ID   NCAP_EBOSB              Reviewed;         738 AA.
AC   Q9QP77;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=NP;
OS   Sudan ebolavirus (strain Boniface-76) (SEBOV) (Sudan Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus sudanense; Sudan ebolavirus.
OX   NCBI_TaxID=128948;
OH   NCBI_TaxID=77231; Epomops franqueti (Franquet's epauletted fruit bat) (Epomophorus franqueti).
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Crise B., Smith J.F., Bray M.;
RT   "Ebola Sudan nucleocapsid protein.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Oligomerizes into helical capsid to encapsidate the viral
CC       genome, protecting it from nucleases and the cellular innate immune
CC       response. VP35 binds to and stabilizes monomeric NP, keeping it
CC       soluble. Upon virus replication, NP is recruited to bind cooperatively
CC       viral genomic RNA and VP35 is released. The encapsidated genomic RNA is
CC       termed the nucleocapsid and serves as template for transcription and
CC       replication. The nucleocapsid is helical with a pitch of 10.81 NP per
CC       turn and a diameter of about 22nm. Each NP binds to six nucleotides of
CC       viral genomic RNA, three being exposed to the solvant and three hidden
CC       into the nucleocapsid. Recruits also host PPP2R5C phosphatase to
CC       dephosphorylate VP30 and thereby promote viral transcription. Upon
CC       virion assembly and budding, NP binds to VP24 and possibly host STAU1.
CC       {ECO:0000250|UniProtKB:P18272}.
CC   -!- SUBUNIT: Homooligomer. Homomultimerizes to form the nucleocapsid. Binds
CC       to viral genomic RNA. Interacts with VP35 and VP30 to form the
CC       nucleocapsid. Interacts with host PPP2R5C; this interaction leads to
CC       VP30 dephosphorylation and viral transcription. Interacts with VP24;
CC       this interaction facilitates nucleocapsid assembly and genome
CC       packaging. Interacts with matrix protein VP40; this interaction allows
CC       recruitment of the nucleocapsid into progeny virions. Interacts with
CC       host STAU1. Interacts with host NXF1 (via RNA-binding domain); this
CC       interaction recruits NXF1 to the inclusion bodies were viral
CC       replication takes place, probably to export viral mRNA-NXF1 complexes
CC       from these sites. Interacts with host CCDC92; this interaction
CC       sequesters NP in the host cytoplasm. Interacts with host TRIM14.
CC       {ECO:0000250|UniProtKB:P18272}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P18272}. Host
CC       cytoplasm {ECO:0000250|UniProtKB:P18272}.
CC   -!- DOMAIN: Comprizes a N-terminal arm involved in oligomerization, a NP
CC       core region involved in RNA binding, a disordered region follwoed by a
CC       C-terminal tail involved in protein-protein interactions. During
CC       oligomerization, NP N-terminal arm binds to a neighbor NP thereby
CC       displacing VP35 bound to monomeric NP. {ECO:0000250|UniProtKB:P18272}.
CC   -!- PTM: Phosphorylated and O-glycosylated by host. Acetylated by host
CC       EP300 in vitro. {ECO:0000250|UniProtKB:P18272}.
CC   -!- SIMILARITY: Belongs to the filoviruses nucleoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; AF173836; AAD51107.1; -; mRNA.
DR   PDB; 6U51; X-ray; 2.52 A; B/D=610-738.
DR   PDB; 6U52; X-ray; 1.90 A; B/D=632-738.
DR   PDB; 6U55; X-ray; 1.93 A; B=632-738.
DR   PDBsum; 6U51; -.
DR   PDBsum; 6U52; -.
DR   PDBsum; 6U55; -.
DR   SMR; Q9QP77; -.
DR   ABCD; Q9QP77; 2 sequenced antibodies.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019074; P:viral RNA genome packaging; IEA:InterPro.
DR   InterPro; IPR008609; Ebola_NP.
DR   Pfam; PF05505; Ebola_NP; 1.
DR   PIRSF; PIRSF003900; N_FiloV; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Coiled coil; Helical capsid protein;
KW   Host cytoplasm; Phosphoprotein; Ribonucleoprotein; RNA-binding;
KW   Viral nucleoprotein; Virion.
FT   CHAIN           1..738
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000222174"
FT   REGION          418..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          334..363
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        492..508
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..565
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..597
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          638..642
FT                   /evidence="ECO:0007829|PDB:6U55"
FT   HELIX           647..658
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   HELIX           661..672
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   STRAND          676..679
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   STRAND          685..688
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   HELIX           690..692
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   STRAND          693..696
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   HELIX           702..705
FT                   /evidence="ECO:0007829|PDB:6U55"
FT   HELIX           708..711
FT                   /evidence="ECO:0007829|PDB:6U55"
FT   STRAND          712..715
FT                   /evidence="ECO:0007829|PDB:6U55"
FT   STRAND          718..721
FT                   /evidence="ECO:0007829|PDB:6U55"
FT   HELIX           722..724
FT                   /evidence="ECO:0007829|PDB:6U52"
FT   HELIX           727..737
FT                   /evidence="ECO:0007829|PDB:6U52"
SQ   SEQUENCE   738 AA;  82008 MW;  21AFE1423CFBF9CD CRC64;
     MDKRVRGSWA LGGQSEVDLD YHKILTAGLS VQQGIVRQRV IPVYVVNDLE GICQHIIQAF
     EAGVDFQDNA DSFLLLLCLH HAYQGDHRLF LKSDAVQYLE GHGFRFEVRE KENVHRLDEL
     LPNVTGGKNL RRTLAAMPEE ETTEANAGQF LSFASLFLPK LVVGEKACLE KVQRQIQVHA
     EQGLIQYPTS WQSVGHMMVI FRLMRTNFLI KFLLIHQGMH MVAGHDANDT VISNSVAQAR
     FSGLLIVKTV LDHILQKTDL GVRLHPLART AKVKNEVSSF KAALGSLAKH GEYAPFARLL
     NLSGVNNLEH GLYPQLSAIA LGVATAHGST LAGVNVGEQY QQLREAATEA EKQLQQYAET
     RELDNLGLDE QEKKILMSFH QKKNEISFQQ TNAMVTLRKE RLAKLTEAIT TASKIKVGDR
     YPDDNDIPFP GPIYDDTHPN PSDDNPDDSR DTTIPGGVVD PYDDESNNYP DYEDSAEGTT
     GDLDLFNLDD DDDDSRPGPP DRGQNKERAA RTYGLQDPTL DGAKKVPELT PGSHQPGNLH
     ITKSGSNTNQ PQGNMSSTLH SMTPIQEESE PDDQKDNDDE SLTSLDSEGD EDGESISEEN
     TPTVAPPAPV YKDTGVDTNQ QNGPSSTVDS QGSESEALPI NSKKSSALEE TYYHLLKTQG
     PFEAINYYHL MSDEPIAFST ESGKEYIFPD SLEEAYPPWL SEKEALEKEN RYLVIDGQQF
     LWPVMSLRDK FLAVLQHD
//