NCAP_I97A1
ID NCAP_I97A1 Reviewed; 498 AA.
AC O92784; O89528; Q9DID1; Q9WA98;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 2.
DT 02-JUN-2021, entry version 87.
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/Hong Kong/156/1997 H5N1 genotype Gs/Gd).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=130763;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9685; Felis catus (Cat) (Felis silvestris catus).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9691; Panthera pardus (Leopard) (Felis pardus).
OH NCBI_TaxID=9694; Panthera tigris (Tiger).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9482438; DOI=10.1016/s0140-6736(97)11212-0;
RA Claas E.C.J., Osterhaus A.D., van Beek R., De Jong J.C., Rimmelzwaan G.F.,
RA Senne D.A., Krauss S., Shortridge K.F., Webster R.G.;
RT "Human influenza A H5N1 virus related to a highly pathogenic avian
RT influenza virus.";
RL Lancet 351:472-477(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9430591; DOI=10.1126/science.279.5349.393;
RA Subbarao K., Klimov A., Katz J., Regnery H., Lim W., Hall H., Perdue M.,
RA Swayne D., Bender C., Huang J., Hemphill M., Rowe T., Shaw M., Xu X.,
RA Fukuda K., Cox N.;
RT "Characterization of an avian influenza A (H5N1) virus isolated from a
RT child with a fatal respiratory illness.";
RL Science 279:393-396(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=9658115; DOI=10.1128/jvi.72.8.6678-6688.1998;
RA Suarez D.L., Perdue M.L., Cox N., Rowe T., Bender C., Huang J.,
RA Swayne D.E.;
RT "Comparisons of highly virulent H5N1 influenza A viruses isolated from
RT humans and chickens from Hong Kong.";
RL J. Virol. 72:6678-6688(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=11112478; DOI=10.1006/viro.2000.0585;
RA Cameron K.R., Gregory V., Banks J., Brown I.H., Alexander D.J., Hay A.J.,
RA Lin Y.P.;
RT "H9N2 subtype influenza A viruses in poultry in pakistan are closely
RT related to the H9N2 viruses responsible for human infection in Hong Kong.";
RL Virology 278:36-41(2000).
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}.
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 -!- SIMILARITY: Belongs to the influenza viruses nucleoprotein family.
CC {ECO:0000255|HAMAP-Rule:MF_04070}.
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DR EMBL; AF028710; AAC40509.1; -; mRNA.
DR EMBL; AF036359; AAC34267.1; -; Genomic_RNA.
DR EMBL; AF046092; AAC32094.1; -; Genomic_RNA.
DR EMBL; AJ291400; CAC19704.1; -; Genomic_RNA.
DR SMR; O92784; -.
DR PRO; PR:O92784; -.
DR Proteomes; UP000008587; Genome.
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: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 2: Evidence at transcript level;
KW 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_0000079066"
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 CONFLICT 205
FT /note="N -> K (in Ref. 1; AAC40509)"
FT CONFLICT 236
FT /note="K -> R (in Ref. 4; CAC19704)"
FT CONFLICT 283
FT /note="P -> L (in Ref. 1, 3 and 4)"
FT CONFLICT 321
FT /note="N -> D (in Ref. 1; AAC40509)"
FT CONFLICT 322
FT /note="P -> S (in Ref. 3; AAC32094)"
FT CONFLICT 330
FT /note="W -> R (in Ref. 1; AAC40509)"
FT CONFLICT 377
FT /note="T -> S (in Ref. 1, 3 and 4)"
FT CONFLICT 402
FT /note="S -> F (in Ref. 1; AAC40509)"
FT CONFLICT 411
FT /note="T -> N (in Ref. 1; AAC40509)"
FT CONFLICT 418
FT /note="L -> F (in Ref. 1; AAC40509)"
FT CONFLICT 437
FT /note="T -> R (in Ref. 1; AAC40509)"
SQ SEQUENCE 498 AA; 56268 MW; 0D46EEDBC3C6C4D6 CRC64;
MASQGTKRSY EQMETGGERQ NATEIRASVG RMVGGIGRFY IQMCTELKLS DQEGRLIQNS
ITIERMVLSA FDERRNRYLE EHPSAGKDPK KTGGPIYRRR DGKWVRELIL YDKEEIRRIW
RQANNGEDAT AGLTHMMIWH SNLNDATYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
AAIKGVGTMV MELIRMIKRG INDRNFWRGE NGRRTRIAYE RMCNILKGKF QTAAQKAMMD
QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEREGYSLVG
IDPFRLLQNS QVFSLIRPKE NPAHKSQLVW MACHSAAFED LRVSSFIRGT RVIPRGQLST
RGVQIASNEN VEAMDSTTLE LRSRYWAIRT RSGGNTNQQR ASAGQISVQP TFSVQRNLPF
ERVTIMAAFK GNTEGRTSDM RTEIIRMMES ARPEDVSFQG RGVFELSDEK ATNPIVPSFD
MSNEGSYFFG DNAEEYDN
