ID   NCAP_MABVR              Reviewed;         695 AA.
AC   Q1PDD0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
GN   Name=NP;
OS   Lake Victoria marburgvirus (strain Ravn-87) (MARV) (Marburg virus (strain
OS   Kenya/Ravn/1987)).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX   NCBI_TaxID=378809;
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=16775337; DOI=10.1128/jvi.00069-06;
RA   Towner J.S., Khristova M.L., Sealy T.K., Vincent M.J., Erickson B.R.,
RA   Bawiec D.A., Hartman A.L., Comer J.A., Zaki S.R., Stroeher U.,
RA   Gomes da Silva F., del Castillo F., Rollin P.E., Ksiazek T.G., Nichol S.T.;
RT   "Marburgvirus genomics and association with a large hemorrhagic fever
RT   outbreak in Angola.";
RL   J. Virol. 80:6497-6516(2006).
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 (By similarity).
CC       {ECO:0000250}.
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       {ECO:0000250}.
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the filoviruses nucleoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; DQ447649; ABE27068.1; -; Genomic_RNA.
DR   SMR; Q1PDD0; -.
DR   Proteomes; UP000008239; 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: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   3: Inferred from homology;
KW   Capsid protein; Coiled coil; Helical capsid protein; Host cytoplasm;
KW   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_0000314975"
FT   REGION          426..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          472..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          316..341
FT                   /evidence="ECO:0000255"
FT   COILED          372..400
FT                   /evidence="ECO:0000255"
FT   MOTIF           603..606
FT                   /note="PTAP/PSAP motif"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        496..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   695 AA;  77739 MW;  B0DB92B5FE0E160A CRC64;
     MDLHSLLELG TKPTAPHVRN KKVILFDTNH QVSICNQIID AINSGIDLGD LLEGGLLTLC
     VEHYYNSDKD KFNTSPIAKY LRDAGYEFDV IKNPDATRFL EVIPNEPHYS PLILALKTLE
     STESQRGRIG LFLSFCSLFL PKLVVGDRAS IEKALRQVTV HQEQGIVTYP NHWLTTGHMK
     VIFGILRSSF ILKFVLIHQG VNLVTGHDAY DSIISNSVGQ TRFSGLLIVK TVLEFILQKT
     DSGVALHPLV RTSKVKNEVA SFKQALSNLA RHGEYAPFAR VLNLSGINNL EHGLYPQLSA
     IALGVATAHG STLAGVNVGE QYQQLREAAH DAEVKLQRRH EHQEIQAIAE DDEERKILEQ
     FHLQKTEITH SQTLAVLSQK REKLARLAAE IENNIAEDQG FKQSQNQVSQ SFLNDPTPVE
     VTVQARSINR PTALPPPVDN KIEHETEEDS SSSSSFVDLN DPFALLNEDE DTLENSVMAP
     STTLREPKEV SEPLRQTQDL DISQKKQGNE STDPARKQFL RYQELPPVQE DDESEYTTDS
     QESDDQPGSD NEQGVDLPPP PLYAQEKRQD PIQHPAVSSQ DPFGSIGDVD GDILEPIRSP
     SSPSAPQEDT RMGEAYELSP DFTSYEDNQQ NWPQRVVTKK GRTFLYPNDL LQTSPPESLI
     TALVEEYQNP VSAKELQADW PDMSFDERRH VAMNL