NCAP_EBORE
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 23-FEB-2022, entry version 71.
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; 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. {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: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
