NCAP_PUUMS
ID NCAP_PUUMS Reviewed; 433 AA.
AC P27313; I4EPA2;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Sotkamo/V-2969/81).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=39002;
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=1353107; DOI=10.1099/0022-1317-73-4-829;
RA Vapalahti O.P., Kallio-Kokko H., Salonen E.M., Brummer-Korvenkontio M.,
RA Vaheri A.;
RT "Cloning and sequencing of Puumala virus Sotkamo strain S and M RNA
RT segments: evidence for strain variation in hantaviruses and expression of
RT the nucleocapsid protein.";
RL J. Gen. Virol. 73:829-838(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Isolate Sotkamo 2009/WHO Arbovirus collection;
RX PubMed=22798055; DOI=10.1007/s11262-012-0780-3;
RA Kurolt I.C., Paessler S., Markotic A.;
RT "Resequencing of the Puumala virus strain Sotkamo from the WHO Arbovirus
RT collection.";
RL Virus Genes 45:389-392(2012).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=11160679; DOI=10.1128/jvi.75.4.1808-1815.2001;
RA Ravkov E.V., Compans R.W.;
RT "Hantavirus nucleocapsid protein is expressed as a membrane-associated
RT protein in the perinuclear region.";
RL J. Virol. 75:1808-1815(2001).
RN [4]
RP INTERACTION WITH HOST DAXX.
RX PubMed=11907324; DOI=10.1099/0022-1317-83-4-759;
RA Li X.D., Maekelae T.P., Guo D., Soliymani R., Koistinen V., Vapalahti O.,
RA Vaheri A., Lankinen H.;
RT "Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis
RT enhancer Daxx.";
RL J. Gen. Virol. 83:759-766(2002).
RN [5]
RP INTERACTION WITH THE GLYCOPROTEIN N, AND INTERACTION WITH THE GLYCOPROTEIN
RP C.
RX PubMed=20444994; DOI=10.1099/vir.0.021006-0;
RA Hepojoki J., Strandin T., Wang H., Vapalahti O., Vaheri A., Lankinen H.;
RT "Cytoplasmic tails of hantavirus glycoproteins interact with the
RT nucleocapsid protein.";
RL J. Gen. Virol. 91:2341-2350(2010).
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 (PubMed:11907324). Interacts (via C-terminus) with the
CC viral glycoprotein N (PubMed:20444994). Interacts (via C-terminus) with
CC the viral glycoprotein C (PubMed:20444994).
CC {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q88918,
CC ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:11907324,
CC ECO:0000269|PubMed:20444994}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P05133}. Host
CC cytoplasm, host perinuclear region {ECO:0000269|PubMed:11160679}. 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}.
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; X61035; CAA43370.1; -; Genomic_RNA.
DR EMBL; HE801633; CCH22846.1; -; Genomic_RNA.
DR PIR; JQ1605; JQ1605.
DR RefSeq; NP_941984.1; NC_005224.1.
DR SMR; P27313; -.
DR GeneID; 2943083; -.
DR KEGG; vg:2943083; -.
DR Proteomes; UP000008482; Genome.
DR Proteomes; UP000110237; 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; 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 1: Evidence at protein level;
KW Capsid protein; Chaperone; Coiled coil; Endonuclease;
KW Helical capsid protein; Host cytoplasm; Host Golgi apparatus; Hydrolase;
KW Nuclease; Reference proteome; Ribonucleoprotein; RNA-binding;
KW Viral nucleoprotein; Virion.
FT CHAIN 1..433
FT /note="Nucleoprotein"
FT /id="PRO_0000222016"
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 67..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:0000269|PubMed:11907324"
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; 49452 MW; 27D98B3F65BA026E CRC64;
MSDLTDIQED ITRHEQQLIV ARQKLKDAER AVEVDPDDVN KNTLQARQQT VSALEDKLAD
YKRRMADAVS RKKMDTKPTD PTGIEPDDHL KERSSLRYGN VLDVNAIDIE EPSGQTADWY
TIGVYVIGFT LPIILKALYM LSTRGRQTVK ENKGTRIRFK DDTSFEDING IRRPKHLYVS
MPTAQSTMKA EELTPGRFRT IVCGLFPTQI QVRNIMSPVM GVIGFSFFVK DWSERIREFM
EKECPFIKPE VKPGTPAQEI EMLKRNKIYF MQRQDVLDKN HVADIDKLID YAASGDPTSP
DNIDSPNAPW VFACAPDRCP PTCIYVAGMA ELGAFFSILQ DMRNTIMASK TVGTAEEKLK
KKSSFYQSYL RRTQSMGIQL DQRIILLFML EWGKEMVDHF HLGDDMDPEL RGLAQALIDQ
KVKEISNQEP LKI
