ID   NCAP_EBOG4              Reviewed;         739 AA.
AC   Q9QCE9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 66.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Ebola NP;
DE            Short=eNP;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
GN   Name=NP;
OS   Zaire ebolavirus (strain Gabon-94) (ZEBOV) (Zaire Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus zairense; Zaire ebolavirus.
OX   NCBI_TaxID=128947;
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 [GENOMIC RNA].
RX   PubMed=9820131; DOI=10.1099/0022-1317-79-11-2565;
RA   Prehaud C.J.C., Hellebrand E., Coudrier D., Volchkov V.E., Volchkova V.A.,
RA   Feldmann B., Le Guenno B., Bouloy M.;
RT   "Recombinant Ebola virus nucleoprotein and glycoprotein (Gabon 94 strain)
RT   provide new tools for the detection of human infections.";
RL   J. Gen. Virol. 79:2565-2572(1998).
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; Y09358; CAA70541.1; -; Genomic_RNA.
DR   SMR; Q9QCE9; -.
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   Gene3D; 1.20.120.1160; -; 1.
DR   InterPro; IPR008609; Ebola_NP.
DR   Pfam; PF05505; Ebola_NP; 1.
DR   PIRSF; PIRSF003900; N_FiloV; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Coiled coil; Helical capsid protein; Host cytoplasm;
KW   Phosphoprotein; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW   Virion.
FT   CHAIN           1..739
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000222173"
FT   REGION          415..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          334..363
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        500..531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..592
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        611..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  83241 MW;  33A96720FFBC638E CRC64;
     MDSRPQKVWM TPSLTESDMD YHKILTAGLS VQQGIVRQRV IPVYQVNNLE EICQLIIQAF
     EAGVDFQESA DSFLLMLCLH HAYQGDYKLF LESGAVKYLE GHGFRFEVKK RDGVKRLEEL
     LPAVSSGKNI KRTLAAMPEE ETTEANAGQF LSFASLFLPK LVVGEKACLR KVQRQIQVHA
     EQGLIQYPTA WQSVGHMMVI FRLMRTNFLI KFLLIHQGMH MVAGHDANDA VISNSVAQAR
     FSGLLIVKTV LDHILQKTQR GVRLHPLART AKVKNEVNSL KAALSSLAKH GEYAPFARLL
     NLSGVNNLEH GLFPQLSAIA LGVATAHGST LAGVNVGEQY QQLREAATEA EKQLQQYAES
     RELDHLGLDD QEKKILMNFH QKKNEISFQQ TNAMVTLKKE RLAKLTEAIT AASLPKTSGH
     YDDDDDIPFP GPINDDDNPG HQDDDPTDSQ DTTIPDVVVD PDDGSYGEYQ SYSENGMNAP
     DDLVLFDLDE DDEDTKPVPN RSTKGGQQKN SQKGQHTEGR QTQSRPTQNI PGPHRTIHHA
     SAPLTDNDRR NEPSGSTSPR MLTPINEEAD PLDDADDETS SLPPLESDDE EQDRDGTSNR
     TPTVAPPAPV YRDHSEKKEL PQDERQDQDH TQEARNQDSD NTQPEHSFEE MYRHILRSQG
     PFDAVLYYHM MKDEPVVFST SDGKEYTYPD SLEEEYPPWL TEKEAMNEEN TFVTLDGQQF
     YWPVMNHKDK FMAILQHHQ
//