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NCAP_CVHN2
ID   NCAP_CVHN2              Reviewed;         441 AA.
AC   Q14EA6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   02-JUN-2021, entry version 55.
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 N2) (HCoV-HKU1).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Betacoronavirus; Embecovirus.
OX   NCBI_TaxID=443240;
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; AY884001; AAX76525.1; -; Genomic_RNA.
DR   SMR; Q14EA6; -.
DR   PRIDE; Q14EA6; -.
DR   Proteomes; UP000006551; 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_0000297768"
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
 
 
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