NCAP_SARS2
ID NCAP_SARS2 Reviewed; 419 AA.
AC P0DTC9;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04096};
DE Short=N;
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};
OS Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Nidovirales; Cornidovirineae; Coronaviridae; Orthocoronavirinae;
OC Betacoronavirus; Sarbecovirus.
OX NCBI_TaxID=2697049;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=32015508; DOI=10.1038/s41586-020-2008-3;
RA Wu F., Zhao S., Yu B., Chen Y.-M., Wang W., Song Z.-G., Hu Y., Tao Z.-W.,
RA Tian J.-H., Pei Y.-Y., Yuan M.-L., Zhang Y.-L., Dai F.-H., Liu Y.,
RA Wang Q.-M., Zheng J.-J., Xu L., Holmes E.C., Zhang Y.-Z.;
RT "A new coronavirus associated with human respiratory disease in China.";
RL Nature 579:265-269(2020).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=33060197; DOI=10.1126/science.abe9403;
RG QCRG Structural Biology Consortium;
RG Zoonomia Consortium;
RA Gordon D.E., Hiatt J., Bouhaddou M., Rezelj V.V., Ulferts S., Braberg H.,
RA Jureka A.S., Obernier K., Guo J.Z., Batra J., Kaake R.M., Weckstein A.R.,
RA Owens T.W., Gupta M., Pourmal S., Titus E.W., Cakir M., Soucheray M.,
RA McGregor M., Cakir Z., Jang G., O'Meara M.J., Tummino T.A., Zhang Z.,
RA Foussard H., Rojc A., Zhou Y., Kuchenov D., Huettenhain R., Xu J.,
RA Eckhardt M., Swaney D.L., Fabius J.M., Ummadi M., Tutuncuoglu B.,
RA Rathore U., Modak M., Haas P., Haas K.M., Naing Z.Z.C., Pulido E.H.,
RA Shi Y., Barrio-Hernandez I., Memon D., Petsalaki E., Dunham A.,
RA Marrero M.C., Burke D., Koh C., Vallet T., Silvas J.A., Azumaya C.M.,
RA Billesboelle C., Brilot A.F., Campbell M.G., Diallo A., Dickinson M.S.,
RA Diwanji D., Herrera N., Hoppe N., Kratochvil H.T., Liu Y., Merz G.E.,
RA Moritz M., Nguyen H.C., Nowotny C., Puchades C., Rizo A.N.,
RA Schulze-Gahmen U., Smith A.M., Sun M., Young I.D., Zhao J., Asarnow D.,
RA Biel J., Bowen A., Braxton J.R., Chen J., Chio C.M., Chio U.S.,
RA Deshpande I., Doan L., Faust B., Flores S., Jin M., Kim K., Lam V.L.,
RA Li F., Li J., Li Y.L., Li Y., Liu X., Lo M., Lopez K.E., Melo A.A.,
RA Moss F.R. III, Nguyen P., Paulino J., Pawar K.I., Peters J.K.,
RA Pospiech T.H. Jr., Safari M., Sangwan S., Schaefer K., Thomas P.V.,
RA Thwin A.C., Trenker R., Tse E., Tsui T.K.M., Wang F., Whitis N., Yu Z.,
RA Zhang K., Zhang Y., Zhou F., Saltzberg D., Hodder A.J., Shun-Shion A.S.,
RA Williams D.M., White K.M., Rosales R., Kehrer T., Miorin L., Moreno E.,
RA Patel A.H., Rihn S., Khalid M.M., Vallejo-Gracia A., Fozouni P.,
RA Simoneau C.R., Roth T.L., Wu D., Karim M.A., Ghoussaini M., Dunham I.,
RA Berardi F., Weigang S., Chazal M., Park J., Logue J., McGrath M.,
RA Weston S., Haupt R., Hastie C.J., Elliott M., Brown F., Burness K.A.,
RA Reid E., Dorward M., Johnson C., Wilkinson S.G., Geyer A., Giesel D.M.,
RA Baillie C., Raggett S., Leech H., Toth R., Goodman N., Keough K.C.,
RA Lind A.L., Klesh R.J., Hemphill K.R., Carlson-Stevermer J., Oki J.,
RA Holden K., Maures T., Pollard K.S., Sali A., Agard D.A., Cheng Y.,
RA Fraser J.S., Frost A., Jura N., Kortemme T., Manglik A., Southworth D.R.,
RA Stroud R.M., Alessi D.R., Davies P., Frieman M.B., Ideker T., Abate C.,
RA Jouvenet N., Kochs G., Shoichet B., Ott M., Palmarini M., Shokat K.M.,
RA Garcia-Sastre A., Rassen J.A., Grosse R., Rosenberg O.S., Verba K.A.,
RA Basler C.F., Vignuzzi M., Peden A.A., Beltrao P., Krogan N.J.;
RT "Comparative host-coronavirus protein interaction networks reveal pan-viral
RT disease mechanisms.";
RL Science 0:0-0(2020).
RN [3]
RP VARIANTS LEU-3 AND F-235.
RC STRAIN=20B/501Y.V1, B.1.1.7, VOC-202012/01, and VUI-202012/01;
RX PubMed=33413740; DOI=10.2807/1560-7917.es.2020.26.1.2002106;
RA Leung K., Shum M.H., Leung G.M., Lam T.T., Wu J.T.;
RT "Early transmissibility assessment of the N501Y mutant strains of SARS-CoV-
RT 2 in the United Kingdom, October to November 2020.";
RL Eurosurveillance 26:0-0(2021).
RN [4]
RP FUNCTION, INTERACTION WITH HOST NLRP3, AND SUBCELLULAR LOCATION.
RX PubMed=34341353; DOI=10.1038/s41467-021-25015-6;
RA Pan P., Shen M., Yu Z., Ge W., Chen K., Tian M., Xiao F., Wang Z., Wang J.,
RA Jia Y., Wang W., Wan P., Zhang J., Chen W., Lei Z., Chen X., Luo Z.,
RA Zhang Q., Xu M., Li G., Li Y., Wu J.;
RT "SARS-CoV-2 N protein promotes NLRP3 inflammasome activation to induce
RT hyperinflammation.";
RL Nat. Commun. 12:4664-4664(2021).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 41-174, AND MUTAGENESIS OF
RP TYR-109.
RX PubMed=32363136; DOI=10.1016/j.apsb.2020.04.009;
RA Kang S., Yang M., Hong Z., Zhang L., Huang Z., Chen X., He S., Zhou Z.,
RA Zhou Z., Chen Q., Yan Y., Zhang C., Shan H., Chen S.;
RT "Crystal structure of SARS-CoV-2 nucleocapsid protein RNA binding domain
RT reveals potential unique drug targeting sites.";
RL Acta Pharmacol. Sin. 10:1228-1238(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 (By
CC similarity). {ECO:0000250|UniProtKB:P59595, ECO:0000255|HAMAP-
CC Rule:MF_04096}.
CC -!- FUNCTION: May induce inflammasome responses in cultured cells and mice.
CC Acts by interacting with host NLRP3 to facilitate inflammasome
CC assembly, which induces cytokine release that may play a role in COVID
CC lung injury. {ECO:0000269|PubMed:34341353}.
CC -!- SUBUNIT: Homooligomer. Both monomeric and oligomeric forms interact
CC with RNA. Interacts with protein M. Interacts with protein E. Interacts
CC with NSP3; this interaction serves to tether the genome to the newly
CC translated replicase-transcriptase complex at a very early stage of
CC infection (By similarity). May interact with host NLRP3
CC (PubMed:34341353). {ECO:0000250|UniProtKB:P59595, ECO:0000255|HAMAP-
CC Rule:MF_04096, ECO:0000269|PubMed:34341353}.
CC -!- INTERACTION:
CC P0DTC9; P0DTC4: E; NbExp=3; IntAct=EBI-25475856, EBI-25475850;
CC P0DTC9; P0DTC5: M; NbExp=6; IntAct=EBI-25475856, EBI-25475853;
CC P0DTC9; P0DTC9: N; NbExp=101; IntAct=EBI-25475856, EBI-25475856;
CC P0DTC9; PRO_0000449621 [P0DTD1]: rep; NbExp=13; IntAct=EBI-25475856, EBI-25492388;
CC P0DTC9; P78563: ADARB1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-2967304;
CC P0DTC9; O15145: ARPC3; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-351829;
CC P0DTC9; Q13895: BYSL; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-358049;
CC P0DTC9; Q16543: CDC37; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-295634;
CC P0DTC9; Q92793: CREBBP; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-81215;
CC P0DTC9; O95786: DDX58; Xeno; NbExp=9; IntAct=EBI-25475856, EBI-995350;
CC P0DTC9; Q08426: EHHADH; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-2339219;
CC P0DTC9; P19525: EIF2AK2; Xeno; NbExp=8; IntAct=EBI-25475856, EBI-640775;
CC P0DTC9; Q14241: ELOA; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-742350;
CC P0DTC9; Q13283: G3BP1; Xeno; NbExp=54; IntAct=EBI-25475856, EBI-1047359;
CC P0DTC9; Q9UN86: G3BP2; Xeno; NbExp=32; IntAct=EBI-25475856, EBI-1044298;
CC P0DTC9; P57764: GSDMD; Xeno; NbExp=13; IntAct=EBI-25475856, EBI-2798865;
CC P0DTC9; P49841: GSK3B; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-373586;
CC P0DTC9; O14920: IKBKB; Xeno; NbExp=7; IntAct=EBI-25475856, EBI-81266;
CC P0DTC9; Q92830: KAT2A; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-477622;
CC P0DTC9; Q92831: KAT2B; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-477430;
CC P0DTC9; Q07866: KLC1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-721019;
CC P0DTC9; Q9H0B6: KLC2; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-726994;
CC P0DTC9; Q9NSK0: KLC4; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-949319;
CC P0DTC9; Q9NX58: LYAR; Xeno; NbExp=6; IntAct=EBI-25475856, EBI-713507;
CC P0DTC9; O43318: MAP3K7; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-358684;
CC P0DTC9; Q9UBU8: MORF4L1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-399246;
CC P0DTC9; Q15014: MORF4L2; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-399257;
CC P0DTC9; Q9HCE1: MOV10; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-1055820;
CC P0DTC9; O15226: NKRF; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-766011;
CC P0DTC9; Q96P20: NLRP3; Xeno; NbExp=18; IntAct=EBI-25475856, EBI-6253230;
CC P0DTC9; O15118: NPC1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-2368710;
CC P0DTC9; Q96HA8: NTAQ1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-741158;
CC P0DTC9; P62937: PPIA; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-437708;
CC P0DTC9; O75569: PRKRA; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-713955;
CC P0DTC9; Q99873: PRMT1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-78738;
CC P0DTC9; P61289: PSME3; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-355546;
CC P0DTC9; P54727: RAD23B; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-954531;
CC P0DTC9; P37840: SNCA; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-985879;
CC P0DTC9; Q96SB4: SRPK1; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-539478;
CC P0DTC9; P78362: SRPK2; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-593303;
CC P0DTC9; P42224: STAT1; Xeno; NbExp=6; IntAct=EBI-25475856, EBI-1057697;
CC P0DTC9; P52630: STAT2; Xeno; NbExp=7; IntAct=EBI-25475856, EBI-1546963;
CC P0DTC9; Q15633: TARBP2; Xeno; NbExp=5; IntAct=EBI-25475856, EBI-978581;
CC P0DTC9; Q14258: TRIM25; Xeno; NbExp=13; IntAct=EBI-25475856, EBI-2341129;
CC P0DTC9; O60763: USO1; Xeno; NbExp=4; IntAct=EBI-25475856, EBI-356164;
CC P0DTC9; Q93008: USP9X; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-302524;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC cytoplasm {ECO:0000269|PubMed:33060197, ECO:0000269|PubMed:34341353}.
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: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.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
CC -!- POLYMORPHISM: Variant Alpha/B.1.1.7 belongs to a lineage isolated first
CC in United Kingdom (December 2020). It is also called Variant of Concern
CC (VOC) 202012/01, Variant Under Investigation (VUI) 202012/01, 501Y.V1
CC or 20B/501Y.V1. {ECO:0000305|PubMed:33413740}.
CC -!- POLYMORPHISM: Variant Omicron/BA.1 and BA.2 belong to a lineage first
CC isolated in South Africa (November 2021). {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the betacoronavirus nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04096}.
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DR EMBL; MN908947; QHD43423.2; -; Genomic_RNA.
DR RefSeq; YP_009724397.2; NC_045512.2.
DR PDB; 6M3M; X-ray; 2.70 A; A/B/C/D=41-174.
DR PDB; 6VYO; X-ray; 1.70 A; A/B/C/D=47-173.
DR PDB; 6WJI; X-ray; 2.05 A; A/B/C/D/E/F=257-364.
DR PDB; 6WKP; X-ray; 2.67 A; A/B/C/D=47-173.
DR PDB; 6WZO; X-ray; 1.42 A; A/B/C/D=247-364.
DR PDB; 6WZQ; X-ray; 1.45 A; A/B/C/D=247-364.
DR PDB; 6YI3; NMR; -; A=44-180.
DR PDB; 6YUN; X-ray; 1.44 A; A/B=249-364.
DR PDB; 6ZCO; X-ray; 1.36 A; A=247-364.
DR PDB; 7ACS; NMR; -; A=44-180.
DR PDB; 7ACT; NMR; -; A=44-180.
DR PDB; 7C22; X-ray; 2.00 A; A/B/C/D=248-364.
DR PDB; 7CDZ; X-ray; 1.80 A; A/B/C/D=44-174.
DR PDB; 7CE0; X-ray; 1.50 A; A/B/C/D=255-364.
DR PDB; 7CR5; X-ray; 2.08 A; A=41-174.
DR PDB; 7DE1; X-ray; 2.00 A; A/B=250-364.
DR PDB; 7F2B; X-ray; 2.00 A; A/B=257-362.
DR PDB; 7F2E; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J/K/L=255-362.
DR PDB; 7KGO; X-ray; 2.15 A; C=351-359.
DR PDB; 7KGP; X-ray; 1.40 A; C=316-324.
DR PDB; 7KGQ; X-ray; 1.34 A; C=222-230.
DR PDB; 7KGR; X-ray; 1.55 A; C=159-167.
DR PDB; 7KGS; X-ray; 1.58 A; C=138-146.
DR PDB; 7KGT; X-ray; 1.90 A; C=226-234.
DR PDB; 7LGD; X-ray; 2.88 A; E/F=105-113.
DR PDB; 7LTU; X-ray; 1.12 A; A/B=217-222.
DR PDB; 7LUX; X-ray; 1.30 A; A=217-222.
DR PDB; 7LUZ; X-ray; 1.10 A; A=243-248.
DR PDB; 7LV2; X-ray; 1.30 A; A=179-184.
DR PDB; 7N0I; X-ray; 2.20 A; A/B/C/D/E/F/G/H=269-364.
DR PDB; 7N0R; X-ray; 1.42 A; A/B=49-174.
DR PDB; 7N3C; X-ray; 1.82 A; C=47-173.
DR PDB; 7N3D; X-ray; 1.53 A; C=47-173.
DR PDB; 7O05; X-ray; 1.94 A; A/B/C/D=247-364.
DR PDB; 7O35; X-ray; 1.80 A; A/B/C/D=247-364.
DR PDB; 7O36; X-ray; 2.00 A; A/B/C/D=247-364.
DR PDB; 7R98; X-ray; 2.51 A; A/B/C=49-174.
DR PDB; 7VNU; X-ray; 1.95 A; A/B/C/D=47-174.
DR PDBsum; 6M3M; -.
DR PDBsum; 6VYO; -.
DR PDBsum; 6WJI; -.
DR PDBsum; 6WKP; -.
DR PDBsum; 6WZO; -.
DR PDBsum; 6WZQ; -.
DR PDBsum; 6YI3; -.
DR PDBsum; 6YUN; -.
DR PDBsum; 6ZCO; -.
DR PDBsum; 7ACS; -.
DR PDBsum; 7ACT; -.
DR PDBsum; 7C22; -.
DR PDBsum; 7CDZ; -.
DR PDBsum; 7CE0; -.
DR PDBsum; 7CR5; -.
DR PDBsum; 7DE1; -.
DR PDBsum; 7F2B; -.
DR PDBsum; 7F2E; -.
DR PDBsum; 7KGO; -.
DR PDBsum; 7KGP; -.
DR PDBsum; 7KGQ; -.
DR PDBsum; 7KGR; -.
DR PDBsum; 7KGS; -.
DR PDBsum; 7KGT; -.
DR PDBsum; 7LGD; -.
DR PDBsum; 7LTU; -.
DR PDBsum; 7LUX; -.
DR PDBsum; 7LUZ; -.
DR PDBsum; 7LV2; -.
DR PDBsum; 7N0I; -.
DR PDBsum; 7N0R; -.
DR PDBsum; 7N3C; -.
DR PDBsum; 7N3D; -.
DR PDBsum; 7O05; -.
DR PDBsum; 7O35; -.
DR PDBsum; 7O36; -.
DR PDBsum; 7R98; -.
DR PDBsum; 7VNU; -.
DR BMRB; P0DTC9; -.
DR SMR; P0DTC9; -.
DR BioGRID; 4383847; 545.
DR ComplexPortal; CPX-5686; SARS-CoV-2 nucleocapsid complex.
DR IntAct; P0DTC9; 518.
DR ABCD; P0DTC9; 26 sequenced antibodies.
DR DNASU; 43740575; -.
DR GeneID; 43740575; -.
DR KEGG; vg:43740575; -.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR Reactome; R-HSA-9694322; Virion Assembly and Release.
DR Reactome; R-HSA-9694614; Attachment and Entry.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR Reactome; R-HSA-9694635; Translation of Structural Proteins.
DR Reactome; R-HSA-9694786; Transcription of SARS-CoV-2 sgRNAs.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9755779; SARS-CoV-2 targets host intracellular signalling and regulatory pathways.
DR SIGNOR; P0DTC9; -.
DR PRO; PR:P0DTC9; -.
DR Proteomes; UP000464024; Genome.
DR GO; GO:0044172; C:host cell endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0044177; C:host cell Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0019028; C:viral capsid; IPI:ComplexPortal.
DR GO; GO:0019013; C:viral nucleocapsid; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IDA:ComplexPortal.
DR GO; GO:1900227; P:positive regulation of NLRP3 inflammasome complex assembly; IDA:UniProtKB.
DR GO; GO:0019074; P:viral RNA genome packaging; IC:ComplexPortal.
DR CDD; cd21595; CoV_N-CTD; 1.
DR CDD; cd21554; CoV_N-NTD; 1.
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; 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 3D-structure; ADP-ribosylation; Host cytoplasm; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; RNA-binding; Transcription;
KW Transcription regulation; Viral nucleoprotein; Virion.
FT CHAIN 1..419
FT /note="Nucleoprotein"
FT /id="PRO_0000449656"
FT DOMAIN 48..174
FT /note="CoV N NTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01276,
FT ECO:0000269|PubMed:32363136"
FT DOMAIN 247..364
FT /note="CoV N CTD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..186
FT /note="RNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..361
FT /note="Dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT REGION 260..340
FT /note="Putative NLRP3 binding"
FT /evidence="ECO:0000269|PubMed:34341353"
FT REGION 361..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..382
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Phosphoserine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT VARIANT 2..3
FT /note="SD -> Y (in strain: Eta/B.1.525)"
FT /evidence="ECO:0000305"
FT VARIANT 3
FT /note="D -> L (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 12
FT /note="A -> G (in strain: Eta/B.1.525)"
FT VARIANT 13
FT /note="P -> L (in strain: Lambda/C.37, Omicron/BA.1,
FT Omicron/BA.2, Omicron/BA.2.12.1, Omicron/BA.4, Omicron/
FT BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 31..33
FT /note="Missing (in strain: Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 63
FT /note="D -> G (in strain: Delta/B.1.617.2)"
FT /evidence="ECO:0000305"
FT VARIANT 80
FT /note="P -> R (in strain: Gamma/P.1)"
FT /evidence="ECO:0000305"
FT VARIANT 119
FT /note="A -> S (in strain: Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 151
FT /note="P -> S (in strain: Omicron/BA.4)"
FT /evidence="ECO:0000305"
FT VARIANT 203..204
FT /note="RG -> KR (in strain: Alpha/B.1.1.7, Gamma/P.1, Zeta/
FT P.2, Theta/P.3, Lambda/C.37, Omicron/BA.1, Omicron/BA.2,
FT Omicron/BA.2.12.1, Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT VARIANT 203
FT /note="R -> M (in strain: Delta/B.1.617.2, Kappa/
FT B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 205
FT /note="T -> I (in strain: Beta/B.1.351, Epsilon/B.1.429,
FT Eta/B.1.525 and Mu/B.1.621)"
FT /evidence="ECO:0000305"
FT VARIANT 214
FT /note="G -> C (in strain: Lambda/C.37)"
FT VARIANT 234
FT /note="M -> I (in strain: Zeta/P.2)"
FT /evidence="ECO:0000305"
FT VARIANT 235
FT /note="S -> F (in strain: Alpha/B.1.1.7)"
FT /evidence="ECO:0000305|PubMed:33413740"
FT VARIANT 377
FT /note="D -> Y (in strain: Delta/B.1.617.2, Kappa/
FT B.1.617.1)"
FT /evidence="ECO:0000305"
FT VARIANT 413
FT /note="S -> R (in strain: Omicron/BA.2, Omicron/BA.2.12.1,
FT Omicron/BA.4, Omicron/BA.5)"
FT /evidence="ECO:0000305"
FT MUTAGEN 109
FT /note="Y->A: Significant decrease of RNA binding capacity."
FT /evidence="ECO:0000269|PubMed:32363136"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:7VNU"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:7N0R"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:7N0R"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:7N0R"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:7ACT"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7N3D"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:7N0R"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:7N0R"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7ACT"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7VNU"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:7ACT"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:7LTU"
FT HELIX 251..256
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:6ZCO"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:7CE0"
FT HELIX 270..274
FT /evidence="ECO:0007829|PDB:6ZCO"
FT STRAND 279..283
FT /evidence="ECO:0007829|PDB:7F2E"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 301..305
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 311..317
FT /evidence="ECO:0007829|PDB:6ZCO"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:6ZCO"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 346..356
FT /evidence="ECO:0007829|PDB:6ZCO"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:6ZCO"
SQ SEQUENCE 419 AA; 45626 MW; 56688DB785414E81 CRC64;
MSDNGPQNQR NAPRITFGGP SDSTGSNQNG ERSGARSKQR RPQGLPNNTA SWFTALTQHG
KEDLKFPRGQ GVPINTNSSP DDQIGYYRRA TRRIRGGDGK MKDLSPRWYF YYLGTGPEAG
LPYGANKDGI IWVATEGALN TPKDHIGTRN PANNAAIVLQ LPQGTTLPKG FYAEGSRGGS
QASSRSSSRS RNSSRNSTPG SSRGTSPARM AGNGGDAALA LLLLDRLNQL ESKMSGKGQQ
QQGQTVTKKS AAEASKKPRQ KRTATKAYNV TQAFGRRGPE QTQGNFGDQE LIRQGTDYKH
WPQIAQFAPS ASAFFGMSRI GMEVTPSGTW LTYTGAIKLD DKDPNFKDQV ILLNKHIDAY
KTFPPTEPKK DKKKKADETQ ALPQRQKKQQ TVTLLPAADL DDFSKQLQQS MSSADSTQA
