NCAP_LASSG
ID NCAP_LASSG Reviewed; 570 AA.
AC P04935;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04085};
DE EC=3.1.13.- {ECO:0000255|HAMAP-Rule:MF_04085};
DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04085};
DE AltName: Full=Protein N {ECO:0000255|HAMAP-Rule:MF_04085};
GN Name=N {ECO:0000255|HAMAP-Rule:MF_04085};
OS Lassa virus (strain GA391) (LASV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=11621;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=10112; Mastomys natalensis (African soft-furred rat) (Praomys natalensis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3840620; DOI=10.1016/0042-6822(85)90278-8;
RA Clegg J.C.S., Oram J.D.;
RT "Molecular cloning of Lassa virus RNA: nucleotide sequence and expression
RT of the nucleocapsid protein gene.";
RL Virology 144:363-372(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2042397; DOI=10.1016/0168-1702(91)90015-n;
RA Clegg J.C.S., Wilson S.M., Oram J.D.;
RT "Nucleotide sequence of the S RNA of Lassa virus (Nigerian strain) and
RT comparative analysis of arenavirus gene products.";
RL Virus Res. 18:151-164(1991).
CC -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC encapsidated genomic RNA is termed the nucleocapsid (NC). Serves as
CC template for viral transcription and replication. The increased
CC presence of protein N in host cell does not seem to trigger the switch
CC from transcription to replication as observed in other negative strain
CC RNA viruses. Through the interaction with host IKBKE, strongly inhibits
CC the phosphorylation and nuclear translocation of host IRF3, a protein
CC involved in interferon activation pathway, leading to the inhibition of
CC interferon-beta and IRF3-dependent promoters activation. Encodes also a
CC functional 3'-5' exoribonuclease that degrades preferentially dsRNA
CC substrates and thereby participates in the suppression of interferon
CC induction. {ECO:0000255|HAMAP-Rule:MF_04085}.
CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC genomic RNA. Interacts with glycoprotein G2. Interacts with protein Z;
CC this interaction probably directs the encapsidated genome to budding
CC sites. Interacts with protein L; this interaction does not interfere
CC with Z-L interaction. Interacts with host IKBKE (via Protein kinase
CC domain); the interaction inhibits IKBKE kinase activity.
CC {ECO:0000255|HAMAP-Rule:MF_04085}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04085}. Host
CC cytoplasm {ECO:0000255|HAMAP-Rule:MF_04085}.
CC -!- DOMAIN: The N-terminal region is important for the cap-binding activity
CC while the C-terminal region contains the 3'-5' exoribonuclease
CC activity. A CCHE zinc binding site is present in the C-terminal region
CC and may thus contribute to the substrate binding and/or the specificity
CC of the exonuclease activity. {ECO:0000255|HAMAP-Rule:MF_04085}.
CC -!- SIMILARITY: Belongs to the arenaviridae nucleocapsid protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04085}.
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DR EMBL; X52400; CAA36646.1; ALT_SEQ; Genomic_RNA.
DR EMBL; K03362; AAA46284.1; -; Genomic_RNA.
DR PIR; B43492; VHXPL2.
DR SMR; P04935; -.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039689; P:negative stranded viral RNA replication; ISS:UniProtKB.
DR GO; GO:0039696; P:RNA-templated viral transcription; ISS:UniProtKB.
DR GO; GO:0039724; P:suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.410; -; 1.
DR HAMAP; MF_04085; ARENA_NCAP; 1.
DR InterPro; IPR000229; Nucleocapsid_arenaviridae.
DR InterPro; IPR035084; Nucleocapsid_C_arenaviridae.
DR InterPro; IPR038115; Nucleocapsid_C_sf.
DR InterPro; IPR035083; Nucleocapsid_N_arenaviridae.
DR Pfam; PF17290; Arena_ncap_C; 1.
DR Pfam; PF00843; Arena_nucleocap; 1.
DR PIRSF; PIRSF004029; N_ArenaV; 1.
PE 3: Inferred from homology;
KW Capsid protein; Helical capsid protein; Host cytoplasm;
KW Host-virus interaction; Hydrolase; Inhibition of host IKBKE by virus;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host RLR pathway by virus;
KW Interferon antiviral system evasion; Manganese; Metal-binding;
KW Ribonucleoprotein; RNA-binding; Viral immunoevasion; Viral nucleoprotein;
KW Virion; Zinc.
FT CHAIN 1..570
FT /note="Nucleoprotein"
FT /id="PRO_0000079191"
FT REGION 54..241
FT /note="Binding site for the cap structure m7GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 390
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 392
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 507
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 530
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 534
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT SITE 467
FT /note="Important for exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
SQ SEQUENCE 570 AA; 62913 MW; AEF39AD598A8C88D CRC64;
MSASKEVRSC LWTQSLRREL SGYCSNIKLQ VVKDAQALLH GLDFSEVSNV QRLMRKQKRD
DGDLKRLRDL NQAVNNLVEL KSTQQKSVLR VGTLSSDDLL ILAADLEKLK SKVTRTERPL
SSGVYMGNLS SQQLDQRRAL LNMIGMTGVS GGGKGASNGI VRVWDVKNAE LLNNQFGTMP
SLTLACLTKQ GQVDLNDAVQ ALTDLGLIYT AKYPNSSDLD RLSQSHPILN MIDTKKSSLN
ISGYNFSLGA AVKAGACMLD GGNMLETIKV SPQTMDGILK SILKVKKSLG MFVSDTPGER
NPYENILYKI CLSGDGWSYI ASRTSIVGRA WENTVVDLEQ DNKPQKIGNG GSNKSLQSAG
FAAGLIYSQL MTLKDFKCFN LIPNAKTWMD IEGRPEDPVE IALYQPSSGC YVHFFREPTD
LKQFKQDAKY SHGRDVTDLF AAQPGLTSAV IEALPRNMVI TCQGSEDIRK LLESQGRRDI
KLIDITLSKA DSRKFENAVW DQFKDLCHMH TGVVVEKKKR GGKEEITPHC ALMDCIMFDA
AVSGGLDAKV LRVVLPRDMV FRTSTPKVVL
