NCAP_FIPV
ID NCAP_FIPV Reviewed; 377 AA.
AC P25909; Q4U5F7; Q52PA7;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 02-JUN-2021, entry version 85.
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 Feline coronavirus (strain FIPV WSU-79/1146) (FCoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Alphacoronavirus; Tegacovirus.
OX NCBI_TaxID=33734;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1847259; DOI=10.1016/0042-6822(91)90499-2;
RA Vennema H., de Groot R.J., Harbour D.A., Horzinek M.C., Spaan W.J.M.;
RT "Primary structure of the membrane and nucleocapsid protein genes of feline
RT infectious peritonitis virus and immunogenicity of recombinant vaccinia
RT viruses in kittens.";
RL Virology 181:327-335(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=16033972; DOI=10.1099/vir.0.80985-0;
RA Dye C., Siddell S.G.;
RT "Genomic RNA sequence of Feline coronavirus strain FIPV WSU-79/1146.";
RL J. Gen. Virol. 86:2249-2253(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Haijema B.J., de Groot-Mijnes J.D.F., Vennema H., Raamsman M.J.,
RA Rottier P.J.M., de Groot R.J.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; X56496; CAA39851.1; -; Genomic_RNA.
DR EMBL; DQ010921; AAY32599.1; -; Genomic_RNA.
DR EMBL; AY994055; AAY16380.1; -; Genomic_RNA.
DR PIR; B38498; VHIH79.
DR RefSeq; YP_004070199.1; NC_002306.3.
DR SMR; P25909; -.
DR GeneID; 10040186; -.
DR KEGG; vg:10040186; -.
DR Proteomes; UP000000835; Genome.
DR Proteomes; UP000140386; 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: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; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..377
FT /note="Nucleoprotein"
FT /id="PRO_0000106023"
FT DOMAIN 31..153
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 220..333
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 121..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..330
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT REGION 327..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 250
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT MOD_RES 252
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT VARIANT 18
FT /note="R -> L"
SQ SEQUENCE 377 AA; 42745 MW; D76382AE6D88D59B CRC64;
MATQGQRVNW GDEPSKRRGR SNSRGRKNND IPLSFYNPIT LEQGSKFWNL CPRDLVPKGI
GNKDQQIGYW NRQIRYRIVK GQRKELAERW FFYFLGTGPH ADAKFKDKID GVFWVARDGA
MNKPTTLGTR GTNNESKPLR FDGKIPPQFQ LEVNRSRNNS RSGSQSRSVS RNRSQSRGRH
HSNNQNNNVE DTIVAVLEKL GVTDKQRSRS KPRERSDSKP RDTTPKNANK HTWKKTAGKG
DVTTFYGARS SSANFGDSDL VANGNAAKCY PQIAECVPSV SSIIFGSQWS AEEAGDQVKV
TLTHTYYLPK DDAKTSQFLE QIDAYKRPSE VAKDQRQRRS RSKSADKKPE ELSVTLVEAY
TDVFDDTQVE MIDEVTN
