRYSG SIRFDSTLPG
FETIMKVLKE NLDAYVNSNQ NTVSGSLSPK PQRKRGVKQS PESFDSLNLS ADTQHISNDF
TPEDHSLLAT LDDPYVEDSV A
