NCAP_JUNIN
ID NCAP_JUNIN Reviewed; 564 AA.
AC P14239;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Junin mammarenavirus (JUNV) (Junn mammarenavirus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Arenaviridae; Mammarenavirus.
OX NCBI_TaxID=2169991;
OH NCBI_TaxID=29095; Akodon azarae (Azara's grass mouse).
OH NCBI_TaxID=10080; Bolomys.
OH NCBI_TaxID=56211; Calomys laucha (Small vesper mouse).
OH NCBI_TaxID=56212; Calomys musculinus (Drylands vesper mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MC2;
RX PubMed=2552421; DOI=10.1093/nar/17.19.8001;
RA Ghiringhelli P.D., Rivera-Pomar R.V., Baro N.I., Rosas M.F., Grau O.,
RA Romanowski V.;
RT "Nucleocapsid protein gene of Junin arenavirus (cDNA sequence).";
RL Nucleic Acids Res. 17:8001-8001(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=MC2;
RX PubMed=1654373; DOI=10.1099/0022-1317-72-9-2129;
RA Ghiringhelli P.D., Rivera-Pomar R.V., Lozano M.E., Grau O., Romanowski V.;
RT "Molecular organization of Junin virus S RNA: complete nucleotide sequence,
RT relationship with other members of the Arenaviridae and unusual secondary
RT structures.";
RL J. Gen. Virol. 72:2129-2141(1991).
RN [3]
RP ZINC BINDING.
RX PubMed=11125165; DOI=10.1099/0022-1317-82-1-121;
RA Tortorici M.A., Ghiringhelli P.D., Lozano M.E., Albarino C.G.,
RA Romanowski V.;
RT "Zinc-binding properties of Junin virus nucleocapsid protein.";
RL J. Gen. Virol. 82:121-128(2001).
RN [4]
RP INTERACTION WITH HOST IKBKE.
RX PubMed=22532683; DOI=10.1128/jvi.00187-12;
RA Pythoud C., Rodrigo W.W., Pasqual G., Rothenberger S., Martinez-Sobrido L.,
RA de la Torre J.C., Kunz S.;
RT "Arenavirus nucleoprotein targets interferon regulatory factor-activating
RT kinase IKKepsilon.";
RL J. Virol. 86:7728-7738(2012).
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 (PubMed:22532683). {ECO:0000255|HAMAP-Rule:MF_04085,
CC ECO:0000269|PubMed:22532683}.
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; X15827; CAA33824.1; -; Genomic_RNA.
DR EMBL; D10072; BAA00965.1; -; Genomic_RNA.
DR PIR; JQ1268; VHXPJV.
DR PIR; S06896; S06896.
DR PIR; S12480; S12480.
DR SMR; P14239; -.
DR PRIDE; P14239; -.
DR Proteomes; UP000127886; Genome.
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 InterPro; IPR012337; RNaseH-like_sf.
DR Pfam; PF17290; Arena_ncap_C; 1.
DR Pfam; PF00843; Arena_nucleocap; 1.
DR PIRSF; PIRSF004029; N_ArenaV; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
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..564
FT /note="Nucleoprotein"
FT /id="PRO_0000079189"
FT REGION 54..236
FT /note="Binding site for the cap structure m7GTP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 380
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 382
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 497
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 500
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT BINDING 529
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
FT SITE 457
FT /note="Important for exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04085"
SQ SEQUENCE 564 AA; 63027 MW; AF7C45E337BD645F CRC64;
MAHSKEVPSF RWTQSLRRGL SQFTQTVKSD VLKDAKLIAD SIDFNQVAQV QRALRKTKRG
EEDLNKLRDL NKEVDRLMSM RSVQRNTVFK AGDLGRVERM ELASGLGNLK TKFRRAETGS
QGVYMGNLSQ SQLAKRSEIL RTLGFQQQGT GGNGVVRVWD VKDPSKLNNQ FGSVPALTIA
CMTVQGGETM NSVIQALTSL GLLYTVKYPN LSDLDRLTQE HDCLQIVTKD ESSINISGYN
FSLSAAVKAG ASILDDGNML ETIRVTPDNF SSLIKSTIQV KRREGMFIDE KPGNRNPYEN
LLYKLCLSGD GWPYIGSRSQ IIGRSWDNTS IDLTRKPVAG PRQPEKNGQN LRLANLTEIQ
EAVIREAVGK LDPTNTLWLD IEGPATDPVE MALFQPAGSK YIHCFRKPHD EKGFKNGSRH
SHGILMKDIE DAMPGVLSYV IGLLPPDMVV TTQGSDDIRK LFDLHGRRDL KLVDVRLTSE
QARQFDQQVW EKFGHLCKHH NGVVVSKKKR DKDAPFKLAS SEPHCALLDC IMFQSVLDGK
LYEEELTPLL PPSLLFLPKA AYAL
