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   10-FEB-2021, entry version 6.
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).
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). May modulate transforming growth factor-beta signaling by
CC       binding host smad3 (By similarity). {ECO:0000250|UniProtKB:P59595,
CC       ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- SUBUNIT: Homooligomer. Both monomeric and oligomeric forms interact
CC       with RNA. Interacts with protein M. Interacts with protein E. May bind
CC       to host HNRNPA1. Interacts with NSP3; this interaction serves to tether
CC       the genome to the newly translated replicase-transcriptase complex at a
CC       very early stage of infection (By similarity). May interact with host
CC       SMAD3 (By similarity). {ECO:0000250|UniProtKB:P59595,
CC       ECO:0000255|HAMAP-Rule:MF_04096}.
CC   -!- INTERACTION:
CC       P0DTC9; P0DTC9: N; NbExp=7; IntAct=EBI-25475856, EBI-25475856;
CC       P0DTC9; P0DMV8: HSPA1A; Xeno; NbExp=2; IntAct=EBI-25475856, EBI-11052499;
CC       P0DTC9; P61289: PSME3; Xeno; NbExp=3; IntAct=EBI-25475856, EBI-355546;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04096}. Host
CC       cytoplasm {ECO:0000269|PubMed:33060197}. Note=Located inside the
CC       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_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   -!- 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   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   BMRB; P0DTC9; -.
DR   SMR; P0DTC9; -.
DR   BioGRID; 4383847; 172.
DR   ComplexPortal; CPX-5686; SARS-CoV-2 nucleocapsid complex.
DR   IntAct; P0DTC9; 32.
DR   GeneID; 43740575; -.
DR   KEGG; vg:43740575; -.
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-9694686; Replication of the SARS-CoV-2 genome.
DR   Reactome; R-HSA-9694786; Transcription of SARS-CoV-2 sgRNAs.
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: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-KW.
DR   HAMAP; MF_04096; BETA_CORONA_NCAP; 1.
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..175
FT                   /note="CoV N NTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01276"
FT   DOMAIN          247..364
FT                   /note="CoV N CTD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01277"
FT   REGION          41..186
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   REGION          258..361
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   MOD_RES         176
FT                   /note="Phosphoserine; by host"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04096"
FT   STRAND          56..58
FT                   /evidence="ECO:0000244|PDB:6M3M"
FT   STRAND          60..62
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          76..78
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   HELIX           80..82
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          84..90
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          93..95
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          99..103
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          107..112
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   TURN            117..120
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          130..134
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   TURN            144..146
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   TURN            151..153
FT                   /evidence="ECO:0000244|PDB:6VYO"
FT   STRAND          171..173
FT                   /evidence="ECO:0000244|PDB:6YI3"
FT   HELIX           251..256
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           259..261
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   STRAND          266..268
FT                   /evidence="ECO:0000244|PDB:6WJI"
FT   HELIX           270..274
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           289..294
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           295..297
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           301..305
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           311..317
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   STRAND          318..325
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   STRAND          328..334
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           346..356
FT                   /evidence="ECO:0000244|PDB:6ZCO"
FT   HELIX           359..362
FT                   /evidence="ECO:0000244|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
//