NCAP_EBOG4
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 29-SEP-2021, entry version 61.
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; Ebolavirus.
OX NCBI_TaxID=128947;
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 [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. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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: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_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
