NCAP_MABVA
ID NCAP_MABVA Reviewed; 695 AA.
AC Q1PD53;
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 Angola/2005) (MARV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC Monjiviricetes; Mononegavirales; Filoviridae; Marburgvirus.
OX NCBI_TaxID=378830;
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].
RC STRAIN=Isolate Ang0126, Isolate Ang0215, Isolate Ang0754, Isolate Ang0998,
RC Isolate Ang1379c, Isolate Ang1381, and Isolate Ang1386;
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; DQ447653; ABE27012.1; -; Genomic_RNA.
DR EMBL; DQ447654; ABE27019.1; -; Genomic_RNA.
DR EMBL; DQ447655; ABE27026.1; -; Genomic_RNA.
DR EMBL; DQ447656; ABE27033.1; -; Genomic_RNA.
DR EMBL; DQ447658; ABE27047.1; -; Genomic_RNA.
DR EMBL; DQ447659; ABE27054.1; -; Genomic_RNA.
DR EMBL; DQ447660; ABE27061.1; -; Genomic_RNA.
DR PDB; 7F1M; EM; 3.10 A; A/B=1-395.
DR PDBsum; 7F1M; -.
DR SMR; Q1PD53; -.
DR Proteomes; UP000008242; Genome.
DR Proteomes; UP000097432; Genome.
DR Proteomes; UP000102513; Genome.
DR Proteomes; UP000109618; Genome.
DR Proteomes; UP000115353; Genome.
DR Proteomes; UP000168007; Genome.
DR Proteomes; UP000171838; 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 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Coiled coil; Helical capsid protein;
KW Host cytoplasm; Host-virus interaction; Phosphoprotein; Ribonucleoprotein;
KW RNA-binding; Viral budding; Viral budding via the host ESCRT complexes;
KW Viral nucleoprotein; Viral release from host cell; Virion.
FT CHAIN 1..695
FT /note="Nucleoprotein"
FT /id="PRO_0000314973"
FT REGION 423..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..612
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 /evidence="ECO:0000250"
FT COMPBIAS 483..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 77792 MW; F2B1446F1A37727E CRC64;
MDLHSLLELG TKPTAPHVRN KKVILFDTNH QVSICNQIID AINSGIDLGD LLEGGLLTLC
VEHYYNSDKD KFNTSPIAKY LRDAGYEFDV IKNADATRFL DVIPNEPHYS 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
VTVQARPINR PTALPPPVDS KIEHESTEDS SSSSSFVDLN DPFALLNEDE DTLDDSVMIP
STTSREFQGI PEPPRQSQDI DNSQGKQEDE STNLIKKPFL RYQELPPVQE DDESEYTTDS
QESIDQPGSD NEQGVDLPPP PLYAQEKRQD PIQHPAVSSQ DPFGSIGDVN GDILEPIRSP
SSPSAPQEDT RAREAYELSP DFTNYEDNQQ NWPQRVVTKK GRTFLYPNDL LQTNPPESLI
TALVEEYQNP VSAKELQADW PDMSFDERRH VAMNL
