ID   NCAP_CVHSA              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   12-AUG-2020, entry version 124.
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   Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome
OS   coronavirus).
OC   Viruses; Riboviria; Nidovirales; Cornidovirineae; Coronaviridae;
OC   Orthocoronavirinae; 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   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   [24]
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   [25]
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   [26]
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   [27]
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   [28]
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   [29]
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   [30]
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   [31]
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   [32]
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   [33]
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). {ECO:0000255|HAMAP-Rule:MF_04096,
CC       ECO:0000269|PubMed:15351485, ECO:0000269|PubMed:24766657,
CC       ECO:0000305|PubMed:15862300, ECO:0000305|PubMed:18055455}.
CC   -!- INTERACTION:
CC       P59595; P59596: M; NbExp=2; IntAct=EBI-7602718, EBI-25487824;
CC       P59595; P59595: N; NbExp=17; IntAct=EBI-7602718, EBI-7602718;
CC       P59595; Q05639: EEF1A2; Xeno; NbExp=10; IntAct=EBI-7602718, EBI-354943;
CC       P59595; P62937: PPIA; Xeno; NbExp=2; IntAct=EBI-7602718, EBI-437708;
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}. 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: ADP-ribosylated. The ADP-ribosylation is retained in the virion
CC       during infection. {ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- PTM: Phosphorylated on serine and threonine residues (By similarity).
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.
CC       {ECO:0000255|HAMAP-Rule:MF_04096, ECO:0000269|PubMed:19106108,
CC       ECO:0000269|PubMed:24766657}.
CC   -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04096}.
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; AY322208; 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   RefSeq; NP_828858.1; NC_004718.3.
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   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   SMR; P59595; -.
DR   BioGRID; 4383916; 14.
DR   ComplexPortal; CPX-5720; SARS-CoV nucleocapsid complex.
DR   IntAct; P59595; 5.
DR   MINT; P59595; -.
DR   iPTMnet; P59595; -.
DR   PRIDE; P59595; -.
DR   ABCD; P59595; 11 sequenced antibodies.
DR   GeneID; 1489678; -.
DR   KEGG; vg:1489678; -.
DR   KO; K24106; -.
DR   SIGNOR; P59595; -.
DR   EvolutionaryTrace; P59595; -.
DR   Proteomes; UP000000354; Genome.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   DisProt; DP00948; -.
DR   HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
DR   InterPro; IPR043505; NCAP_bCoV.
DR   InterPro; IPR001218; Nucleocap_CoV.
DR   InterPro; IPR037179; Nucleocapsid_C.
DR   InterPro; IPR037195; Nucleocapsid_N.
DR   Pfam; PF00937; Corona_nucleoca; 1.
DR   PIRSF; PIRSF003888; Corona_nucleocap; 1.
DR   SUPFAM; SSF103068; SSF103068; 1.
DR   SUPFAM; SSF110304; SSF110304; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Host cytoplasm; Host Golgi apparatus;
KW   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   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          259..362
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   COMPBIAS        181..213
FT                   /note="Ser-rich"
FT   COMPBIAS        220..225
FT                   /note="Poly-Leu"
FT   COMPBIAS        240..245
FT                   /note="Poly-Gln"
FT   COMPBIAS        370..376
FT                   /note="Poly-Lys"
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   STRAND          56..59
FT                   /evidence="ECO:0000244|PDB:1SSK"
FT   STRAND          61..63
FT                   /evidence="ECO:0000244|PDB:2OG3"
FT   STRAND          77..79
FT                   /evidence="ECO:0000244|PDB:1SSK"
FT   HELIX           81..83
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   STRAND          85..91
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   STRAND          94..96
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   TURN            98..100
FT                   /evidence="ECO:0000244|PDB:1SSK"
FT   STRAND          102..104
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   STRAND          108..113
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   TURN            118..121
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   STRAND          131..135
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   STRAND          140..142
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   TURN            145..147
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   TURN            152..154
FT                   /evidence="ECO:0000244|PDB:2OFZ"
FT   STRAND          254..258
FT                   /evidence="ECO:0000244|PDB:2CJR"
FT   HELIX           260..262
FT                   /evidence="ECO:0000244|PDB:2CJR"
FT   HELIX           271..275
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   TURN            282..284
FT                   /evidence="ECO:0000244|PDB:2JW8"
FT   HELIX           290..295
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   HELIX           296..298
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   HELIX           302..306
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   HELIX           312..318
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   STRAND          319..325
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   STRAND          330..340
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   HELIX           347..357
FT                   /evidence="ECO:0000244|PDB:2GIB"
FT   HELIX           360..363
FT                   /evidence="ECO:0000244|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
//