NCAP_EBORR
ID NCAP_EBORR Reviewed; 739 AA.
AC Q8JPY1; Q5UAL1;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
DE AltName: Full=Reston NP;
DE Short=rNP;
GN Name=NP;
OS Reston ebolavirus (strain Reston-89) (REBOV) (Reston Ebola virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Ebolavirus.
OX NCBI_TaxID=386032;
OH NCBI_TaxID=77231; Epomops franqueti (Franquet's epauleted fruit bat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=77243; Myonycteris torquata (Little collared fruit bat).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12191779; DOI=10.1016/s0168-1702(02)00087-4;
RA Groseth A., Stroeher U., Theriault S., Feldmann H.;
RT "Molecular characterization of an isolate from the 1989/90 epizootic of
RT Ebola virus Reston among macaques imported into the United States.";
RL Virus Res. 87:155-163(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Pennsylvania-89;
RX PubMed=15661171; DOI=10.1016/j.virol.2004.11.018;
RA Boehmann Y., Enterlein S., Randolf A., Muehlberger E.I.;
RT "A reconstituted replication and transcription system for Ebola virus
RT Reston and comparison with Ebola virus Zaire.";
RL Virology 332:406-417(2005).
RN [3] {ECO:0007744|PDB:5W2B}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 641-739.
RA Radwanska M.J., Derewenda U., Kossiakoff A.A., Derewenda Z.S.;
RT "Crystal structure of C-terminal domain of Ebola (Reston) nucleoprotein in
RT complex with Fab fragment.";
RL Submitted (JUN-2017) to the PDB data bank.
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; AF522874; AAN04448.1; -; Genomic_RNA.
DR EMBL; AY769362; AAV48574.1; -; Genomic_RNA.
DR RefSeq; NP_690580.1; NC_004161.1.
DR PDB; 5W2B; X-ray; 2.25 A; A=641-739.
DR PDBsum; 5W2B; -.
DR SMR; Q8JPY1; -.
DR ABCD; Q8JPY1; 2 sequenced antibodies.
DR GeneID; 955194; -.
DR KEGG; vg:955194; -.
DR Proteomes; UP000007207; Genome.
DR Proteomes; UP000138664; 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; IDA:CACAO.
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..739
FT /note="Nucleoprotein"
FT /id="PRO_0000245052"
FT REGION 414..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..641
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..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 28
FT /note="G -> V (in strain: Isolate Pennsylvania-89)"
FT VARIANT 67
FT /note="Q -> R (in strain: Isolate Pennsylvania-89)"
FT VARIANT 373
FT /note="R -> G (in strain: Isolate Pennsylvania-89)"
FT VARIANT 483
FT /note="L -> W (in strain: Isolate Pennsylvania-89)"
FT VARIANT 517
FT /note="I -> T (in strain: Isolate Pennsylvania-89)"
FT VARIANT 721
FT /note="F -> S (in strain: Isolate Pennsylvania-89)"
FT HELIX 645..658
FT /evidence="ECO:0007829|PDB:5W2B"
FT HELIX 661..672
FT /evidence="ECO:0007829|PDB:5W2B"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:5W2B"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:5W2B"
FT HELIX 690..692
FT /evidence="ECO:0007829|PDB:5W2B"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:5W2B"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:5W2B"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:5W2B"
FT STRAND 712..715
FT /evidence="ECO:0007829|PDB:5W2B"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:5W2B"
FT HELIX 722..724
FT /evidence="ECO:0007829|PDB:5W2B"
FT HELIX 727..737
FT /evidence="ECO:0007829|PDB:5W2B"
SQ SEQUENCE 739 AA; 83453 MW; AB1BFE0970BB2A86 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
QDDGNEIPFP GPISNNPDQD HLEDDPRDSR DTIIPNGAID PEDGDFENYN GYHDDEVGTA
GDLVLFDLDD HEDDNKAFEP QDSSPQSQRE IERERLIHPP PGNNKDDNRA SDNNQQSADS
EEQGGQYNWH RGPERTTANR RLSPVHEEDT LMDQGDDDPS SLPPLESDDD DASSSQQDPD
YTAVAPPAPV YRSAEAHEPP HKSSNEPAET SQLNEDPDIG QSKSMQKLEE TYHHLLRTQG
PFEAINYYHM MKDEPVIFST DDGKEYTYPD SLEEAYPPWL TEKERLDKEN RYIYINNQQF
FWPVMSPRDK FLAILQHHQ
