NCAP_TULV
ID NCAP_TULV Reviewed; 429 AA.
AC Q88918;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Nucleoprotein;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q89462};
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Tula orthohantavirus (TULV) (Tula virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980494;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=47230; Microtus arvalis (Common vole) (Field vole).
OH NCBI_TaxID=523745; Microtus obscurus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Tula/Moravia/5302Ma/94;
RX PubMed=8837887; DOI=10.1016/0168-1702(95)00086-0;
RA Plyusnin A., Cheng Y., Vapalahti O., Pejcoch M., Unar J., Jelinkova Z.,
RA Lehvaeslaiho H., Lundkvist A., Vaheri A.;
RT "Genetic variation in Tula hantaviruses: sequence analysis of the S and M
RT segments of strains from Central Europe.";
RL Virus Res. 39:237-250(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Tula/Moravia/5302v/95;
RX PubMed=9000098; DOI=10.1099/0022-1317-77-12-3063;
RA Vapalahti O., Lundkvist A., Kukkonen S.K., Cheng Y., Gilljam M.,
RA Kanerva M., Manni T., Pejcoch M., Niemimaa J., Kaikusalo A., Henttonen H.,
RA Vaheri A., Plyusnin A.;
RT "Isolation and characterization of Tula virus, a distinct serotype in the
RT genus Hantavirus, family Bunyaviridae.";
RL J. Gen. Virol. 77:3063-3067(1996).
RN [3]
RP SUBUNIT.
RX PubMed=14512541; DOI=10.1128/jvi.77.20.10910-10916.2003;
RA Kaukinen P., Vaheri A., Plyusnin A.;
RT "Mapping of the regions involved in homotypic interactions of Tula
RT hantavirus N protein.";
RL J. Virol. 77:10910-10916(2003).
RN [4]
RP INTERACTION WITH HOST SUMO1, AND SUBCELLULAR LOCATION.
RX PubMed=12606074; DOI=10.1016/s0168-1702(02)00312-x;
RA Kaukinen P., Vaheri A., Plyusnin A.;
RT "Non-covalent interaction between nucleocapsid protein of Tula hantavirus
RT and small ubiquitin-related modifier-1, SUMO-1.";
RL Virus Res. 92:37-45(2003).
RN [5]
RP SUBUNIT.
RX PubMed=15564476; DOI=10.1128/jvi.78.24.13669-13677.2004;
RA Kaukinen P., Kumar V., Tulimaeki K., Engelhardt P., Vaheri A., Plyusnin A.;
RT "Oligomerization of Hantavirus N protein: C-terminal alpha-helices interact
RT to form a shared hydrophobic space.";
RL J. Virol. 78:13669-13677(2004).
RN [6]
RP SUBUNIT, AND DOMAIN.
RX PubMed=16940519; DOI=10.1128/jvi.00515-06;
RA Alminaite A., Halttunen V., Kumar V., Vaheri A., Holm L., Plyusnin A.;
RT "Oligomerization of hantavirus nucleocapsid protein: analysis of the N-
RT terminal coiled-coil domain.";
RL J. Virol. 80:9073-9081(2006).
RN [7]
RP DOMAIN, COILED COIL, AND SUBUNIT.
RX PubMed=18753226; DOI=10.1099/vir.0.2008/004044-0;
RA Alminaite A., Backstroem V., Vaheri A., Plyusnin A.;
RT "Oligomerization of hantaviral nucleocapsid protein: charged residues in
RT the N-terminal coiled-coil domain contribute to intermolecular
RT interactions.";
RL J. Gen. Virol. 89:2167-2174(2008).
RN [8]
RP INTERACTION WITH GYCOPROTEIN N, AND DOMAIN.
RC STRAIN=Moravia;
RX PubMed=20566401; DOI=10.1016/j.virusres.2010.05.008;
RA Wang H., Alminaite A., Vaheri A., Plyusnin A.;
RT "Interaction between hantaviral nucleocapsid protein and the cytoplasmic
RT tail of surface glycoprotein Gn.";
RL Virus Res. 151:205-212(2010).
RN [9]
RP FUNCTION.
RX PubMed=33478127; DOI=10.3390/v13010140;
RA Gallo G., Caignard G., Badonnel K., Chevreux G., Terrier S., Szemiel A.,
RA Roman-Sosa G., Binder F., Gu Q., Da Silva Filipe A., Ulrich R.G., Kohl A.,
RA Vitour D., Tordo N., Ermonval M.;
RT "Interactions of Viral Proteins from Pathogenic and Low or Non-Pathogenic
RT Orthohantaviruses with Human Type I Interferon Signaling.";
RL Viruses 13:0-0(2021).
CC -!- FUNCTION: Encapsidates the genome protecting it from nucleases
CC (Probable). The encapsidated genomic RNA is termed the nucleocapsid
CC (NC) and serves as template for transcription and replication
CC (Probable). The nucleocapsid has a left-handed helical structure (By
CC similarity). As a trimer, specifically binds and acts as a chaperone to
CC unwind the panhandle structure formed by the viral RNA (vRNA) termini
CC (By similarity). Involved in the transcription and replication
CC initiation of vRNA by mediating primer annealing (By similarity). Plays
CC a role in cap snatching by sequestering capped RNAs in P bodies for use
CC by the viral RdRp during transcription initiation (By similarity).
CC Substitutes for the cellular cap-binding complex (eIF4F) to
CC preferentially facilitate the translation of capped mRNAs (By
CC similarity). Initiates the translation by specifically binding to the
CC cap and 40S ribosomal subunit (By similarity). Prevents the viral
CC glycoprotein N (Gn) from autophagy-dependent breakdown maybe by
CC blocking autophagosome formation (By similarity). Inhibits host
CC EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown
CC in cells and thus the activation of the antiviral state (By
CC similarity). Also displays sequence-unspecific DNA endonuclease
CC activity (By similarity). Inhibits the IFN signaling response directed
CC by the dsRNA sensor DDX58/RIG-I (PubMed:33478127).
CC {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:P05133,
CC ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:33478127,
CC ECO:0000305}.
CC -!- SUBUNIT: Homotrimer (PubMed:15564476, PubMed:16940519). Homomultimer
CC (PubMed:14512541, PubMed:18753226, PubMed:15564476). Homomultimerizes
CC and binds to viral genomic RNA to form the nucleocapsid (By
CC similarity). Interacts with host MAP1LC3B; this interaction
CC participates to the protection of Gn from virus-triggered autophagy (By
CC similarity). Interacts with host SNAP29; this interaction participates
CC to the protection of glycoprotein N from virus-triggered autophagy (By
CC similarity). Interacts (via N-terminus) with host RPS19; this
CC interaction probably mediates the loading of the 40S ribosomal subunit
CC on viral capped mRNA during N-mediated translation initiation (By
CC similarity). Interacts with the viral RdRp (By similarity). Interacts
CC with host SUMO1 (via N-terminus) (PubMed:12606074). Interacts with host
CC DAXX (By similarity). Interacts with the viral glycoprotein N (via C-
CC terminus) (PubMed:20566401). Interacts with the viral glycoprotein C
CC (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P05133,
CC ECO:0000250|UniProtKB:P27313, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000269|PubMed:12606074, ECO:0000269|PubMed:14512541,
CC ECO:0000269|PubMed:15564476, ECO:0000269|PubMed:16940519,
CC ECO:0000269|PubMed:18753226, ECO:0000269|PubMed:20566401}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:12606074}. Host Golgi apparatus,
CC host cis-Golgi network {ECO:0000250|UniProtKB:P05133}. Note=Internal
CC protein of virus particle. {ECO:0000305}.
CC -!- DOMAIN: The N-terminus is required for chaperone activity and, in
CC trimeric form, this region likely serves in high affinity vRNA
CC panhandle recognition (By similarity). The N-terminus also contains a
CC coiled coil region, which probably participates in but is insufficient
CC to initiate N trimerization (PubMed:18753226, PubMed:16940519). The
CC YxxL motif is indispensable for the interaction with host MAP1LC3B (By
CC similarity). The central region is involved in specific RNA-binding (By
CC similarity). Has distinct cap- and RNA-binding sites so it can bind
CC simultaneously both the vRNA and mRNA cap (By similarity).
CC {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000269|PubMed:16940519, ECO:0000269|PubMed:18753226}.
CC -!- SIMILARITY: Belongs to the hantavirus nucleocapsid protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z49915; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR EMBL; Z69991; CAA93823.1; -; Genomic_RNA.
DR Proteomes; UP000243699; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR InterPro; IPR002214; Hanta_nucleocap.
DR Pfam; PF00846; Hanta_nucleocap; 1.
DR PIRSF; PIRSF003949; N_HantaV; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Endonuclease; Host cytoplasm; Host Golgi apparatus;
KW Hydrolase; Nuclease; Ribonucleoprotein; RNA-binding; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..429
FT /note="Nucleoprotein"
FT /id="PRO_0000455188"
FT REGION 1..175
FT /note="Viral panhandle binding"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 1..100
FT /note="Chaperone activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 1..79
FT /note="Homomultimerization"
FT /evidence="ECO:0000269|PubMed:14512541,
FT ECO:0000269|PubMed:18753226, ECO:0000305|PubMed:16940519"
FT REGION 1..50
FT /note="RdRP binding"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 80..248
FT /note="Interaction with glycoprotein N"
FT /evidence="ECO:0000269|PubMed:20566401"
FT REGION 100..125
FT /note="Homomultimerization"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 150..175
FT /note="Interaction with host RPS19"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 175..217
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 188..191
FT /note="Interaction with host UBE2I/UBC9"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 373..429
FT /note="Interaction with host DAXX"
FT /evidence="ECO:0000250|UniProtKB:P27313"
FT REGION 373..421
FT /note="Homomultimerization"
FT /evidence="ECO:0000269|PubMed:14512541,
FT ECO:0000269|PubMed:15564476, ECO:0000305|PubMed:16940519"
FT COILED 4..71
FT /evidence="ECO:0000305|PubMed:18753226"
FT MOTIF 178..181
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT SITE 88
FT /note="Important for the endonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT SITE 103
FT /note="Important for the endonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
SQ SEQUENCE 429 AA; 48556 MW; 098DEDDDE2859B0F CRC64;
MSQLKEIQEE ITRHEQQIVI ARQKLKDVEK TVEADPDDVN KSTLQSRRAA VSALEDKLAD
FKRQLADLVS SQKMGEKPVD PTGLEPDDHL KERSSLRYGN VLDVNAIDID EPSGQTADWF
SIGQYITGFA LAIILKALYM LSTRGRQTIK ENKGTRIRFK DDSSYEEING IRRPKHLYVS
MPTAQSTMKA DELTPGRFRT IVCGLFPAQI MYRNIISPVM GVIGFSFFVK DWPEKIEEFL
IKPCPFLKKS GPSKEEDFLV SNDAYLLGRE KALRESHLAE IDDLIDLAAS GDPTPPDSIK
SPQAPWVFAC RPDRCPPTCI YIAGMAELGA FFSILQDMRN TIMASKTVGT AEEKLKKKSS
FYQSYLRRTQ SMGIQLDQRI ILLFMTEWGS DIVNHFHLGD DMDPELRTLA QSLIDQKVKE
ISNQEPLKI
