NCAP_HANTV
ID NCAP_HANTV Reviewed; 429 AA.
AC P05133;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 89.
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 Hantaan virus (strain 76-118) (Korean hemorrhagic fever virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=11602;
OH NCBI_TaxID=39030; Apodemus agrarius (Eurasian field mouse).
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3024404; DOI=10.1016/0042-6822(86)90223-0;
RA Schmaljohn C.S., Jennings G.B., Hay J., Dalrymple J.M.;
RT "Coding strategy of the S genome segment of Hantaan virus.";
RL Virology 155:633-643(1986).
RN [2]
RP DOMAIN, AND RNA-BINDING.
RX PubMed=11884555; DOI=10.1128/jvi.76.7.3301-3308.2002;
RA Xu X., Severson W., Villegas N., Schmaljohn C.S., Jonsson C.B.;
RT "The RNA binding domain of the hantaan virus N protein maps to a central,
RT conserved region.";
RL J. Virol. 76:3301-3308(2002).
RN [3]
RP SUBUNIT.
RX PubMed=12502810; DOI=10.1128/jvi.77.2.943-952.2003;
RA Yoshimatsu K., Lee B.H., Araki K., Morimatsu M., Ogino M., Ebihara H.,
RA Arikawa J.;
RT "The multimerization of hantavirus nucleocapsid protein depends on type-
RT specific epitopes.";
RL J. Virol. 77:943-952(2003).
RN [4]
RP INTERACTION WITH HOST HIPK2, INTERACTION WITH HOST CHD3, AND INTERACTION
RP WITH HOST TDP2/TTRAP.
RX PubMed=14609633; DOI=10.1016/j.virusres.2003.09.001;
RA Lee B.H., Yoshimatsu K., Maeda A., Ochiai K., Morimatsu M., Araki K.,
RA Ogino M., Morikawa S., Arikawa J.;
RT "Association of the nucleocapsid protein of the Seoul and Hantaan
RT hantaviruses with small ubiquitin-like modifier-1-related molecules.";
RL Virus Res. 98:83-91(2003).
RN [5]
RP INTERACTION WITH HOST UBE2I/UBC9, INTERACTION WITH HOST SUMO1, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LYS-189 AND GLU-191.
RX PubMed=12573574; DOI=10.1006/viro.2002.1767;
RA Maeda A., Lee B.H., Yoshimatsu K., Saijo M., Kurane I., Arikawa J.,
RA Morikawa S.;
RT "The intracellular association of the nucleocapsid protein (NP) of hantaan
RT virus (HTNV) with small ubiquitin-like modifier-1 (SUMO-1) conjugating
RT enzyme 9 (Ubc9).";
RL Virology 305:288-297(2003).
RN [6]
RP DOMAIN, RNA-BINDING, AND MUTAGENESIS OF TYR-178; GLU-192; TYR-206 AND
RP SER-217.
RX PubMed=16014963; DOI=10.1128/jvi.79.15.10032-10039.2005;
RA Severson W., Xu X., Kuhn M., Senutovitch N., Thokala M., Ferron F.,
RA Longhi S., Canard B., Jonsson C.B.;
RT "Essential amino acids of the hantaan virus N protein in its interaction
RT with RNA.";
RL J. Virol. 79:10032-10039(2005).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST NF-KAPPA-B.
RX PubMed=20227103; DOI=10.1016/j.virol.2010.02.018;
RA Ontiveros S.J., Li Q., Jonsson C.B.;
RT "Modulation of apoptosis and immune signaling pathways by the Hantaan virus
RT nucleocapsid protein.";
RL Virology 401:165-178(2010).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=24070985; DOI=10.1016/j.virusres.2013.09.022;
RA Shimizu K., Yoshimatsu K., Koma T., Yasuda S.P., Arikawa J.;
RT "Role of nucleocapsid protein of hantaviruses in intracellular traffic of
RT viral glycoproteins.";
RL Virus Res. 178:349-356(2013).
RN [9]
RP FUNCTION, INTERACTION WITH HOST MAP1LC3B, INTERACTION WITH HOST SNAP29, AND
RP DOMAIN.
RX PubMed=31091447; DOI=10.1016/j.celrep.2019.04.061;
RA Wang K., Ma H., Liu H., Ye W., Li Z., Cheng L., Zhang L., Lei Y., Shen L.,
RA Zhang F.;
RT "The Glycoprotein and Nucleocapsid Protein of Hantaviruses Manipulate
RT Autophagy Flux to Restrain Host Innate Immune Responses.";
RL Cell Rep. 27:2075-2091.e5(2019).
RN [10] {ECO:0007744|PDB:5FSG}
RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 113-429, SUBUNIT, RNA-BINDING,
RP AND FUNCTION.
RX PubMed=26923588; DOI=10.1016/j.celrep.2016.02.005;
RA Olal D., Daumke O.;
RT "Structure of the Hantavirus Nucleoprotein Provides Insights into the
RT Mechanism of RNA Encapsidation.";
RL Cell Rep. 14:2092-2099(2016).
RN [11] {ECO:0007744|PDB:6I2N}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS), SUBUNIT, AND FUNCTION.
RX PubMed=30638449; DOI=10.7554/elife.43075;
RA Arragain B., Reguera J., Desfosses A., Gutsche I., Schoehn G., Malet H.;
RT "High resolution cryo-EM structure of the helical RNA-bound Hantaan virus
RT nucleocapsid reveals its assembly mechanisms.";
RL Elife 8:0-0(2019).
CC -!- FUNCTION: Encapsidates the genome protecting it from nucleases
CC (PubMed:26923588). The encapsidated genomic RNA is termed the
CC nucleocapsid (NC) and serves as template for transcription and
CC replication (Probable). The nucleocapsid has a left-handed helical
CC structure (PubMed:30638449). As a trimer, specifically binds and acts
CC as a chaperone to unwind the panhandle structure formed by the viral
CC RNA (vRNA) termini (By similarity). Involved in the transcription and
CC replication initiation of vRNA by mediating primer annealing (By
CC similarity). Plays a role in cap snatching by sequestering capped RNAs
CC in P bodies for use by the viral RdRp during transcription initiation
CC (By similarity). Substitutes for the cellular cap-binding complex
CC (eIF4F) to preferentially facilitate the translation of capped mRNAs
CC (By similarity). Initiates the translation by specifically binding to
CC the cap and 40S ribosomal subunit (By similarity). Prevents the viral
CC glycoprotein N (Gn) from autophagy-dependent breakdown maybe by
CC blocking autophagosome formation (PubMed:31091447). 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). Suppresses apoptosis probably through the
CC inhibition of nuclear import of NF-kappa-B (PubMed:20227103).
CC {ECO:0000250|UniProtKB:O36307, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000269|PubMed:20227103, ECO:0000269|PubMed:26923588,
CC ECO:0000269|PubMed:30638449, ECO:0000269|PubMed:31091447, ECO:0000305}.
CC -!- SUBUNIT: Homotrimer (By similarity). Homomultimer (PubMed:12502810,
CC PubMed:26923588, PubMed:30638449). Homomultimerizes and binds to viral
CC genomic RNA to form the nucleocapsid (PubMed:26923588). Interacts with
CC host MAP1LC3B; this interaction participates to the protection of Gn
CC from virus-triggered autophagy (PubMed:31091447). Interacts with host
CC SNAP29; this interaction participates to the protection of glycoprotein
CC N from virus-triggered autophagy (PubMed:31091447). Interacts (via N-
CC terminus) with host RPS19; this interaction probably mediates the
CC loading of the 40S ribosomal subunit on viral capped mRNA during N-
CC mediated translation initiation (By similarity). Interacts with the
CC viral RdRp (By similarity). Interacts with host SUMO1
CC (PubMed:12573574). Interacts with host DAXX (By similarity). Interacts
CC with the viral glycoprotein N (via C-terminus) (By similarity).
CC Interacts with the viral glycoprotein C (via C-terminus) (By
CC similarity). Interacts with host SUMO1-interacting proteins HIPK2,
CC CHD3, and TDP2/TTRAP (PubMed:14609633). Interacts with host UBE2I/UBC9
CC (PubMed:12573574). Interacts weakly with host NF-kappa-B
CC (PubMed:20227103). {ECO:0000250|UniProtKB:P27313,
CC ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:12502810,
CC ECO:0000269|PubMed:12573574, ECO:0000269|PubMed:14609633,
CC ECO:0000269|PubMed:20227103, ECO:0000269|PubMed:26923588,
CC ECO:0000269|PubMed:30638449, ECO:0000269|PubMed:31091447}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm, host
CC perinuclear region {ECO:0000269|PubMed:12573574}. Host Golgi apparatus,
CC host cis-Golgi network {ECO:0000269|PubMed:24070985}. 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 (By similarity). The YxxL motif is
CC indispensable for the interaction with host MAP1LC3B (PubMed:31091447).
CC The central region is involved in specific RNA-binding
CC (PubMed:11884555, PubMed:16014963). Has distinct cap- and RNA-binding
CC sites so it can bind simultaneously both the vRNA and mRNA cap (By
CC similarity). {ECO:0000250|UniProtKB:Q89462,
CC ECO:0000269|PubMed:11884555, ECO:0000269|PubMed:16014963,
CC ECO:0000269|PubMed:31091447}.
CC -!- SIMILARITY: Belongs to the hantavirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; M14626; AAA43837.1; -; Genomic_RNA.
DR PIR; A25617; VHVUHV.
DR PDB; 4FI5; X-ray; 2.20 A; A=3-93.
DR PDB; 5FSG; X-ray; 3.21 A; A=113-429.
DR PDB; 6I2N; EM; 3.30 A; D=1-429.
DR PDBsum; 4FI5; -.
DR PDBsum; 5FSG; -.
DR PDBsum; 6I2N; -.
DR SMR; P05133; -.
DR Proteomes; UP000008627; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
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; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0019050; P:suppression by virus of host apoptotic process; IDA:UniProtKB.
DR InterPro; IPR002214; Hanta_nucleocap.
DR Pfam; PF00846; Hanta_nucleocap; 1.
DR PIRSF; PIRSF003949; N_HantaV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Chaperone; Coiled coil; Endonuclease;
KW Helical capsid protein; Host cytoplasm; Host Golgi apparatus;
KW Host-virus interaction; Hydrolase;
KW Modulation of host cell apoptosis by virus; Nuclease; Reference proteome;
KW Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..429
FT /note="Nucleoprotein"
FT /id="PRO_0000222009"
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:0000250|UniProtKB:Q88918"
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:0000250|UniProtKB:Q88918"
FT REGION 100..125
FT /note="Homomultimerization"
FT /evidence="ECO:0000269|PubMed:12502810"
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:0000269|PubMed:11884555,
FT ECO:0000269|PubMed:16014963"
FT REGION 188..191
FT /note="Interaction with host UBE2I/UBC9"
FT /evidence="ECO:0000269|PubMed:12573574"
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:0000250|UniProtKB:Q88918"
FT COILED 4..31
FT /evidence="ECO:0000255"
FT MOTIF 178..181
FT /note="YxxL"
FT /evidence="ECO:0000269|PubMed:31091447"
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"
FT MUTAGEN 178
FT /note="Y->A: No effect on RNA binding."
FT /evidence="ECO:0000269|PubMed:16014963"
FT MUTAGEN 189
FT /note="K->A: Decreased interaction with host UBE2I/UBC9 and
FT SUMO1."
FT /evidence="ECO:0000269|PubMed:12573574"
FT MUTAGEN 189
FT /note="K->R: Slightly decreased interaction with host SUMO1
FT and no effect on interaction with host UBE2I/UBC9."
FT /evidence="ECO:0000269|PubMed:12573574"
FT MUTAGEN 191
FT /note="E->A: Slightly decreased interaction with host SUMO1
FT and no effect on interaction with host UBE2I/UBC9."
FT /evidence="ECO:0000269|PubMed:12573574"
FT MUTAGEN 191
FT /note="E->D: No effect on the interaction with host SUMO1
FT and UBE2I/UBC9."
FT /evidence="ECO:0000269|PubMed:12573574"
FT MUTAGEN 192
FT /note="E->A: 84% loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:16014963"
FT MUTAGEN 206
FT /note="Y->A: 78% loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:16014963"
FT MUTAGEN 217
FT /note="S->A: 84% loss of RNA binding."
FT /evidence="ECO:0000269|PubMed:16014963"
FT HELIX 4..34
FT /evidence="ECO:0007829|PDB:4FI5"
FT HELIX 38..70
FT /evidence="ECO:0007829|PDB:4FI5"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:6I2N"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 131..141
FT /evidence="ECO:0007829|PDB:5FSG"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:6I2N"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:5FSG"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:5FSG"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:5FSG"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 226..230
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:5FSG"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 262..276
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:5FSG"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:6I2N"
FT HELIX 325..346
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 351..357
FT /evidence="ECO:0007829|PDB:6I2N"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:5FSG"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:6I2N"
FT HELIX 378..394
FT /evidence="ECO:0007829|PDB:5FSG"
FT HELIX 404..420
FT /evidence="ECO:0007829|PDB:5FSG"
SQ SEQUENCE 429 AA; 48142 MW; DD3B12CB24BC9EC7 CRC64;
MATMEELQRE INAHEGQLVI ARQKVRDAEK QYEKDPDELN KRTLTDREGV AVSIQAKIDE
LKRQLADRIA TGKNLGKEQD PTGVEPGDHL KERSMLSYGN VLDLNHLDID EPTGQTADWL
SIIVYLTSFV VPILLKALYM LTTRGRQTTK DNKGTRIRFK DDSSFEDVNG IRKPKHLYVS
LPNAQSSMKA EEITPGRYRT AVCGLYPAQI KARQMISPVM SVIGFLALAK DWSDRIEQWL
IEPCKLLPDT AAVSLLGGPA TNRDYLRQRQ VALGNMETKE SKAIRQHAEA AGCSMIEDIE
SPSSIWVFAG APDRCPPTCL FIAGIAELGA FFSILQDMRN TIMASKTVGT SEEKLRKKSS
FYQSYLRRTQ SMGIQLGQRI IVLFMVAWGK EAVDNFHLGD DMDPELRTLA QSLIDVKVKE
ISNQEPLKL
