NCAP_I33A0
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 02-JUN-2021, entry version 98.
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.
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}.
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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 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: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.
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
