NCAP_EBOSB
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 29-SEP-2021, entry version 64.
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; Ebolavirus.
OX NCBI_TaxID=128948;
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).
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. {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: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
