NCAP_CVPFS
ID NCAP_CVPFS Reviewed; 382 AA.
AC P05991;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1988, sequence version 1.
DT 02-JUN-2021, entry version 84.
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 Porcine transmissible gastroenteritis coronavirus (strain FS772/70) (TGEV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=11150;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2835592; DOI=10.1111/j.1365-2958.1988.tb00010.x;
RA Britton P., Carmenes R.S., Page K.W., Garwes D.J., Parra F.;
RT "Sequence of the nucleoprotein gene from a virulent British field isolate
RT of transmissible gastroenteritis virus and its expression in Saccharomyces
RT cerevisiae.";
RL Mol. Microbiol. 2:89-99(1988).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=11533198; DOI=10.1128/jvi.75.19.9345-9356.2001;
RA Wurm T., Chen H., Hodgson T., Britton P., Brooks G., Hiscox J.A.;
RT "Localization to the nucleolus is a common feature of coronavirus
RT nucleoproteins, and the protein may disrupt host cell division.";
RL J. Virol. 75:9345-9356(2001).
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 -!- INTERACTION:
CC P05991; P02543: VIM; Xeno; NbExp=4; IntAct=EBI-25636086, EBI-25636029;
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}. Host nucleus, host nucleolus
CC {ECO:0000269|PubMed:11533198}. 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; Y00542; CAA68607.1; -; Genomic_RNA.
DR PIR; S03762; S03762.
DR SMR; P05991; -.
DR IntAct; P05991; 3.
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:0044196; C:host cell nucleolus; 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 1: Evidence at protein level;
KW ADP-ribosylation; Host Golgi apparatus; Host nucleus; Phosphoprotein;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..382
FT /note="Nucleoprotein"
FT /id="PRO_0000106012"
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..29
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..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 329..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..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; 43483 MW; 25152E1D8F327F9E CRC64;
MANQGQRVSW GDESTKIRGR SNSRGRKSNN IPLSFFNPIT LQQGSKFWNL CPRDFVPKGI
GNRDQQIGYW NRQTRYRMVK GQRKELPERW FFYYLGTGPH ADAKFKDKLD GVVWVAKDGA
MNKPTTLGSR GANNESKALK FDGKVPGEFQ LEVNQSRDNS RSRSQSRSRS RNRSQSRGRQ
QSNNKKDDSV EQAVLAALKK LGVDTEKQQQ RSCSKSKERS NSKTRDTTPK NENKHTWKRT
AGKGDVTRFY GARSSSANFG DSDLVANGSS AKHYPQLAEC VPSVSSILFG SYWTSKEDGD
QIEVTFTHKY HLPKDDPKTE QFLQQINAYA RPSEVAKEQR KRKSRSKSAE RSEQEVVPDA
LIENYTDVFD DTQVEMIDEV TN
