NCAP_CVPR8
ID NCAP_CVPR8 Reviewed; 382 AA.
AC P33463;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 02-JUN-2021, entry version 82.
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};
OS Porcine respiratory coronavirus (strain 86/137004 / isolate British)
OS (PRCoV) (PRCV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33736;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1662846; DOI=10.1016/0168-1702(91)90032-q;
RA Britton P., Mawditt K.L., Page K.W.;
RT "The cloning and sequencing of the virion protein genes from a British
RT isolate of porcine respiratory coronavirus: comparison with transmissible
RT gastroenteritis virus genes.";
RL Virus Res. 21:181-198(1991).
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}.
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; X60056; CAA42657.1; -; Genomic_RNA.
DR PIR; S24282; S24282.
DR SMR; P33463; -.
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: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 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..382
FT /note="Nucleoprotein"
FT /id="PRO_0000106015"
FT DOMAIN 31..153
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 224..337
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..159
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 150..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..334
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 334..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 156
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 254
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 256
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
SQ SEQUENCE 382 AA; 43553 MW; 50350CED886FFCD4 CRC64;
MANQGQRVSW GDESTKIRGR SNSRGRKINN IPLSFFNPIT LQQGAKFWNS CPRDFVPKGI
GNRDQQIGYW NRQTRYRMVK GQRKELPERW FFYYLGTGPH ADAKFKDKLD GVVWVAKDGA
MNKPTTLGSR GANNESKALK FDGKVPGEFQ LEVNQSRDNS RSRSQSRSRS RNRSQSRGRQ
QSNNKKDDSV EQAVLAALKK LGVYTEKQQQ RSRSKSKERS NSKTRDTTPK NENKHTWKRT
AGKGDVTRFY GARSSSANFG DSDLVANGSS AKHYPQLAEC VPSVSSILFG SYWTSKEDGD
QIEVTFTHKY HLPKDHPKTE QFLQQINAYA CPSEVAKEQR KRKSRSKSAE RSEQEVVPDS
LIENYTDVFD DTQVEMIDEV TN
