ID   NCAP_PUUMP              Reviewed;         433 AA.
AC   P41270;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-NOV-2023, entry version 68.
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 P360).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC   Orthohantavirus; Orthohantavirus puumalaense.
OX   NCBI_TaxID=39001;
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; L11347; AAC37850.1; -; Genomic_RNA.
DR   SMR; P41270; -.
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:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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   Gene3D; 1.20.58.90; -; 1.
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_0000222015"
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..90
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;  49518 MW;  E5E928C93B8FE767 CRC64;
     MSDLTDIQEE ITRHEQQLVV ARQKLKDAER AVEVYPDDVN 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
     DDIESPNAPW VFACAPDRCP PTCIYVAGMA ELGAFFSILQ DMRNTIMASK TVGTAEEKLK
     KKSSFYQSYL RRTQSMGIQL DQRIILLYML EWGKEMVDHF HLGDDMDPEL RGLAQSLIDQ
     KVKEISNQEP LKI
//