ID NCAP_I33A0 Reviewed; 498 AA. AC P15682; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 24-JAN-2024, entry version 102. DE RecName: Full=Nucleoprotein {ECO:0000255|HAMAP-Rule:MF_04070}; DE AltName: Full=Nucleocapsid protein {ECO:0000255|HAMAP-Rule:MF_04070}; DE Short=Protein N {ECO:0000255|HAMAP-Rule:MF_04070}; GN Name=NP {ECO:0000255|HAMAP-Rule:MF_04070}; OS Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus OS (strain A/WS/1933 H1N1)). OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina; OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus; OC Alphainfluenzavirus influenzae; Influenza A virus. OX NCBI_TaxID=381518; OH NCBI_TaxID=8782; Aves. OH NCBI_TaxID=9606; Homo sapiens (Human). OH NCBI_TaxID=9823; Sus scrofa (Pig). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC RNA]. RX PubMed=2319644; DOI=10.1128/jvi.64.4.1487-1497.1990; RA Gorman O.T., Bean W.J., Kawaoka Y., Webster R.G.; RT "Evolution of the nucleoprotein gene of influenza A virus."; RL J. Virol. 64:1487-1497(1990). RN [2] RP CLEAVAGE. RX PubMed=10559331; DOI=10.1128/jvi.73.12.10158-10163.1999; RA Zhirnov O.P., Konakova T.E., Garten W., Klenk H.; RT "Caspase-dependent N-terminal cleavage of influenza virus nucleocapsid RT protein in infected cells."; RL J. Virol. 73:10158-10163(1999). RN [3] RP FUNCTION. RX PubMed=15702989; DOI=10.1111/j.1600-0854.2005.00263.x; RA Cros J.F., Garcia-Sastre A., Palese P.; RT "An unconventional NLS is critical for the nuclear import of the influenza RT A virus nucleoprotein and ribonucleoprotein."; RL Traffic 6:205-213(2005). CC -!- FUNCTION: Encapsidates the negative strand viral RNA, protecting it CC from nucleases. The encapsidated genomic RNA is termed the CC ribonucleoprotein (RNP) and serves as template for transcription and CC replication. The RNP needs to be localized in the host nucleus to start CC an infectious cycle, but is too large to diffuse through the nuclear CC pore complex. NP comprises at least 2 nuclear localization signals that CC are responsible for the active RNP import into the nucleus through CC cellular importin alpha/beta pathway. Later in the infection, nclear CC export of RNPs are mediated through viral proteins NEP interacting with CC M1 which binds nucleoproteins. It is possible that nucleoprotein binds CC directly host exportin-1/XPO1 and plays an active role in RNPs nuclear CC export. M1 interaction with RNP seems to hide nucleoprotein's nuclear CC localization signals. Soon after a virion infects a new cell, M1 CC dissociates from the RNP under acidification of the virion driven by M2 CC protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear CC localization signals, targeting the RNP to the nucleus. CC {ECO:0000255|HAMAP-Rule:MF_04070, ECO:0000269|PubMed:15702989}. CC -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. May bind host CC exportin-1/XPO1. Binds to viral genomic RNA. Protein-RNA contacts are CC mediated by a combination of electrostatic interactions between CC positively charged residues and the phosphate backbone and planar CC interactions between aromatic side chains and bases. CC {ECO:0000255|HAMAP-Rule:MF_04070}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04070}. Host CC nucleus {ECO:0000255|HAMAP-Rule:MF_04070}. CC -!- PTM: Late in virus-infected cells, may be cleaved from a 56-kDa protein CC to a 53-kDa protein by a cellular caspase. This cleavage might be a CC marker for the onset of apoptosis in infected cells or have a specific CC function in virus host interaction. {ECO:0000255|HAMAP-Rule:MF_04070, CC ECO:0000269|PubMed:10559331}. CC -!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family. CC {ECO:0000255|HAMAP-Rule:MF_04070}. 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; M30746; AAA43452.1; -; Genomic_RNA. DR PDB; 3ZDP; X-ray; 2.69 A; A/B/C=1-498. DR PDB; 4BBL; EM; 18.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=8-498. DR PDB; 4IRY; X-ray; 2.80 A; A/B=1-401, A/B=430-498. DR PDB; 5B7B; X-ray; 3.00 A; A/B/C/D/E/F=1-498. DR PDB; 6I7B; EM; 10.00 A; B/D=402-420. DR PDB; 6I85; EM; 24.00 A; B/D=402-428. DR PDB; 6J1U; X-ray; 2.80 A; A/B/C=1-498. DR PDBsum; 3ZDP; -. DR PDBsum; 4BBL; -. DR PDBsum; 4IRY; -. DR PDBsum; 5B7B; -. DR PDBsum; 6I7B; -. DR PDBsum; 6I85; -. DR PDBsum; 6J1U; -. DR EMDB; EMD-0175; -. DR EMDB; EMD-2205; -. DR EMDB; EMD-4412; -. DR EMDB; EMD-4423; -. DR EMDB; EMD-4430; -. DR SMR; P15682; -. DR IntAct; P15682; 1. DR BindingDB; P15682; -. DR ChEMBL; CHEMBL3706556; -. DR PRO; PR:P15682; -. DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule. DR GO; GO:0039689; P:negative stranded viral RNA replication; IDA:UniProtKB. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule. DR HAMAP; MF_04070; INFV_NCAP; 1. DR InterPro; IPR002141; Flu_NP. DR Pfam; PF00506; Flu_NP; 1. DR SUPFAM; SSF161003; flu NP-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Capsid protein; Helical capsid protein; Host nucleus; KW Host-virus interaction; Ribonucleoprotein; RNA-binding; KW Viral nucleoprotein; Viral penetration into host nucleus; Virion; KW Virus entry into host cell. FT CHAIN 1..498 FT /note="Nucleoprotein" FT /id="PRO_0000079113" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 1..18 FT /note="Unconventional nuclear localization signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04070" FT MOTIF 198..216 FT /note="Bipartite nuclear localization signal" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04070" FT HELIX 22..47 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 51..54 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 57..72 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 103..108 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 113..123 FT /evidence="ECO:0007829|PDB:3ZDP" FT TURN 124..126 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 130..147 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 151..155 FT /evidence="ECO:0007829|PDB:3ZDP" FT TURN 156..158 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 161..166 FT /evidence="ECO:0007829|PDB:3ZDP" FT TURN 168..171 FT /evidence="ECO:0007829|PDB:3ZDP" FT TURN 178..180 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 186..199 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 200..202 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 211..229 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 233..243 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 250..263 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 278..286 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 291..294 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 301..309 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 313..316 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 322..333 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 341..348 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 355..357 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:5B7B" FT STRAND 375..378 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 384..390 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 422..428 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:3ZDP" FT HELIX 439..449 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 456..458 FT /evidence="ECO:0007829|PDB:6J1U" FT STRAND 460..465 FT /evidence="ECO:0007829|PDB:3ZDP" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:6J1U" FT TURN 487..490 FT /evidence="ECO:0007829|PDB:3ZDP" SQ SEQUENCE 498 AA; 56244 MW; 27AA1703050AA877 CRC64; MATKGTKRSY EQMETDGERQ NATEIRASVG KMIGGIGRFY IQMCTELKLS DYEGRLIQNS LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYRRV DGKWMRELIL YDKEEIRRIW RQANNGDDAT AGLTHMMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQRAMVD QVRESRNPGN AEFEDLIFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG IDPFRLLQNS QVYSLIRPNE NPAHKSQLVW MACHSAAFED LRVSSFIRGT KVVPRGKLST RGVQIASNEN METMESSTLE LRSRYWAIRT RSGGNTNQQR ASSGQISIQP TFSVQRNLPF DRPTIMAAFT GNTEGRTSDM RTEIIRLMES ARPEDVSFQG RGVFELSDEK AASPIVPSFD MSNEGSYFFG DNAEEYDN //