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NCAP_PEDV7
ID   NCAP_PEDV7              Reviewed;         441 AA.
AC   Q07499;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   02-JUN-2021, entry version 104.
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 epidemic diarrhea virus (strain CV777) (PEDV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Pedacovirus.
OX   NCBI_TaxID=229032;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8397280; DOI=10.1099/0022-1317-74-9-1795;
RA   Bridgen A., Duarte M., Tobler K., Laude H., Ackermann M.;
RT   "Sequence determination of the nucleocapsid protein gene of the porcine
RT   epidemic diarrhea virus confirms that this virus is a coronavirus related
RT   to human coronavirus 229E and porcine transmissible gastroenteritis
RT   virus.";
RL   J. Gen. Virol. 74:1795-1804(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=8291230; DOI=10.1006/viro.1994.1058;
RA   Duarte M., Tobler K., Bridgen A., Rasschaert D., Ackermann M., Laude H.;
RT   "Sequence analysis of the porcine epidemic diarrhea virus genome between
RT   the nucleocapsid and spike protein genes reveals a polymorphic ORF.";
RL   Virology 198:466-476(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=9782358; DOI=10.1007/978-1-4615-5331-1_101;
RA   Bridgen A., Kocherhans R., Tobler K., Carvajal A., Ackermann M.;
RT   "Further analysis of the genome of porcine epidemic diarrhea virus.";
RL   Adv. Exp. Med. Biol. 440:781-786(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11724265; DOI=10.1023/a:1011831902219;
RA   Kocherhans R., Bridgen A., Ackermann M., Tobler K.;
RT   "Completion of the porcine epidemic diarrhoea coronavirus (PEDV) genome
RT   sequence.";
RL   Virus Genes 23:137-144(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA   Chen J.F., Feng L., Shi H.Y., Sun D.B., Tong Y.E.;
RT   "Molecular characteristics of nucleocapsid protein gene of porcine epidemic
RT   diarrhea virus strain CV777.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH HOST RSAD2, AND SUBCELLULAR LOCATION.
RX   PubMed=32719955; DOI=10.1007/s00705-020-04747-8;
RA   Wu J., Chi H., Fu Y., Cao A., Shi J., Zhu M., Zhang L., Hua D., Huang J.;
RT   "The antiviral protein viperin interacts with the viral N protein to
RT   inhibit proliferation of porcine epidemic diarrhea virus.";
RL   Arch. Virol. 165:2279-2289(2020).
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 (By
CC       similarity). Interacts with host RSAD2; this interaction inhibits viral
CC       replication (PubMed:32719955). {ECO:0000255|HAMAP-Rule:MF_04095,
CC       ECO:0000269|PubMed:32719955}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04095}. Host
CC       endoplasmic reticulum-Golgi intermediate compartment
CC       {ECO:0000255|HAMAP-Rule:MF_04095, ECO:0000269|PubMed:32719955}. Host
CC       Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04095}. Note=Located inside
CC       the virion, complexed with the viral RNA. Probably associates with ER-
CC       derived membranes where it participates in viral RNA synthesis and
CC       virus 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; Z14976; CAA78697.1; -; Genomic_RNA.
DR   EMBL; AF353511; AAK38660.1; -; Genomic_RNA.
DR   EMBL; DQ355221; ABC84372.1; -; Genomic_RNA.
DR   PIR; JQ2191; JQ2191.
DR   RefSeq; NP_598314.1; NC_003436.1.
DR   SMR; Q07499; -.
DR   GeneID; 935179; -.
DR   KEGG; vg:935179; -.
DR   Proteomes; UP000008159; 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; 2.
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; Phosphoprotein; Ribonucleoprotein;
KW   RNA-binding; Transcription; Transcription regulation; Viral nucleoprotein;
KW   Virion.
FT   CHAIN           1..441
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000283929"
FT   DOMAIN          14..136
FT                   /note="CoV N NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT   DOMAIN          266..382
FT                   /note="CoV N CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT   REGION          16..146
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT   REGION          131..219
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..379
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT   COMPBIAS        140..216
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..278
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
FT   MOD_RES         143
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095"
SQ   SEQUENCE   441 AA;  48967 MW;  5D0692DDE78D2469 CRC64;
     MASVSFQDRG RKRVPLSLYA PLRVTNDKPL SKVLANNAVP TNKGNKDQQI GYWNEQIRWR
     MRRGERIEQP SNWHFYYLGT GPHGDLRYRT RTEGVFWVAK EGAKTEPTNL GVRKASEKPI
     IPKFSQQLPS VVEIVEPNTP PASRANSRSR SRGNGNNRSR SPSNNRGNNQ SRGNSQNRGN
     NQGRGASQNR GGNNNNNNKS RNQSNNRNQS NDRGGVTSRD DLVAAVKDAL KSLGIGENPD
     RHKQQQKPKQ EKSDNSGKNT PKKNKSRATS KERDLKDIPE WRRIPKGENS VAACFGPRGG
     FKNFGDAEFV EKGVDASGYA QIASLAPNVA ALLFGGNVAV RELADSYEIT YNYKMTVPKS
     DPNVELLVSQ VDAFKTGNAK LQRKKEKKNK RETTLQQHEE AIYDDVGAPS DVTHANLEWD
     TAVDGGDTAV EIINEIFDTG N
 
 
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