NCAP_I68A6
ID NCAP_I68A6 Reviewed; 498 AA.
AC P03467;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, 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/Northern Territory/60/1968 H3N2) (Influenza A
OS virus (strain NT60)) (Influenza A virus (strain A/NT/60/1968 H3N2)).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Alphainfluenzavirus.
OX NCBI_TaxID=384505;
OH NCBI_TaxID=8782; Aves.
OH NCBI_TaxID=9721; Cetacea (whales).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9709; Phocidae (true seals).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6278431; DOI=10.1093/nar/10.3.1029;
RA Huddleston J.A., Brownlee G.G.;
RT "The sequence of the nucleoprotein gene of human influenza A virus, strain
RT A/NT/60/68.";
RL Nucleic Acids Res. 10:1029-1038(1982).
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).
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 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; J02137; AAA43465.1; -; Genomic_RNA.
DR PIR; A04078; VHIV68.
DR PDB; 7NT8; X-ray; 2.22 A; A/B=1-498.
DR PDBsum; 7NT8; -.
DR SMR; P03467; -.
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 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_0000079089"
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 SITE 16..17
FT /note="Cleavage; by host caspase"
SQ SEQUENCE 498 AA; 55954 MW; 72D640C1976A94F0 CRC64;
MASQGTKRSY EQMETDGERQ NATEIRASVG KMIDGIGRFY IQMCTELKLS DYEGRLIQNS
LTIERMVLSA FDERRNKYLE EHPSAGKDPK KTGGPIYKRV DGKWMRELVL YDKGEIRRIW
RQANNGDDAT AGLTHMMIWH SNLNDTTYQR TRALVRTGMD PRMCSLMQGS TLPRRSGAAG
AAVKGVGTMV MELIRMIKRG INDRNFWRGE NGRKTRSAYE RMCNILKGKF QTAAQRAMMD
QVRESRNPGN AEIEDLIFLA RSALILRGSV AHKSCLPACV YGPAVASGYD FEKEGYSLVG
IDPFKLLQNS QVYSLIRPNE NPAHKSQLVW MACNSAAFED LRVLSFIRGT KVSPRGKLST
RGVQIASNEN MDAMESSTLE LRSRYWAIRT RSGGNTNQQR ASAGQISVQP AFSVQRNLPF
DKPTIMAAFT GNTEGRTSDM RAEIIRMMEG AKPEEMSFQG RGVFELSDEK AANPIVPSFD
MSNEGSYFFG DNAEEYDN
