ID   NCAP_EBORE              Reviewed;         739 AA.
AC   Q91DE1;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=Protein N;
DE   AltName: Full=Reston NP {ECO:0000303|PubMed:12825739};
DE            Short=rNP {ECO:0000303|PubMed:12825739};
GN   Name=NP;
OS   Reston ebolavirus (strain Philippines-96) (REBOV) (Reston Ebola virus).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Orthoebolavirus;
OC   Orthoebolavirus restonense; Reston ebolavirus.
OX   NCBI_TaxID=129003;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=77225; Pteropodinae.
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=11722021; DOI=10.1007/s007050170049;
RA   Ikegami T., Calaor A.B., Miranda M.E., Niikura M., Saijo M., Kurane I.,
RA   Yoshikawa Y., Morikawa S.;
RT   "Genome structure of Ebola virus subtype Reston: differences among Ebola
RT   subtypes.";
RL   Arch. Virol. 146:2021-2027(2001).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=12825739; DOI=10.1017/s0950268803008264;
RA   Ikegami T., Saijo M., Niikura M., Miranda M.E., Calaor A.B., Hernandez M.,
RA   Manalo D.L., Kurane I., Yoshikawa Y., Morikawa S.;
RT   "Immunoglobulin G enzyme-linked immunosorbent assay using truncated
RT   nucleoproteins of Reston Ebola virus.";
RL   Epidemiol. Infect. 130:533-539(2003).
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; AB050936; BAB69003.1; -; Genomic_RNA.
DR   SMR; Q91DE1; -.
DR   Proteomes; UP000002322; Genome.
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   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_0000245051"
FT   REGION          414..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          498..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          334..363
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        506..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..642
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  83463 MW;  7F7C5A73168700F2 CRC64;
     MDRGTRRIWV SQNQGDTDLD YHKILTAGLT VQQGIVRQKI ISVYLVDNLE AMCQLVIQAF
     EAGIDFQENA DSFLLMLCLH HAYQGDYKLF LESNAVQYLE GHGFKFELRK KDGVNRLEEL
     LPAATSGKNI RRTLAALPEE ETTEANAGQF LSFASLFLPK LVVGEKACLE KVQRQIQVHA
     EQGLIQYPTA WQSVGHMMVI FRLMRTNFLI KYLLIHQGMH MVAGHDANDA VIANSVAQAR
     FSGLLIVKTV LDHILQKTDQ GVRLHPLART AKVRNEVNAF KAALSSLAKH GEYAPFARLL
     NLSGVNNLEH GLYPQLSAIA LGVATAHGST LAGVNVGEQY QQLREAATEA EKQLQQYAES
     RELDSLGLDD QERRILMNFH QKKNEISFQQ TNAMVTLRKE RLAKLTEAIT LASRPNLGSR
     QDDDNEIPFP GPISNNPDQD HLEDDPRDSR DTIIPNSAID PEDGDFENYN GYHDDEVGTA
     GDLVLFDLDD HEDDNKAFEL QDSSPQSQRE IERERLIHPP PGNNKDDNRA SDNNQQSADS
     EEQEGQYNRH RGPERTTANR RLSPVHEEDT PIDQGDDDPS SPPPLESDDD DASSSQQDPD
     YTAVAPPAPV YRSAEAHEPP HKSSNEPAET SQLNEDPDIG QSKSMQKLGE TYHHLLRTQG
     PFEAINYYHM MKDEPVIFST DDGKEYTYPD SLEEAYPPWL TEKERLDNEN RYIYINNQQF
     FWPVMSPRDK FLAILQHHQ
//