NCAP_PUUMK
ID NCAP_PUUMK Reviewed; 433 AA.
AC P41269;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 66.
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 Puumala virus (strain K27).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=39000;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=8266723; DOI=10.1016/0168-1702(93)90019-j;
RA Xiao S.Y., Spik K.W., Li D., Schmaljohn C.S.;
RT "Nucleotide and deduced amino acid sequences of the M and S genome segments
RT of two Puumala virus isolates from Russia.";
RL Virus Res. 30:97-103(1993).
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). {ECO:0000250|UniProtKB:O36307,
CC ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000305}.
CC -!- SUBUNIT: Homotrimer (By similarity). Homomultimer (By similarity).
CC Homomultimerizes and binds to viral genomic RNA to form the
CC nucleocapsid (By similarity). Interacts with host MAP1LC3B; this
CC interaction participates to the protection of Gn from virus-triggered
CC autophagy (By similarity). Interacts with host SNAP29; this interaction
CC participates to the protection of glycoprotein N from virus-triggered
CC autophagy (By similarity). Interacts (via N-terminus) with host RPS19;
CC this interaction probably mediates the loading of the 40S ribosomal
CC subunit on viral capped mRNA during N-mediated translation initiation
CC (By similarity). Interacts with the viral RdRp (By similarity).
CC Interacts with host SUMO1 (via N-terminus) (By similarity). Interacts
CC with host DAXX (By similarity). Interacts with the viral glycoprotein N
CC (via C-terminus) (By similarity). Interacts with the viral glycoprotein
CC C (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P05133,
CC ECO:0000250|UniProtKB:P27313, ECO:0000250|UniProtKB:Q88918,
CC ECO:0000250|UniProtKB:Q89462}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P05133}. Host
CC cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host
CC Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}.
CC Note=Internal protein of virus particle.
CC {ECO:0000250|UniProtKB:P05133}.
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 (By similarity).
CC The central region is involved in specific RNA-binding (By similarity).
CC Has distinct cap- and RNA-binding sites so it can bind simultaneously
CC both the vRNA and mRNA cap (By similarity).
CC {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462}.
CC -!- SIMILARITY: Belongs to the hantavirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; L08804; AAC37849.1; -; Genomic_RNA.
DR SMR; P41269; -.
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; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR InterPro; IPR002214; Hanta_nucleocap.
DR Pfam; PF00846; Hanta_nucleocap; 1.
DR PIRSF; PIRSF003949; N_HantaV; 1.
PE 3: Inferred from homology;
KW Capsid protein; Chaperone; Coiled coil; Endonuclease;
KW Helical capsid protein; Host cytoplasm; Host Golgi apparatus; Hydrolase;
KW Nuclease; Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT CHAIN 1..433
FT /note="Nucleoprotein"
FT /id="PRO_0000222014"
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 69..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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: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 377..433
FT /note="Interaction with host DAXX"
FT /evidence="ECO:0000250|UniProtKB:P27313"
FT REGION 377..425
FT /note="Homomultimerization"
FT /evidence="ECO:0000250|UniProtKB:Q88918"
FT COILED 4..71
FT /evidence="ECO:0000255"
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 433 AA; 49528 MW; CDFC65CE298EFAC1 CRC64;
MSDLTDIQEE ITRHEQQLVV ARQKLKDAER AVEVYPDDVI KNTLQARQQT VSALEDKLAD
YKRRMADAVS RKKMDTKPTD PTGIEPDDHL KERSSLRYGN VLDVNAIDIE EPSGQTADWY
TIGVYVIGFT IPIILKALYM LSTRGRQTVK ENKGTRIRFK DDTSFEDING IRRPKHLYVS
MPTAQSTMKA EELTPGRFRT IVCGLFPTQI QVRNIMSPVM GVIGFSFFVK DWPEKIREFM
EKECPFIKPE VKPGTPAQEV EFLKRNRVYF MTRQDVLDKN HVADIDKLID YAASGDPTSP
DDIKSPNAPW VFACAPDRSP PTCIYVAGMA ELGAFFSILQ DMRNTIMASK TVGTAEEKLK
RKSSFYQSYL RRTQSMGIQL DQRIILLYML EWGKEMVDHF HLGDDMDPEL RGLAQSLIDQ
KVKEISNQEP LKI
