ID NCAP_SARS Reviewed; 422 AA.
AC P59595; Q7T3Z4; Q7TA14; Q7TF99; Q80E50;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=NC {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04096};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04096}; ORFNames=9a;
OS Severe acute respiratory syndrome coronavirus (SARS-CoV).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=694009;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9675; Paguma larvata (Masked palm civet).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Urbani;
RX PubMed=12730500; DOI=10.1126/science.1085952;
RA Rota P.A., Oberste M.S., Monroe S.S., Nix W.A., Campagnoli R.,
RA Icenogle J.P., Penaranda S., Bankamp B., Maher K., Chen M.-H., Tong S.,
RA Tamin A., Lowe L., Frace M., DeRisi J.L., Chen Q., Wang D., Erdman D.D.,
RA Peret T.C.T., Burns C., Ksiazek T.G., Rollin P.E., Sanchez A., Liffick S.,
RA Holloway B., Limor J., McCaustland K., Olsen-Rasmussen M., Fouchier R.,
RA Guenther S., Osterhaus A.D.M.E., Drosten C., Pallansch M.A., Anderson L.J.,
RA Bellini W.J.;
RT "Characterization of a novel coronavirus associated with severe acute
RT respiratory syndrome.";
RL Science 300:1394-1399(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Tor2;
RX PubMed=12730501; DOI=10.1126/science.1085953;
RA Marra M.A., Jones S.J.M., Astell C.R., Holt R.A., Brooks-Wilson A.,
RA Butterfield Y.S.N., Khattra J., Asano J.K., Barber S.A., Chan S.Y.,
RA Cloutier A., Coughlin S.M., Freeman D., Girn N., Griffith O.L., Leach S.R.,
RA Mayo M., McDonald H., Montgomery S.B., Pandoh P.K., Petrescu A.S.,
RA Robertson A.G., Schein J.E., Siddiqui A., Smailus D.E., Stott J.M.,
RA Yang G.S., Plummer F., Andonov A., Artsob H., Bastien N., Bernard K.,
RA Booth T.F., Bowness D., Czub M., Drebot M., Fernando L., Flick R.,
RA Garbutt M., Gray M., Grolla A., Jones S., Feldmann H., Meyers A.,
RA Kabani A., Li Y., Normand S., Stroher U., Tipples G.A., Tyler S.,
RA Vogrig R., Ward D., Watson B., Brunham R.C., Krajden M., Petric M.,
RA Skowronski D.M., Upton C., Roper R.L.;
RT "The genome sequence of the SARS-associated coronavirus.";
RL Science 300:1399-1404(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate CUHK-Su10, and Isolate CUHK-W1;
RX PubMed=12853594; DOI=10.1056/nejm200307103490216;
RA Tsui S.K.W., Chim S.S.C., Lo Y.M.D.;
RT "Coronavirus genomic-sequence variations and the epidemiology of the severe
RT acute respiratory syndrome.";
RL N. Engl. J. Med. 349:187-188(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate GZ50, and Isolate HKU-36871;
RX PubMed=12958366; DOI=10.1126/science.1087139;
RA Guan Y., Zheng B.J., He Y.Q., Liu X.L., Zhuang Z.X., Cheung C.L., Luo S.W.,
RA Li P.H., Zhang L.J., Guan Y.J., Butt K.M., Wong K.L., Chan K.W., Lim W.,
RA Shortridge K.F., Yuen K.Y., Peiris J.S.M., Poon L.L.M.;
RT "Isolation and characterization of viruses related to the SARS coronavirus
RT from animals in southern China.";
RL Science 302:276-278(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HKU-39849;
RX PubMed=12876307; DOI=10.1177/15353702-0322807-13;
RA Zeng F.Y., Chan C.W., Chan M.N., Chen J.D., Chow K.Y.C., Hon C.C.C.,
RA Hui R.K.H., Li J., Li V.Y.Y., Wang C.Y., Wang P.Y., Guan Y., Zheng B.,
RA Poon L.L.M., Chan K.H., Yuen K.Y., Peiris J.S.M., Leung F.C.;
RT "The complete genome sequence of severe acute respiratory syndrome
RT coronavirus strain HKU-39849 (HK-39).";
RL Exp. Biol. Med. 228:866-873(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Sin2500, Isolate Sin2677, Isolate Sin2679, Isolate Sin2748,
RC and Isolate sin2774;
RX PubMed=12781537; DOI=10.1016/s0140-6736(03)13414-9;
RA Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
RA Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
RA Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.;
RT "Comparative full-length genome sequence analysis of 14 SARS coronavirus
RT isolates and common mutations associated with putative origins of
RT infection.";
RL Lancet 361:1779-1785(2003).
RN [7]
RP ERRATUM OF PUBMED:12781537.
RA Ruan Y., Wei C.L., Ling A.E., Vega V.B., Thoreau H., Se Thoe S.Y.,
RA Chia J.-M., Ng P., Chiu K.P., Lim L., Zhang T., Chan K.P., Oon L.E.L.,
RA Ng M.L., Leo S.Y., Ng L.F.P., Ren E.C., Stanton L.W., Long P.M., Liu E.T.;
RL Lancet 361:1832-1832(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, and
RC Isolate GD01;
RA Qin E., Zhu Q., Yu M., Fan B., Chang G., Si B., Yang B., Peng W., Jiang T.,
RA Liu B., Deng Y., Liu H., Zhang Y., Wang C., Li Y., Gan Y., Li X., Lu F.,
RA Tan G., Yang R., Cao W.S., Wang J., Chen W., Cong L., Deng Y., Dong W.,
RA Han Y., Hu W., Lei M., Li C., Li G., Li G., Li H., Li S., Li S., Li W.,
RA Li W., Lin W., Liu J., Liu Z., Lu H., Ni P., Qi Q., Sun Y., Tang L.,
RA Tong Z., Wang J., Wang X., Wu Q., Xi Y., Xu Z., Yang L., Ye C., Ye J.,
RA Zhang B., Zhang F., Zhang J., Zhang X., Zhou J., Yang H.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TW1;
RA Yeh S.-H., Kao C.-L., Tsai C.-Y., Liu C.-J., Chen D.-S., Chen P.-J.;
RT "The complete genome of SARS coronavirus clone TW1.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate FRA;
RA Eickmann M., Becker S., Klenk H.-D., Doerr H.W., Stadler K., Censini S.,
RA Guidotti S., Masignani V., Scarselli M., Mora M., Donati C., Han J.,
RA Song H.C., Abrignani S., Covacci A., Rappuoli R.;
RT "SARS virus is a close relative of type II coronaviruses.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Frankfurt 1;
RX PubMed=12917450; DOI=10.1099/vir.0.19424-0;
RA Thiel V., Ivanov K.A., Putics A., Hertzig T., Schelle B., Bayer S.,
RA Weissbrich B., Snijder E.J., Rabenau H., Doerr H.W., Gorbalenya A.E.,
RA Ziebuhr J.;
RT "Mechanisms and enzymes involved in SARS coronavirus genome expression.";
RL J. Gen. Virol. 84:2305-2315(2003).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Sun K., Anwar A., Gupta V., Tabiin M.T., Atkinson R., Chandrasekarn A.,
RA August T.J.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate ZJ01;
RX PubMed=14527350;
RA Li L., Wang Z., Lu Y., Bao Q., Chen S., Wu N., Cheng S., Weng J., Zhang Y.,
RA Yan J., Mei L., Wang X., Zhu H., Yu Y., Zhang M., Li M., Yao J., Lu Q.,
RA Yao P., Bo X., Wo J., Wang S., Hu S.;
RT "Severe acute respiratory syndrome-associated coronavirus genotype and its
RT characterization.";
RL Chin. Med. J. 116:1288-1292(2003).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TWC;
RA Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee S.C., Lin Y.-C.,
RA Hsu C.-K., Chen H.-Y., Chang J.G., Chen P.-J., Su I.-J.;
RT "Genomic sequence of SARS isolate from the first fatal case in Taiwan.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Shanghai LY;
RA Yuan Z., Zhang X., Hu Y., Lan S., Wang H., Zhou Z., Wen Y.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Taiwan TC1, Isolate Taiwan TC2, and Isolate Taiwan TC3;
RA Chang J.-G.C., Lin T.-H., Chen C.-M., Lin C.-S., Chan W.-L., Shih M.-C.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TWH, Isolate TWJ, Isolate TWK, Isolate TWS, and Isolate TWY;
RA Shu H.Y., Wu K.M., Tsai S.F.;
RT "The complete genome of SARS coronavirus TWH.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [18]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate HSR 1;
RA Canducci F., Clementi M., Poli G., Vicenzi E.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [19]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate TWC2, and Isolate TWC3;
RA Yang J.-Y., Lin J.-H., Chiu S.-C., Wang S.-F., Lee H.-C., Lin Y.-C.,
RA Hsu C.-K., Chen H.-Y., Chen P.-J., Su I.-J.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate AS;
RA Balotta C., Corvasce S., Violin M., Galli M., Moroni M., Vigevani G.M.,
RA Ruan Y.J., Salemi M.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [21]
RP INTERACTION WITH MEMBRANE PROTEIN M.
RX PubMed=15351485; DOI=10.1016/j.virusres.2004.05.002;
RA He R., Leeson A., Ballantine M., Andonov A., Baker L., Dobie F., Li Y.,
RA Bastien N., Feldmann H., Strocher U., Theriault S., Cutts T., Cao J.,
RA Booth T.F., Plummer F.A., Tyler S., Li X.;
RT "Characterization of protein-protein interactions between the nucleocapsid
RT protein and membrane protein of the SARS coronavirus.";
RL Virus Res. 105:121-125(2004).
RN [22]
RP INTERACTION WITH HOST HNRNPA1.
RX PubMed=15862300; DOI=10.1016/j.febslet.2005.03.080;
RA Luo H., Chen Q., Chen J., Chen K., Shen X., Jiang H.;
RT "The nucleocapsid protein of SARS coronavirus has a high binding affinity
RT to the human cellular heterogeneous nuclear ribonucleoprotein A1.";
RL FEBS Lett. 579:2623-2628(2005).
RN [23]
RP INTERACTION WITH HOST PPIA.
RX PubMed=15688292; DOI=10.1086/427811;
RA Chen Z., Mi L., Xu J., Yu J., Wang X., Jiang J., Xing J., Shang P.,
RA Qian A., Li Y., Shaw P.X., Wang J., Duan S., Ding J., Fan C., Zhang Y.,
RA Yang Y., Yu X., Feng Q., Li B., Yao X., Zhang Z., Li L., Xue X., Zhu P.;
RT "Function of HAb18G/CD147 in invasion of host cells by severe acute
RT respiratory syndrome coronavirus.";
RL J. Infect. Dis. 191:755-760(2005).
RN [24]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=17210170; DOI=10.1016/j.virol.2006.11.027;
RA Stertz S., Reichelt M., Spiegel M., Kuri T., Martinez-Sobrido L.,
RA Garcia-Sastre A., Weber F., Kochs G.;
RT "The intracellular sites of early replication and budding of SARS-
RT coronavirus.";
RL Virology 361:304-315(2007).
RN [25]
RP INTERACTION WITH HOST SMAD3, AND FUNCTION.
RX PubMed=18055455; DOI=10.1074/jbc.m708033200;
RA Zhao X., Nicholls J.M., Chen Y.G.;
RT "Severe acute respiratory syndrome-associated coronavirus nucleocapsid
RT protein interacts with Smad3 and modulates transforming growth factor-beta
RT signaling.";
RL J. Biol. Chem. 283:3272-3280(2008).
RN [26]
RP CLEAVAGE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 257-LYS--LYS-262 AND
RP 400-ASP--ASP-403.
RX PubMed=18155731; DOI=10.1016/j.jmb.2007.11.081;
RA Diemer C., Schneider M., Seebach J., Quaas J., Froesner G., Schaetzl H.M.,
RA Gilch S.;
RT "Cell type-specific cleavage of nucleocapsid protein by effector caspases
RT during SARS coronavirus infection.";
RL J. Mol. Biol. 376:23-34(2008).
RN [27]
RP PHOSPHORYLATION AT SER-177 BY HOST GSK3A AND GSK3B, AND SUBCELLULAR
RP LOCATION.
RX PubMed=19106108; DOI=10.1074/jbc.m805747200;
RA Wu C.H., Yeh S.H., Tsay Y.G., Shieh Y.H., Kao C.L., Chen Y.S., Wang S.H.,
RA Kuo T.J., Chen D.S., Chen P.J.;
RT "Glycogen synthase kinase-3 regulates the phosphorylation of severe acute
RT respiratory syndrome coronavirus nucleocapsid protein and viral
RT replication.";
RL J. Biol. Chem. 284:5229-5239(2009).
RN [28]
RP INTERACTION WITH ENVELOPE SMALL MEMBRANE PROTEIN E.
RX PubMed=24766657; DOI=10.1186/1423-0127-21-34;
RA Tseng Y.T., Wang S.M., Huang K.J., Wang C.T.;
RT "SARS-CoV envelope protein palmitoylation or nucleocapid association is not
RT required for promoting virus-like particle production.";
RL J. Biomed. Sci. 21:34-34(2014).
RN [29]
RP ADP-RIBOSYLATION.
RX PubMed=29199039; DOI=10.1016/j.virol.2017.11.020;
RA Grunewald M.E., Fehr A.R., Athmer J., Perlman S.;
RT "The coronavirus nucleocapsid protein is ADP-ribosylated.";
RL Virology 517:62-68(2018).
RN [30]
RP CLEAVAGE.
RX PubMed=35922005; DOI=10.1038/s41586-022-05148-4;
RA Chu H., Hou Y., Yang D., Wen L., Shuai H., Yoon C., Shi J., Chai Y.,
RA Yuen T.T., Hu B., Li C., Zhao X., Wang Y., Huang X., Lee K.S., Luo C.,
RA Cai J.P., Poon V.K., Chan C.C., Zhang A.J., Yuan S., Sit K.Y., Foo D.C.,
RA Au W.K., Wong K.K., Zhou J., Kok K.H., Jin D.Y., Chan J.F., Yuen K.Y.;
RT "Coronaviruses exploit a host cysteine-aspartic protease for replication.";
RL Nature 0:0-0(2022).
RN [31]
RP REVIEW.
RX PubMed=32974389; DOI=10.3389/fmolb.2020.00219;
RA Nikolakaki E., Giannakouros T.;
RT "SR/RS Motifs as Critical Determinants of Coronavirus Life Cycle.";
RL Front. Mol. Biosci. 7:219-219(2020).
RN [32]
RP STRUCTURE BY NMR OF 45-181.
RX PubMed=15147189; DOI=10.1021/bi036155b;
RA Huang Q., Yu L., Petros A.M., Gunasekera A., Liu Z., Xu N., Hajduk P.,
RA Mack J., Fesik S.W., Olejniczak E.T.;
RT "Structure of the N-terminal RNA-binding domain of the SARS CoV
RT nucleocapsid protein.";
RL Biochemistry 43:6059-6063(2004).
RN [33]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 362-370.
RX PubMed=16041067; DOI=10.1107/s0907444905013090;
RA Blicher T., Kastrup J.S., Buus S., Gajhede M.;
RT "High-resolution structure of HLA-A*1101 in complex with SARS nucleocapsid
RT peptide.";
RL Acta Crystallogr. D 61:1031-1040(2005).
RN [34]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 270-370.
RX PubMed=16627473; DOI=10.1074/jbc.m602107200;
RA Yu I.M., Oldham M.L., Zhang J., Chen J.;
RT "Crystal structure of the severe acute respiratory syndrome (SARS)
RT coronavirus nucleocapsid protein dimerization domain reveals evolutionary
RT linkage between corona- and arteriviridae.";
RL J. Biol. Chem. 281:17134-17139(2006).
RN [35]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 248-365.
RX PubMed=17379242; DOI=10.1016/j.jmb.2007.02.069;
RA Chen C.Y., Chang C.K., Chang Y.W., Sue S.C., Bai H.I., Riang L.,
RA Hsiao C.D., Huang T.H.;
RT "Structure of the SARS coronavirus nucleocapsid protein RNA-binding
RT dimerization domain suggests a mechanism for helical packaging of viral
RT RNA.";
RL J. Mol. Biol. 368:1075-1086(2007).
RN [36]
RP RNA-BINDING, AND X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) OF 49-129.
RC STRAIN=Isolate Tor2;
RX PubMed=17229691; DOI=10.1128/jvi.02236-06;
RA Saikatendu K.S., Joseph J.S., Subramanian V., Neuman B.W., Buchmeier M.J.,
RA Stevens R.C., Kuhn P.;
RT "Ribonucleocapsid formation of severe acute respiratory syndrome
RT coronavirus through molecular action of the N-terminal domain of N
RT protein.";
RL J. Virol. 81:3913-3921(2007).
RN [37]
RP STRUCTURE BY NMR OF 248-365.
RX PubMed=18561946; DOI=10.1016/j.jmb.2007.11.093;
RA Takeda M., Chang C.K., Ikeya T., Guentert P., Chang Y.H., Hsu Y.L.,
RA Huang T.H., Kainosho M.;
RT "Solution structure of the c-terminal dimerization domain of SARS
RT coronavirus nucleocapsid protein solved by the SAIL-NMR method.";
RL J. Mol. Biol. 380:608-622(2008).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 346-354.
RX PubMed=20844028; DOI=10.1128/jvi.01464-10;
RA Liu J., Wu P., Gao F., Qi J., Kawana-Tachikawa A., Xie J., Vavricka C.J.,
RA Iwamoto A., Li T., Gao G.F.;
RT "Novel immunodominant peptide presentation strategy: a featured HLA-A*2402-
RT restricted cytotoxic T-lymphocyte epitope stabilized by intrachain hydrogen
RT bonds from severe acute respiratory syndrome coronavirus nucleocapsid
RT protein.";
RL J. Virol. 84:11849-11857(2010).
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 (PubMed:17210170). May modulate transforming growth factor-beta
CC signaling by binding host SMAD3 (PubMed:18055455). {ECO:0000255|HAMAP-
CC Rule:MF_04096, ECO:0000269|PubMed:17210170,
CC ECO:0000269|PubMed:18055455}.
CC -!- SUBUNIT: Homooligomer. Both monomeric and oligomeric forms interact
CC with RNA. Interacts with protein M (PubMed:15351485). Interacts with
CC protein E (PubMed:24766657). May bind to host HNRNPA1 (Probable).
CC Interacts with NSP3; this interaction serves to tether the genome to
CC the newly translated replicase-transcriptase complex at a very early
CC stage of infection (By similarity). May interact with host SMAD3
CC (Probable). Interacts with host PPIA/CYPA (PubMed:15688292).
CC {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:15351485,
CC ECO:0000269|PubMed:15688292, ECO:0000269|PubMed:24766657,
CC ECO:0000305|PubMed:15862300, ECO:0000305|PubMed:18055455}.
CC -!- INTERACTION:
CC P59595; P59637: E; NbExp=4; IntAct=EBI-7602718, EBI-25487741;
CC P59595; P59596: M; NbExp=19; IntAct=EBI-7602718, EBI-25487824;
CC P59595; P59595: N; NbExp=42; IntAct=EBI-7602718, EBI-7602718;
CC P59595; P24385: CCND1; Xeno; NbExp=3; IntAct=EBI-7602718, EBI-375001;
CC P59595; Q05639: EEF1A2; Xeno; NbExp=10; IntAct=EBI-7602718, EBI-354943;
CC P59595; Q13283: G3BP1; Xeno; NbExp=12; IntAct=EBI-7602718, EBI-1047359;
CC P59595; Q92830: KAT2A; Xeno; NbExp=2; IntAct=EBI-7602718, EBI-477622;
CC P59595; Q92831: KAT2B; Xeno; NbExp=2; IntAct=EBI-7602718, EBI-477430;
CC P59595; P62937: PPIA; Xeno; NbExp=4; IntAct=EBI-7602718, EBI-437708;
CC P59595; O75569: PRKRA; Xeno; NbExp=6; IntAct=EBI-7602718, EBI-713955;
CC P59595; P62333: PSMC6; Xeno; NbExp=3; IntAct=EBI-7602718, EBI-357669;
CC P59595; P84025: Smad3; Xeno; NbExp=4; IntAct=EBI-7602718, EBI-7201857;
CC P59595; P63279: UBE2I; Xeno; NbExp=12; IntAct=EBI-7602718, EBI-80168;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:17210170, ECO:0000269|PubMed:19106108}. Host
CC endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:17210170}. Host
CC Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:17210170}. Host cytoplasm, host perinuclear region
CC {ECO:0000269|PubMed:17210170}. Host nucleus
CC {ECO:0000269|PubMed:18155731}. 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_04096}.
CC -!- PTM: Proteolytically cleaved by host CASP6. The cleavage leads to two
CC fragments and facilitates viral replication by inhibiting host IFN
CC signaling. The two fragments may interact with IRF3 inhibiting its
CC nuclear translocation after activation and reduce the expression of
CC IFNB and IFN-stimulated genes. {ECO:0000269|PubMed:35922005}.
CC -!- PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC during infection. {ECO:0000255|HAMAP-Rule:MF_04096,
CC ECO:0000269|PubMed:29199039}.
CC -!- PTM: Phosphorylated on serine and threonine residues (PubMed:19106108).
CC Phosphorylated by host GSK3A and GSK3B. Phosphorylation allows
CC recruitment of host RNA helicase DDX1 which facilitates template
CC readthrough and enables longer subgenomic mRNA synthesis. This promotes
CC the solubility of homodimers that would otherwise aggregate
CC (PubMed:32974389). Host phosphatase would dephosphorylate the protein
CC during assembly at M bound membranes (PubMed:32974389).
CC {ECO:0000269|PubMed:19106108, ECO:0000269|PubMed:24766657,
CC ECO:0000305|PubMed:32974389}.
CC -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR EMBL; AY278741; AAP13445.1; -; Genomic_RNA.
DR EMBL; AY274119; AAP41047.1; -; Genomic_RNA.
DR EMBL; AY278554; AAP13814.1; -; Genomic_RNA.
DR EMBL; AY282752; AAP30714.1; -; Genomic_RNA.
DR EMBL; AY304492; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY304495; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278491; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283794; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283795; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283796; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY283797; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278487; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY278488; AAP30037.1; -; Genomic_RNA.
DR EMBL; AY278489; AAP51234.1; -; Genomic_RNA.
DR EMBL; AY278490; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY279354; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY291451; AAP37024.1; -; Genomic_RNA.
DR EMBL; AY310120; AAP50495.1; -; Genomic_RNA.
DR EMBL; AY291315; AAP33707.1; -; Genomic_RNA.
DR EMBL; AY307165; AAP49024.1; -; Genomic_RNA.
DR EMBL; AY290752; AAP44772.1; -; Genomic_RNA.
DR EMBL; AY321118; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AH012999; AAP82974.1; -; Genomic_RNA.
DR EMBL; AY338174; AAQ01605.1; -; Genomic_RNA.
DR EMBL; AY338175; AAQ01617.1; -; Genomic_RNA.
DR EMBL; AY348314; AAP97890.1; -; Genomic_RNA.
DR EMBL; AP006557; BAC81358.1; -; Genomic_RNA.
DR EMBL; AP006558; BAC81372.1; -; Genomic_RNA.
DR EMBL; AP006559; BAC81386.1; -; Genomic_RNA.
DR EMBL; AP006560; BAC81400.1; -; Genomic_RNA.
DR EMBL; AP006561; BAC81414.1; -; Genomic_RNA.
DR EMBL; AY323977; AAP72984.1; -; Genomic_RNA.
DR EMBL; AY362698; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY362699; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; AY427439; AAQ94070.1; -; Genomic_RNA.
DR PDB; 1SSK; NMR; -; A=45-181.
DR PDB; 1X7Q; X-ray; 1.45 A; C=362-370.
DR PDB; 2CJR; X-ray; 2.50 A; A/B/C/D/E/F/G/H=248-365.
DR PDB; 2GIB; X-ray; 1.75 A; A/B=270-370.
DR PDB; 2JW8; NMR; -; A/B=248-365.
DR PDB; 2OFZ; X-ray; 1.17 A; A=49-174.
DR PDB; 2OG3; X-ray; 1.85 A; A=49-174.
DR PDB; 3I6L; X-ray; 2.40 A; F=346-354.
DR PDB; 6IEX; X-ray; 2.31 A; C=216-225.
DR PDB; 7LG0; X-ray; 2.30 A; C=106-114.
DR PDBsum; 1SSK; -.
DR PDBsum; 1X7Q; -.
DR PDBsum; 2CJR; -.
DR PDBsum; 2GIB; -.
DR PDBsum; 2JW8; -.
DR PDBsum; 2OFZ; -.
DR PDBsum; 2OG3; -.
DR PDBsum; 3I6L; -.
DR PDBsum; 6IEX; -.
DR PDBsum; 7LG0; -.
DR BMRB; P59595; -.
DR SMR; P59595; -.
DR BioGRID; 4383916; 104.
DR ComplexPortal; CPX-5720; SARS-CoV nucleocapsid complex.
DR IntAct; P59595; 252.
DR MINT; P59595; -.
DR iPTMnet; P59595; -.
DR ABCD; P59595; 13 sequenced antibodies.
DR DNASU; 1489678; -.
DR OrthoDB; 3036at10239; -.
DR Reactome; R-HSA-9678110; Attachment and Entry.
DR Reactome; R-HSA-9679509; Virion Assembly and Release.
DR Reactome; R-HSA-9682708; Transcription of SARS-CoV-1 sgRNAs.
DR Reactome; R-HSA-9683610; Maturation of nucleoprotein.
DR Reactome; R-HSA-9683701; Translation of Structural Proteins.
DR Reactome; R-HSA-9692914; SARS-CoV-1-host interactions.
DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses.
DR Reactome; R-HSA-9735869; SARS-CoV-1 modulates host translation machinery.
DR Reactome; R-HSA-9735871; SARS-CoV-1 targets host intracellular signalling and regulatory pathways.
DR SIGNOR; P59595; -.
DR EvolutionaryTrace; P59595; -.
DR Proteomes; UP000000354; Segment.
DR Proteomes; UP000103670; Genome.
DR Proteomes; UP000109640; Genome.
DR Proteomes; UP000116947; Genome.
DR Proteomes; UP000121636; Genome.
DR Proteomes; UP000131569; Genome.
DR Proteomes; UP000131955; Genome.
DR Proteomes; UP000137377; Genome.
DR Proteomes; UP000138690; Genome.
DR Proteomes; UP000143093; Genome.
DR Proteomes; UP000145651; Genome.
DR Proteomes; UP000146108; Genome.
DR Proteomes; UP000146181; Genome.
DR Proteomes; UP000146296; Genome.
DR Proteomes; UP000148194; Genome.
DR Proteomes; UP000153467; Genome.
DR Proteomes; UP000160648; Genome.
DR Proteomes; UP000172416; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0044177; C:host cell Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; ISO:ComplexPortal.
DR GO; GO:0019013; C:viral nucleocapsid; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; EXP:DisProt.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; EXP:DisProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:ComplexPortal.
DR GO; GO:0019074; P:viral RNA genome packaging; NAS:ComplexPortal.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
DR DisProt; DP00948; -.
DR HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
DR InterPro; IPR044344; N_prot_C_CoV.
DR InterPro; IPR044345; N_prot_N_CoV.
DR InterPro; IPR043505; NCAP_bCoV.
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; SSF110304; Coronavirus RNA-binding domain; 1.
DR SUPFAM; SSF103068; Nucleocapsid protein dimerization domain; 1.
DR PROSITE; PS51929; COV_N_CTD; 1.
DR PROSITE; PS51928; COV_N_NTD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Host cytoplasm; Host Golgi apparatus;
KW Host nucleus; Host-virus interaction; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Transcription; Transcription regulation;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..422
FT /note="Nucleoprotein"
FT /id="PRO_0000106003"
FT DOMAIN 49..176
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT DOMAIN 248..365
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..187
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 45..181
FT /note="RNA-binding"
FT REGION 167..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..204
FT /note="SR region"
FT /evidence="ECO:0000305|PubMed:32974389"
FT REGION 234..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..362
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 362..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 257..265
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:18155731"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 93
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000250|UniProtKB:P0DTC9"
FT BINDING 108
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000250|UniProtKB:P0DTC9"
FT BINDING 150
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /evidence="ECO:0000250|UniProtKB:P0DTC9"
FT SITE 400..403
FT /note="Cleavage (by host CASP6)"
FT /evidence="ECO:0000269|PubMed:18155731"
FT MOD_RES 177
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096,
FT ECO:0000269|PubMed:19106108"
FT VARIANT 50
FT /note="T -> I (in strain: Isolate Frankfurt 1 and Isolate
FT FRA)"
FT VARIANT 154
FT /note="N -> Y (in strain: Isolate BJ03)"
FT VARIANT 193
FT /note="G -> C (in strain: Isolate CUHK-Su10)"
FT VARIANT 325..326
FT /note="VT -> AA (in strain: Isolate Shanghai LY)"
FT MUTAGEN 257..262
FT /note="KKPRQK->GGPRQG: Loss of cleavage by host CASP6."
FT /evidence="ECO:0000269|PubMed:18155731"
FT MUTAGEN 400..403
FT /note="DMDD->EMDE: Loss of cleavage by host CASP6."
FT /evidence="ECO:0000269|PubMed:18155731"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:1SSK"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2OG3"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1SSK"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2OFZ"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:2OFZ"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:2OFZ"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:1SSK"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:2OFZ"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:2OFZ"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:2OFZ"
FT STRAND 131..135
FT /evidence="ECO:0007829|PDB:2OFZ"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2OFZ"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2OFZ"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:2OFZ"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:2CJR"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:2CJR"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:2GIB"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:2JW8"
FT HELIX 290..295
FT /evidence="ECO:0007829|PDB:2GIB"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:2GIB"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:2GIB"
FT HELIX 312..318
FT /evidence="ECO:0007829|PDB:2GIB"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:2GIB"
FT STRAND 330..340
FT /evidence="ECO:0007829|PDB:2GIB"
FT HELIX 347..357
FT /evidence="ECO:0007829|PDB:2GIB"
FT HELIX 360..363
FT /evidence="ECO:0007829|PDB:2GIB"
SQ SEQUENCE 422 AA; 46025 MW; 43FC8750F1253034 CRC64;
MSDNGPQSNQ RSAPRITFGG PTDSTDNNQN GGRNGARPKQ RRPQGLPNNT ASWFTALTQH
GKEELRFPRG QGVPINTNSG PDDQIGYYRR ATRRVRGGDG KMKELSPRWY FYYLGTGPEA
SLPYGANKEG IVWVATEGAL NTPKDHIGTR NPNNNAATVL QLPQGTTLPK GFYAEGSRGG
SQASSRSSSR SRGNSRNSTP GSSRGNSPAR MASGGGETAL ALLLLDRLNQ LESKVSGKGQ
QQQGQTVTKK SAAEASKKPR QKRTATKQYN VTQAFGRRGP EQTQGNFGDQ DLIRQGTDYK
HWPQIAQFAP SASAFFGMSR IGMEVTPSGT WLTYHGAIKL DDKDPQFKDN VILLNKHIDA
YKTFPPTEPK KDKKKKTDEA QPLPQRQKKQ PTVTLLPAAD MDDFSRQLQN SMSGASADST
QA
//