NCAP_INBP9
ID NCAP_INBP9 Reviewed; 560 AA.
AC O36433;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 02-JUN-2021, entry version 74.
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 B virus (strain B/Panama/45/1990).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Insthoviricetes; Articulavirales; Orthomyxoviridae; Betainfluenzavirus.
OX NCBI_TaxID=408929;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9281500; DOI=10.1006/viro.1997.8682;
RA Jambrina E., Barcena J., Uez O., Portela A.;
RT "The three subunits of the polymerase and the nucleoprotein of influenza B
RT virus are the minimum set of viral proteins required for expression of a
RT model RNA template.";
RL Virology 235:209-217(1997).
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; AF005739; AAB72046.1; -; mRNA.
DR SMR; O36433; -.
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..560
FT /note="Nucleoprotein"
FT /id="PRO_0000079143"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 560 AA; 61644 MW; 1F4F44EFBF5C3F2F CRC64;
MSNMDIDGIN TGTIDKTPEE ITSGTSGTTR PIIRPATLAP PSNKRTRNPS PERATTSSEA
DVGRKTQKKQ TPTEIKKSVY NMVVKLGEFY NQMMVKAGLN DDMERNLIQN AHAVERILLA
ATDDKKTEFQ RKKNARDVKE GKEEIDHNKT GGTFYKMVRD DKTIYFSPIR ITFLKEEVKT
MYKTTMGSDG FSGLNHIMIG HSQMNDVCFQ RSKALKRVGL DPSLISTFAG STLPRRSGAT
GVAIKGGGTL VAEAIRFIGR AMADRGLLRD IKAKTAYEKI LLNLKNKCSA PQQKALVDQV
IGSRNPGIAD IEDLTLLARS MVVVRPSVAS KVVLPISIYA KIPQLGFNVE EYSMVGYEAM
ALYNMATPVS ILRMGDDAKD KSQLFFMSCF GAAYEDLRVL SALTGIEFKP RSALKCKGFH
VPAKEQVEGM GAALMSIKLQ FWAPMTRSGG NEVGGDGGSG QISCSPVFAV ERPIALSKQA
VRRMLSMNIE GRDADVKGNL LKMMNDSMAK KTNGNAFIGK KMFQISDKNK TNPVEIPIKQ
TIPNFFFGRD TAEDYDDLDY
