ID   NCAP_PI2HT              Reviewed;         542 AA.
AC   P21737;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   02-JUN-2021, entry version 95.
DE   RecName: Full=Nucleoprotein;
DE   AltName: Full=Nucleocapsid protein;
DE            Short=NP;
DE            Short=Protein N;
GN   Name=N; Synonyms=NP;
OS   Human parainfluenza 2 virus (strain Toshiba) (HPIV-2).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Haploviricotina;
OC   Monjiviricetes; Mononegavirales; Paramyxoviridae; Rubulavirinae;
OC   Orthorubulavirus; Human parainfluenza 2 virus.
OX   NCBI_TaxID=11214;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2173261; DOI=10.1016/0042-6822(90)90145-h;
RA   Yuasa T., Bando H., Kawano M., Tsurudome M., Nishio M., Kondo K.,
RA   Komada H., Ito Y.;
RT   "Sequence analyses of the 3' genome end and NP gene of human parainfluenza
RT   type 2 virus: sequence variation of the gene-starting signal and the
RT   conserved 3' end.";
RL   Virology 179:777-784(1990).
RN   [2]
RP   INTERACTION WITH P PROTEIN.
RX   PubMed=8887478; DOI=10.1099/0022-1317-77-10-2457;
RA   Nishio M., Tsurudome M., Kawano M., Watanabe N., Ohgimoto S., Ito M.,
RA   Komada H., Ito Y.;
RT   "Interaction between nucleocapsid protein (NP) and phosphoprotein (P) of
RT   human parainfluenza virus type 2: one of the two NP binding sites on P is
RT   essential for granule formation.";
RL   J. Gen. Virol. 77:2457-2463(1996).
RN   [3]
RP   HOMOMULTIMERIZATION.
RX   PubMed=10466799; DOI=10.1099/0022-1317-80-8-2017;
RA   Nishio M., Tsurudome M., Ito M., Kawano M., Kusagawa S., Komada H., Ito Y.;
RT   "Mapping of domains on the human parainfluenza virus type 2 nucleocapsid
RT   protein (NP) required for NP-phosphoprotein or NP-NP interaction.";
RL   J. Gen. Virol. 80:2017-2022(1999).
CC   -!- FUNCTION: Encapsidates the genome, protecting it from nucleases. The
CC       nucleocapsid (NC) has a helical structure. The encapsidated genomic RNA
CC       is termed the NC and serves as template for transcription and
CC       replication. During replication, encapsidation by N is coupled to RNA
CC       synthesis and all replicative products are resistant to nucleases (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homomultimerizes to form the nucleocapsid. Binds to viral
CC       genomic RNA. In nucleocapsid, binds the P protein and thereby positions
CC       the polymerase on the template.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm.
CC   -!- DOMAIN: Ncore is globular and carries regions required for N self-
CC       assembly and RNA-binding. Ntail is an intrinsically disordered
CC       monomeric domain (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the paramyxoviruses nucleocapsid family.
CC       {ECO:0000305}.
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DR   EMBL; M55320; AAA46865.1; -; mRNA.
DR   EMBL; X57559; CAA40783.1; -; Genomic_RNA.
DR   PIR; A36420; VHNZP2.
DR   SMR; P21737; -.
DR   Proteomes; UP000000472; Genome.
DR   GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR002021; Paramyx_ncap.
DR   Pfam; PF00973; Paramyxo_ncap; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Helical capsid protein; Host cytoplasm; Reference proteome;
KW   Ribonucleoprotein; RNA-binding; Viral nucleoprotein; Virion.
FT   CHAIN           1..542
FT                   /note="Nucleoprotein"
FT                   /id="PRO_0000142670"
FT   REGION          1..400
FT                   /note="Ncore"
FT                   /evidence="ECO:0000250"
FT   REGION          1..294
FT                   /note="Homomultimerization"
FT   REGION          295..402
FT                   /note="P protein-binding 1"
FT   REGION          401..542
FT                   /note="Ntail"
FT                   /evidence="ECO:0000250"
FT   REGION          402..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..494
FT                   /note="P protein-binding 2"
FT   COMPBIAS        443..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   542 AA;  61121 MW;  AB9F6636497045FF CRC64;
     MSSVLKTFER FTIQQELQEQ SDDTPVPLET IKPTIRVFVI NNNDPVVRSR LLFFNLRIIM
     SNTAREGHRA GALLSLLSLP SAAMSNHIKL AMHSPEASID RVEITGFENN SFRVIPDARS
     TMSRGEVLAF EALAEDIPDT LNHQTPFVNN DVEDDIFDET EKFLDVCYSV LMQAWIVTCK
     CMTAPDQPPV SVAKMAKYQQ QGRINARYVL QPEAQRLIQN AIRKSMVVRH FMTYELQLSQ
     SRSLLANRYY AMVGDIGKYI EHSGMGGFFL TLKYGLGTRW PTLALAAFSG ELQKLKALML
     HYQSLGPMAK YMALLESPKL MDFVPSEYPL DYSYAMGIGT VLDTNMRNYA YGRSYLNQQY
     FQLGVETARK QQGAVDNRTA EDLGMTAADK ADLTATISKL SLSQLPRGRQ PISDPFAGAN
     DREMGGQAND TPVYNFNPID TRRYDNYDSD GEDRIDNDQD QAIRENRGEP GQPNNQTSDN
     QQRFNPPIPQ RTSGMSSEEF QHSMNQYIRA MHEQYRGSQD DDANDATDGN DISLELVGDF
     DS