NCAP_MABVM
ID NCAP_MABVM Reviewed; 695 AA.
AC P27588; Q38L45; Q6T6U3; Q6T6V0;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 02-JUN-2021, entry version 94.
DE RecName: Full=Nucleoprotein;
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=NP;
OS Lake Victoria marburgvirus (strain Musoke-80) (MARV) (Marburg virus (strain
OS Kenya/Musoke/1980)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=33727;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9407; Rousettus aegyptiacus (Egyptian rousette) (Egyptian fruit bat).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=1538192; DOI=10.1099/0022-1317-73-2-347;
RA Sanchez A., Kiley M.P., Klenk H.-D., Feldmann H.;
RT "Sequence analysis of the Marburg virus nucleoprotein gene: comparison to
RT Ebola virus and other non-segmented negative-strand RNA viruses.";
RL J. Gen. Virol. 73:347-357(1992).
RN [2]
RP SEQUENCE REVISION.
RA Feldmann H.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
RA Chain P.S.G., Malfatti S.A., Hajjaj A., Vergez L.M., Do L.H., Smith K.L.,
RA McCready P.M.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=pp3/guinea pig lethal, and pp4/guinea pig nonlethal;
RA Ichou M.A., Paragas J., Jahrling P.B., Ibrahim M.S., Lofts L., Hevey M.,
RA Schmaljohn A.;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Enterlein;
RX PubMed=16379005; DOI=10.1128/jvi.80.2.1038-1043.2006;
RA Enterlein S., Volchkov V., Weik M., Kolesnikova L., Volchkova V.,
RA Klenk H.-D., Muehlberger E.;
RT "Rescue of recombinant Marburg virus from cDNA is dependent on nucleocapsid
RT protein VP30.";
RL J. Virol. 80:1038-1043(2006).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=8151297; DOI=10.1099/0022-1317-75-4-809;
RA Becker S., Huppertz S., Klenk H.-D., Feldmann H.;
RT "The nucleoprotein of Marburg virus is phosphorylated.";
RL J. Gen. Virol. 75:809-818(1994).
RN [7]
RP INTERACTION WITH VP24.
RX PubMed=16227263; DOI=10.1128/jvi.79.21.13421-13433.2005;
RA Bamberg S., Kolesnikova L., Moeller P., Klenk H.-D., Becker S.;
RT "VP24 of Marburg virus influences formation of infectious particles.";
RL J. Virol. 79:13421-13433(2005).
RN [8]
RP INTERACTION WITH VP35, AND COILED-COIL DOMAIN.
RX PubMed=17958906; DOI=10.1186/1743-422x-4-105;
RA Dicarlo A., Moeller P., Lander A., Kolesnikova L., Becker S.;
RT "Nucleocapsid formation and RNA synthesis of Marburg virus is dependent on
RT two coiled coil motifs in the nucleoprotein.";
RL Virol. J. 4:105-105(2007).
RN [9]
RP LATE-BUDDING DOMAIN.
RX PubMed=20504928; DOI=10.1128/jvi.00476-10;
RA Dolnik O., Kolesnikova L., Stevermann L., Becker S.;
RT "Tsg101 is recruited by a late domain of the nucleocapsid protein to
RT support budding of Marburg virus-like particles.";
RL J. Virol. 84:7847-7856(2010).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC encapsidated genomic RNA is termed the nucleocapsid and serves as
CC template for transcription and replication. During replication,
CC encapsidation by NP is coupled to RNA synthesis and all replicative
CC products are resistant to nucleases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer. Homomultimerizes to form the nucleocapsid. Binds
CC to viral genomic RNA. Interacts with VP35 and VP30 to form the
CC nucleocapsid. Also interacts with VP24 and VP40 (Probable).
CC {ECO:0000305|PubMed:16227263, ECO:0000305|PubMed:17958906}.
CC -!- SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000250}.
CC -!- DOMAIN: This protein can be divided into a hydrophobic N-terminal half,
CC and a hydrophilic and highly acidic C-terminal half. {ECO:0000250}.
CC -!- DOMAIN: The coiled coil region is critical for homooligomerization, for
CC the interaction with VP35 and for NP function in RNA synthesis.
CC -!- DOMAIN: Late-budding domains (L domains) are short sequence motifs
CC essential for viral particle budding. They recruit proteins of the host
CC ESCRT machinery (Endosomal Sorting Complex Required for Transport) or
CC ESCRT-associated proteins. Nucleoprotein contains one L domain: a
CC PTAP/PSAP motif, which interacts with the UEV domain of TSG101.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:8151297}.
CC -!- SIMILARITY: Belongs to the filoviruses nucleoprotein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA78114.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M72714; AAA46563.1; -; Genomic_RNA.
DR EMBL; Z12132; CAA78114.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY430365; AAR85460.1; -; Genomic_RNA.
DR EMBL; AY430366; AAR85453.1; -; Genomic_RNA.
DR EMBL; DQ217792; ABA87124.1; -; Genomic_RNA.
DR PIR; JQ1408; VHIWMV.
DR RefSeq; YP_001531153.1; NC_001608.3.
DR PDB; 4W2O; X-ray; 3.20 A; B/D/F/H=601-695.
DR PDB; 4W2Q; X-ray; 2.70 A; B/D/F/H=632-695.
DR PDB; 5T3W; X-ray; 3.25 A; A/B/C/D/E/F/G/H=552-579.
DR PDB; 6APP; X-ray; 1.75 A; B=601-695.
DR PDBsum; 4W2O; -.
DR PDBsum; 4W2Q; -.
DR PDBsum; 5T3W; -.
DR PDBsum; 6APP; -.
DR SMR; P27588; -.
DR ELM; P27588; -.
DR ABCD; P27588; 3 sequenced antibodies.
DR DNASU; 920944; -.
DR GeneID; 920944; -.
DR KEGG; vg:920944; -.
DR Proteomes; UP000007771; Genome.
DR Proteomes; UP000137266; Genome.
DR Proteomes; UP000160614; Genome.
DR Proteomes; UP000180448; 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:0039702; P:viral budding via host ESCRT complex; 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; Host-virus interaction; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Viral budding;
KW Viral budding via the host ESCRT complexes; Viral nucleoprotein;
KW Viral release from host cell; Virion.
FT CHAIN 1..695
FT /note="Nucleoprotein"
FT /id="PRO_0000222175"
FT REGION 424..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 316..341
FT /evidence="ECO:0000255"
FT COILED 372..399
FT /evidence="ECO:0000255"
FT MOTIF 603..606
FT /note="PTAP/PSAP motif"
FT COMPBIAS 477..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 77
FT /note="V -> I (in strain: pp3/guinea pig lethal, pp4/guinea
FT pig nonlethal and Isolate Enterlein)"
FT VARIANT 103
FT /note="S -> I (in strain: pp3/guinea pig lethal, pp4/guinea
FT pig nonlethal and Isolate Enterlein)"
FT VARIANT 514
FT /note="R -> P (in strain: pp3/guinea pig lethal, pp4/guinea
FT pig nonlethal and Isolate Enterlein)"
FT VARIANT 611
FT /note="R -> K (in strain: pp4/guinea pig nonlethal)"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:6APP"
FT STRAND 643..646
FT /evidence="ECO:0007829|PDB:6APP"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:6APP"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6APP"
FT HELIX 657..665
FT /evidence="ECO:0007829|PDB:6APP"
FT HELIX 670..679
FT /evidence="ECO:0007829|PDB:6APP"
FT HELIX 680..682
FT /evidence="ECO:0007829|PDB:6APP"
FT HELIX 685..694
FT /evidence="ECO:0007829|PDB:6APP"
SQ SEQUENCE 695 AA; 77862 MW; A48BDB59731C6D73 CRC64;
MDLHSLLELG TKPTAPHVRN KKVILFDTNH QVSICNQIID AINSGIDLGD LLEGGLLTLC
VEHYYNSDKD KFNTSPVAKY LRDAGYEFDV IKNADATRFL DVSPNEPHYS PLILALKTLE
STESQRGRIG LFLSFCSLFL PKLVVGDRAS IEKALRQVTV HQEQGIVTYP NHWLTTGHMK
VIFGILRSSF ILKFVLIHQG VNLVTGHDAY DSIISNSVGQ TRFSGLLIVK TVLEFILQKT
DSGVTLHPLV RTSKVKNEVA SFKQALSNLA RHGEYAPFAR VLNLSGINNL EHGLYPQLSA
IALGVATAHG STLAGVNVGE QYQQLREAAH DAEVKLQRRH EHQEIQAIAE DDEERKILEQ
FHLQKTEITH SQTLAVLSQK REKLARLAAE IENNIVEDQG FKQSQNRVSQ SFLNDPTPVE
VTVQARPMNR PTALPPPVDD KIEHESTEDS SSSSSFVDLN DPFALLNEDE DTLDDSVMIP
GTTSREFQGI PEPPRQSQDL NNSQGKQEDE STNRIKKQFL RYQELPPVQE DDESEYTTDS
QESIDQPGSD NEQGVDLPPP PLYAQEKRQD PIQHPAANPQ DPFGSIGDVN GDILEPIRSP
SSPSAPQEDT RMREAYELSP DFTNDEDNQQ NWPQRVVTKK GRTFLYPNDL LQTNPPESLI
TALVEEYQNP VSAKELQADW PDMSFDERRH VAMNL
