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NCAP_CVPPU
ID   NCAP_CVPPU              Reviewed;         382 AA.
AC   P04134; Q9IW03;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   25-MAY-2022, entry version 99.
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 Purdue) (TGEV).
OC   Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC   Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC   Alphacoronavirus; Tegacovirus.
OX   NCBI_TaxID=11151;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=2825819; DOI=10.1016/0300-9084(87)90178-7;
RA   Rasschaert D., Gelfi J., Laude H.;
RT   "Enteric coronavirus TGEV: partial sequence of the genomic RNA, its
RT   organization and expression.";
RL   Biochimie 69:591-600(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=3008432; DOI=10.1016/0042-6822(86)90102-9;
RA   Kapke P.A., Brian D.A.;
RT   "Sequence analysis of the porcine transmissible gastroenteritis coronavirus
RT   nucleocapsid protein gene.";
RL   Virology 151:41-49(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate PUR46-MAD;
RX   PubMed=10805807; DOI=10.1073/pnas.97.10.5516;
RA   Almazan F., Gonzalez J.M., Penzes Z., Izeta A., Calvo E., Plana-Duran J.,
RA   Enjuanes L.;
RT   "Engineering the largest RNA virus genome as an infectious bacterial
RT   artificial chromosome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5516-5521(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-21.
RX   PubMed=2841792; DOI=10.1016/0042-6822(88)90581-8;
RA   Kapke P.A., Tung F.Y.T., Hogue B.G., Brian D.A., Woods R.D., Wesley R.;
RT   "The amino-terminal signal peptide on the porcine transmissible
RT   gastroenteritis coronavirus matrix protein is not an absolute requirement
RT   for membrane translocation and glycosylation.";
RL   Virology 165:367-376(1988).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1645905; DOI=10.1016/0168-1702(91)90019-r;
RA   Pulford D.J., Britton P.;
RT   "Expression and cellular localisation of porcine transmissible
RT   gastroenteritis virus N and M proteins by recombinant vaccinia viruses.";
RL   Virus Res. 18:203-217(1991).
RN   [6]
RP   FUNCTION.
RX   PubMed=15507657; DOI=10.1128/jvi.78.22.12683-12688.2004;
RA   Almazan F., Galan C., Enjuanes L.;
RT   "The nucleoprotein is required for efficient coronavirus genome
RT   replication.";
RL   J. Virol. 78:12683-12688(2004).
RN   [7]
RP   PHOSPHORYLATION AT SER-9; SER-156; SER-254 AND SER-256, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=Isolate PUR-C11;
RX   PubMed=16033973; DOI=10.1099/vir.0.80975-0;
RA   Calvo E., Escors D., Lopez J.A., Gonzalez J.M., Alvarez A., Arza E.,
RA   Enjuanes L.;
RT   "Phosphorylation and subcellular localization of transmissible
RT   gastroenteritis virus nucleocapsid protein in infected cells.";
RL   J. Gen. Virol. 86:2255-2267(2005).
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:0000250|UniProtKB:P03416, ECO:0000255|HAMAP-Rule:MF_04095,
CC       ECO:0000269|PubMed:15507657}.
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:0000250|UniProtKB:P03416, ECO:0000255|HAMAP-Rule:MF_04095}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03416,
CC       ECO:0000255|HAMAP-Rule:MF_04095}. Host endoplasmic reticulum-Golgi
CC       intermediate compartment {ECO:0000250|UniProtKB:P03416,
CC       ECO:0000255|HAMAP-Rule:MF_04095}. Host Golgi apparatus
CC       {ECO:0000250|UniProtKB:P03416, ECO:0000255|HAMAP-Rule:MF_04095}.
CC       Note=Located inside the virion, complexed with the viral RNA. Probably
CC       associates with ER-derived membranes where it participates in viral RNA
CC       synthesis and virus budding. {ECO:0000250|UniProtKB:P03416,
CC       ECO:0000255|HAMAP-Rule:MF_04095}.
CC   -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC       during infection. {ECO:0000250|UniProtKB:P03416, ECO:0000255|HAMAP-
CC       Rule:MF_04095}.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       {ECO:0000250|UniProtKB:P03416, ECO:0000255|HAMAP-Rule:MF_04095,
CC       ECO:0000269|PubMed:16033973}.
CC   -!- SIMILARITY: Belongs to the alphacoronavirus nucleocapsid protein
CC       family. {ECO:0000255|HAMAP-Rule:MF_04095}.
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DR   EMBL; X06371; CAA29674.1; -; Genomic_RNA.
DR   EMBL; M14878; AAA47915.1; -; Genomic_RNA.
DR   EMBL; AJ271965; CAB91150.1; -; Genomic_RNA.
DR   EMBL; M21627; AAA47913.1; -; Genomic_RNA.
DR   PIR; A04025; VHIHPC.
DR   SMR; P04134; -.
DR   IntAct; P04134; 1.
DR   iPTMnet; P04134; -.
DR   Proteomes; UP000001440; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   ADP-ribosylation; Host Golgi apparatus; Phosphoprotein; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..382
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000106014"
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          328..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                   ECO:0000269|PubMed:16033973"
FT   MOD_RES         156
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095,
FT                   ECO:0000269|PubMed:16033973"
FT   MOD_RES         254
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095,
FT                   ECO:0000269|PubMed:16033973"
FT   MOD_RES         256
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04095,
FT                   ECO:0000269|PubMed:16033973"
FT   CONFLICT        237
FT                   /note="W -> S (in Ref. 2; AAA47915)"
FT   CONFLICT        376
FT                   /note="I -> N (in Ref. 1; CAA29674)"
SQ   SEQUENCE   382 AA;  43521 MW;  E299502A0FB36ABA CRC64;
     MANQGQRVSW GDESTKTRGR SNSRGRKNNN IPLSFFNPIT LQQGSKFWNL CPRDFVPKGI
     GNRDQQIGYW NRQTRYRMVK GQRKELPERW FFYYLGTGPH ADAKFKDKLD GVVWVAKDGA
     MNKPTTLGSR GANNESKALK FDGKVPGEFQ LEVNQSRDNS RSRSQSRSRS RNRSQSRGRQ
     QFNNKKDDSV EQAVLAALKK LGVDTEKQQQ RSRSKSKERS NSKTRDTTPK NENKHTWKRT
     AGKGDVTRFY GARSSSANFG DTDLVANGSS AKHYPQLAEC VPSVSSILFG SYWTSKEDGD
     QIEVTFTHKY HLPKDDPKTG QFLQQINAYA RPSEVAKEQR KRKSRSKSAE RSEQDVVPDA
     LIENYTDVFD DTQVEIIDEV TN
 
 
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